DMD

Summary: Dystrophin products support cell–matrix adhesion in experimental contexts.

Reason: The literal mouse Dmd donor is grounded by PMID:12370193, whose human platelet observations and mouse adhesion experiments implicate short dystrophin-associated complexes. This supports a contextual adhesion contribution, without assigning an integrin receptor activity or transferring a measured activity to every human product. It is retained as non-core alongside the better established membrane–cytoskeleton linkage.

Summary: Dystrophin deficiency alters cardiac rhythm control in mice.

Reason: The mouse donor is PMID:20080623. Its mdx recordings show reduced heart-rate variability and increased susceptibility to ventricular tachycardia, although basal heart rate and RR interval were not significantly altered. Retain the contextual regulatory assertion with that distinction; the experiments do not make dystrophin a pacemaker channel or establish a separate heart-rate molecular activity.

Summary: The precise heart-rate assertion is unresolved from the accessible clinical report.

Reason: PMID:19027585 reports frequent ECG abnormalities in young patients with DMD mutations, including deep Q waves and reduced voltage measures. The complete Methods and results were not recovered, and the abstract does not specify the evidence for control of contraction frequency. Preserve the positive clinical evidence and curator assertion, but leave this source-specific heart-rate claim unresolved rather than treating the incomplete abstract as evidence of error.

Summary: Dystrophin binds the cytoplasmic tail of beta-dystroglycan.

Reason: PMID:7592992 directly tests recombinant human dystrophin fragments against a rabbit beta-dystroglycan tail translated in vitro. Human DMD residues 3054–3271 bind less strongly than a longer 3054–3446 fragment; the distal 3435–3685 fragment is negative. Retain the biologically established dystroglycan-binding activity while preserving the imported partner identity: this paper does not separately measure a full-length human DAG1 counterpart. The later human-mapped peptide complex in PMID:10932245 corroborates the contact in its fragment context.

Summary: Dystrophin binds the cytoplasmic tail of beta-dystroglycan.

Reason: PMID:7592992 directly tests recombinant human dystrophin fragments against a rabbit beta-dystroglycan tail translated in vitro. Human DMD residues 3054–3271 bind less strongly than a longer 3054–3446 fragment; the distal 3435–3685 fragment is negative. Retain the biologically established dystroglycan-binding activity while preserving the imported partner identity: this paper does not separately measure a full-length human DAG1 counterpart. The later human-mapped peptide complex in PMID:10932245 corroborates the contact in its fragment context.

Summary: Actin binding is an established activity of long dystrophin products.

Reason: PMID:16803572 reports platelet dystrophin-complex association with the actin network but is abstract-only after bounded original-access attempts. Independent human dystrophin N-terminal assays in PMID:16000376 and the native-complex evidence support actin binding at gene level. Retain the curator assertion, while not claiming that its short platelet products use the long product’s N-terminal actin-binding domain or that a purified direct assay was recovered from this particular paper.

Summary: The electronic actin-binding assignment agrees with direct functional evidence.

Reason: The current ARBA00028548 condition branch matches the target’s official FunFam classifications and hominid lineage, and the rat donor has an experimental actin-binding record from PMID:10984432. These are provenance checks rather than independent assays. Direct human N-terminal work in PMID:16000376 supports the conserved actin-binding activity, restricted to products and constructs that retain the tested regions.

Summary: Actin binding is supported independently of the broad review citation.

Reason: The cached PMID:12376554 abstract foregrounds plakin and spectraplakin comparisons, so its complete dystrophin discussion was not independently verified. This is not evidence of a miscitation: human dystrophin actin-binding constructs were directly assessed in PMID:16000376. Retain the correct gene-level activity with the reference-access distinction and without assigning it to all short products.

Summary: Dystrophin association with an integrin adhesion complex is supported, but integrin binding itself remains unresolved.

Reason: The rat donor points to PMID:18677563. Its accessible abstract describes Dp71f association with the beta1-integrin complex and direct analysis of GSK3-beta recruitment, rather than resolving a Dp71–integrin interface. The full original was not recovered. Preserve the association and curator evidence, but do not equate binding to the complex with verified recognition of integrin itself or assert that the interaction is false.

Summary: Long dystrophin provides a cytoskeleton-to-membrane anchor.

Reason: PMID:3282674 establishes the architecture of human dystrophin as a large cytoskeletal protein. Targeted binding and native-complex evidence establish its more informative structural role: connecting the intracellular filament network to membrane-associated dystroglycan complexes. Replace the broad structural-constituent term with cytoskeletal protein–membrane anchor activity, without assigning this complete long-product mechanism to every natural short product.

Proposed replacements: cytoskeletal protein-membrane anchor activity

Summary: Dystrophin binds the syntrophin scaffold SNTG1.

Reason: PMID:10747910 explicitly reports yeast two-hybrid and pull-down binding of human gamma syntrophins to the dystrophin C-terminal domain. The curated syntrophin family/function classification identifies a multipartner adapter that organizes membrane-associated signaling proteins, supporting scaffold protein binding. This is a partner-class refinement of the measured binding, not evidence that DMD itself catalyzes signaling or that every natural dystrophin product binds SNTG1. The current interaction query did not recover this old pair, so the positive original abstract and curator assertion remain the source-specific basis; the full original was not independently inspected.

Proposed replacements: scaffold protein binding

Summary: Dystrophin binds the syntrophin scaffold SNTG2.

Reason: PMID:10747910 explicitly reports yeast two-hybrid and pull-down binding of human gamma syntrophins to the dystrophin C-terminal domain. The curated syntrophin family/function classification identifies a multipartner adapter that organizes membrane-associated signaling proteins, supporting scaffold protein binding. This is a partner-class refinement of the measured binding, not evidence that DMD itself catalyzes signaling or that every natural dystrophin product binds SNTG2. The current interaction query did not recover this old pair, so the positive original abstract and curator assertion remain the source-specific basis; the full original was not independently inspected.

Proposed replacements: scaffold protein binding

Summary: Dystrophin binds alpha-dystrobrevin through its C-terminal region.

Reason: The source-specific MINT record reports an in vitro filter-binding interaction between human dystrophin residues 3464–3605 and alpha-dystrobrevin residues 372–505. This positive pair is retained despite the abstract emphasizing utrophin. The available source does not justify assigning a particular signaling activity or recognition of a named domain to DMD. Retain the supported generic interaction as non-core under the scoped project instruction; the full original was not independently inspected.

Summary: The human dystrophin N-terminal domain binds keratin 19 and associates specifically with K8/K19 intermediate filaments.

Reason: PMID:16000376 tests human dystrophin residues 1–246. Figures 1–3 show specific association with assembled K8/K19 filaments in COS7 cells, retained after microfilament or microtubule disruption; Figure 6 demonstrates direct binding to purified K19 subunits. Together these support intermediate filament binding, rather than partner class alone. The fragment did not simultaneously colocalize with actin and keratin filaments; these experiments do not establish the same activity for every shorter dystrophin product.

Proposed replacements: intermediate filament binding

Summary: Dystrophin binds the intermediate-filament protein synemin.

Reason: The complete PMID:16777071 abstract explicitly reports direct binding of human alpha- and beta-synemin domains to dystrophin; avian synemin experiments are a separate part of that study. Synemin is an intermediate-filament cytoskeletal protein, supporting this partner-class refinement. The full original and all construct endpoints were not recovered, so no additional interface or isoform-wide claim is made. GO:0019215 requires binding to an assembled intermediate filament. The accessible text establishes human domain binding and cellular colocalization, but does not resolve that filament-level claim. Retain GO:0008092 without assuming either a missing full-text experiment or its absence.

Proposed replacements: cytoskeletal protein binding

Summary: Dystrophin associates with the alpha-syntrophin-containing DAPC.

Reason: PMID:18468998 and its literal IntAct pair place dystrophin in a HEK293 tandem-affinity-purified alpha-syntrophin complex. The original receptor-function experiments and mapped adapter interfaces do not isolate a binary DMD–SNTA1 contact in this particular assay. Preserve the positive complex association as non-core under the project instruction without transferring receptor or enzyme activity to DMD.

Summary: Dystrophin associates with alpha-catulin-containing DAPC assemblies.

Reason: The recovered PMID:21115837 original and source-specific IntAct records report HEK293 tandem-affinity purification/co-immunoprecipitation involving alpha-catulin and DAPC members. The directly tested PLCbeta2-binding mechanism belongs to alpha-catulin, not dystrophin. This source supports DMD complex association but does not establish the DMD–alpha-catulin interface as binary; retain the generic association as non-core under the project instruction.

Summary: Dystrophin binds the beta-dystrobrevin scaffold (beta-dystrobrevin).

Reason: PMID:25416956 supports a binary yeast two-hybrid interaction with beta-dystrobrevin. The literal pair has prey-pooling, array and validated two-hybrid records. Independent rat-brain co-immunoprecipitation/fractionation in PMID:10545507 corroborates dystrophin–beta-dystrobrevin–syntrophin assemblies, but that paper presents the added nNOS signaling linkage as a hypothesis. Positive binary binding and native complex context are retained without treating structural DGC association alone as proof of the stricter signaling-scaffold class. The generic interaction remains non-core under the project instruction.

Summary: Dystrophin has a validated binary interaction with HAUS1.

Reason: The PMID:25416956 source-specific records include array, pooling and validated yeast two-hybrid detection of human DMD–HAUS1. The binary result is retained. HAUS1 augmin membership does not by itself establish a DMD microtubule-nucleation function or a sufficiently specific recognition class, so the supported interaction remains non-core under the project instruction.

Summary: Dystrophin binds the signaling scaffold alpha-catulin.

Reason: PMID:25416956 supplies source-specific validated binary yeast two-hybrid records for DMD and CTNNAL1. Alpha-catulin is a signaling scaffold: its curated function and independent PMID:21115837 experiments place it in multipartner signaling assemblies, including recruitment of PLCbeta2. The binding term classifies the partner; it does not transfer alpha-catulin's downstream signaling mechanism to DMD or establish the endogenous interface and affinity.

Proposed replacements: scaffold protein binding

Summary: Dystrophin interacts with the DNA-binding transcription factor HNF4A.

Reason: PMID:25910212 tests wild-type and mutant human proteins by binary yeast two-hybrid screening and pairwise retesting. The literal DMD–HNF4A records include a non-mutated pair and two residue-102 perturbation records for HNF4A isoform P41235-3. This product retains the nuclear-receptor DNA-binding region; curated HNF4A function independently establishes sequence-specific transcriptional regulation. The partner classification is independently supported, without asserting that dystrophin regulates transcription, binds DNA, or forms a demonstrated native nuclear complex. The source-specific binding capacity is positive, but this untargeted screen and partner identity do not establish the independent physiological pair context needed here for a more specific partner-class refinement. Retain the generic association as non-core under the project instruction; neither interaction falsity nor incompatible localization is inferred.

Summary: Dystrophin associates with nNOS in human atrial tissue.

Reason: PMID:27225184 shows reciprocal endogenous dystrophin–nNOS co-immunoprecipitation and sarcolemmal colocalization in human atria, with loss of the association in atrial fibrillation. These are positive complex-association observations, not purified binary binding or a measured DMD–nNOS interface. Retain the generic association as non-core under the project instruction; the source does not establish nitric-oxide synthase activity in dystrophin.

Summary: Dystrophin associates with SNTA1 in the BioPlex 2.0 complex map.

Reason: PMID:28514442 has a literal DMD–SNTA1 anti-tag co-immunoprecipitation record from human HEK293T cells, represented by spoke expansion of an affinity-purified complex. The original describes controlled tagged-bait AP-MS and statistical interaction filtering. These data establish association but do not isolate a binary binding interface or a DMD activity inferred from the partner's function. Retain this supported generic association as non-core under the scoped project instruction.

Summary: Dystrophin associates with SNTB2 in the BioPlex 2.0 complex map.

Reason: PMID:28514442 has a literal DMD–SNTB2 anti-tag co-immunoprecipitation record from human HEK293T cells, represented by spoke expansion of an affinity-purified complex. The original describes controlled tagged-bait AP-MS and statistical interaction filtering. These data establish association but do not isolate a binary binding interface or a DMD activity inferred from the partner's function. Retain this supported generic association as non-core under the scoped project instruction.

Summary: Dystrophin associates with SNTB1 in the BioPlex 2.0 complex map.

Reason: PMID:28514442 has a literal DMD–SNTB1 anti-tag co-immunoprecipitation record from human HEK293T cells, represented by spoke expansion of an affinity-purified complex. The original describes controlled tagged-bait AP-MS and statistical interaction filtering. These data establish association but do not isolate a binary binding interface or a DMD activity inferred from the partner's function. Retain this supported generic association as non-core under the scoped project instruction.

Summary: Dystrophin associates with HAUS1 in the BioPlex 2.0 complex map.

Reason: PMID:28514442 has a literal DMD–HAUS1 anti-tag co-immunoprecipitation record from human HEK293T cells, represented by spoke expansion of an affinity-purified complex. The original describes controlled tagged-bait AP-MS and statistical interaction filtering. These data establish association but do not isolate a binary binding interface or a DMD activity inferred from the partner's function. Retain this supported generic association as non-core under the scoped project instruction.

Summary: Dystrophin binds the beta-dystrobrevin scaffold (beta-dystrobrevin).

Reason: PMID:31515488 supports a binary yeast two-hybrid interaction with beta-dystrobrevin. The literal two-hybrid record contains a beta-dystrobrevin residue-396 variant recorded as having no effect; the study compares mutant and wild-type interaction profiles. Independent rat-brain co-immunoprecipitation/fractionation in PMID:10545507 corroborates dystrophin–beta-dystrobrevin–syntrophin assemblies, but that paper presents the added nNOS signaling linkage as a hypothesis. Positive binary binding and native complex context are retained without treating structural DGC association alone as proof of the stricter signaling-scaffold class. The generic interaction remains non-core under the project instruction.

Summary: Dystrophin binds the beta-dystrobrevin scaffold (beta-dystrobrevin isoform O60941-5).

Reason: PMID:32296183 supports a binary yeast two-hybrid interaction with beta-dystrobrevin isoform O60941-5. The literal pair has pooling, array and validated two-hybrid records and identifies O60941-5, rather than silently substituting the displayed partner product. Independent rat-brain co-immunoprecipitation/fractionation in PMID:10545507 corroborates dystrophin–beta-dystrobrevin–syntrophin assemblies, but that paper presents the added nNOS signaling linkage as a hypothesis. Positive binary binding and native complex context are retained without treating structural DGC association alone as proof of the stricter signaling-scaffold class. The generic interaction remains non-core under the project instruction. O60941-5 retains the annotated syntrophin-binding segment but deletes canonical residues 519–525 within the predicted coiled coil; neither retained sequence nor the gene-level function establishes identical multipartner scaffold function for that product.

Summary: Dystrophin has binary binding capacity for the PICK1 scaffold.

Reason: PMID:32296183 supplies pooling, array and validated yeast two-hybrid records for DMD–PICK1. PICK1 is an independently characterized multipartner receptor-trafficking scaffold. The assay does not establish that dystrophin binds the PICK1 PDZ domain, regulates receptor trafficking, or forms the same complex at native concentrations. The source-specific binding capacity is positive, but this untargeted screen and partner identity do not establish the independent physiological pair context needed here for a more specific partner-class refinement. Retain the generic association as non-core under the project instruction; neither interaction falsity nor incompatible localization is inferred.

Summary: Dystrophin binds the signaling scaffold alpha-catulin.

Reason: PMID:32296183 supplies source-specific validated binary yeast two-hybrid records for DMD and CTNNAL1. Alpha-catulin is a signaling scaffold: its curated function and independent PMID:21115837 experiments place it in multipartner signaling assemblies, including recruitment of PLCbeta2. The binding term classifies the partner; it does not transfer alpha-catulin's downstream signaling mechanism to DMD or establish the endogenous interface and affinity.

Proposed replacements: scaffold protein binding

Summary: Dystrophin associates with DTNB in the BioPlex 3.0 complex map.

Reason: PMID:33961781 includes source-specific DMD–DTNB anti-tag co-immunoprecipitation records in the BioPlex cell-line networks. Tagged human ORF baits were affinity purified with replicate and statistical controls; the imported pair is a spoke-expanded complex association. Neither those controls nor the partner's functional class by themselves establish a binary DMD recognition activity. Preserve this source-specific association as non-core under the project instruction, without assigning a natural DMD isoform from the canonical database accession.

Summary: Dystrophin associates with SNTA1 in the BioPlex 3.0 complex map.

Reason: PMID:33961781 includes source-specific DMD–SNTA1 anti-tag co-immunoprecipitation records in the BioPlex cell-line networks. Tagged human ORF baits were affinity purified with replicate and statistical controls; the imported pair is a spoke-expanded complex association. Neither those controls nor the partner's functional class by themselves establish a binary DMD recognition activity. Preserve this source-specific association as non-core under the project instruction, without assigning a natural DMD isoform from the canonical database accession.

Summary: Dystrophin associates with SNTB2 in the BioPlex 3.0 complex map.

Reason: PMID:33961781 includes source-specific DMD–SNTB2 anti-tag co-immunoprecipitation records in the BioPlex cell-line networks. Tagged human ORF baits were affinity purified with replicate and statistical controls; the imported pair is a spoke-expanded complex association. Neither those controls nor the partner's functional class by themselves establish a binary DMD recognition activity. Preserve this source-specific association as non-core under the project instruction, without assigning a natural DMD isoform from the canonical database accession.

Summary: Dystrophin associates with SNTB1 in the BioPlex 3.0 complex map.

Reason: PMID:33961781 includes source-specific DMD–SNTB1 anti-tag co-immunoprecipitation records in the BioPlex cell-line networks. Tagged human ORF baits were affinity purified with replicate and statistical controls; the imported pair is a spoke-expanded complex association. Neither those controls nor the partner's functional class by themselves establish a binary DMD recognition activity. Preserve this source-specific association as non-core under the project instruction, without assigning a natural DMD isoform from the canonical database accession.

Summary: Dystrophin associates with HAUS1 in the BioPlex 3.0 complex map.

Reason: PMID:33961781 includes source-specific DMD–HAUS1 anti-tag co-immunoprecipitation records in the BioPlex cell-line networks. Tagged human ORF baits were affinity purified with replicate and statistical controls; the imported pair is a spoke-expanded complex association. Neither those controls nor the partner's functional class by themselves establish a binary DMD recognition activity. Preserve this source-specific association as non-core under the project instruction, without assigning a natural DMD isoform from the canonical database accession.

Summary: Dystrophin associates with CTNNAL1 in the BioPlex 3.0 complex map.

Reason: PMID:33961781 includes source-specific DMD–CTNNAL1 anti-tag co-immunoprecipitation records in the BioPlex cell-line networks. Tagged human ORF baits were affinity purified with replicate and statistical controls; the imported pair is a spoke-expanded complex association. Neither those controls nor the partner's functional class by themselves establish a binary DMD recognition activity. Preserve this source-specific association as non-core under the project instruction, without assigning a natural DMD isoform from the canonical database accession.

Summary: Dystrophin associates with DTNA in the BioPlex 3.0 complex map.

Reason: PMID:33961781 includes source-specific DMD–DTNA anti-tag co-immunoprecipitation records in the BioPlex cell-line networks. Tagged human ORF baits were affinity purified with replicate and statistical controls; the imported pair is a spoke-expanded complex association. Neither those controls nor the partner's functional class by themselves establish a binary DMD recognition activity. Preserve this source-specific association as non-core under the project instruction, without assigning a natural DMD isoform from the canonical database accession.

Summary: Dystrophin associates with DTNB in the 2025 U2OS AP-MS network.

Reason: The actual PMID:40205054 deposited AP-MS network contains the exact DMD–DTNB edge; this is source-specific support rather than substitution of an earlier experiment. Its Methods use sequence-verified human ORF baits with C-terminal HA/FLAG tags in U2OS cells and CompPASS-based interaction filtering. The result supports a cellular complex association, not an isolated binary interface or partner-derived DMD activity. Retain the supported generic association as non-core under the project instruction.

Summary: Dystrophin associates with SNTA1 in the 2025 U2OS AP-MS network.

Reason: The actual PMID:40205054 deposited AP-MS network contains the exact DMD–SNTA1 edge; this is source-specific support rather than substitution of an earlier experiment. Its Methods use sequence-verified human ORF baits with C-terminal HA/FLAG tags in U2OS cells and CompPASS-based interaction filtering. The result supports a cellular complex association, not an isolated binary interface or partner-derived DMD activity. Retain the supported generic association as non-core under the project instruction.

Summary: Dystrophin associates with SNTB2 in the 2025 U2OS AP-MS network.

Reason: The actual PMID:40205054 deposited AP-MS network contains the exact DMD–SNTB2 edge; this is source-specific support rather than substitution of an earlier experiment. Its Methods use sequence-verified human ORF baits with C-terminal HA/FLAG tags in U2OS cells and CompPASS-based interaction filtering. The result supports a cellular complex association, not an isolated binary interface or partner-derived DMD activity. Retain the supported generic association as non-core under the project instruction.

Summary: Dystrophin associates with SNTB1 in the 2025 U2OS AP-MS network.

Reason: The actual PMID:40205054 deposited AP-MS network contains the exact DMD–SNTB1 edge; this is source-specific support rather than substitution of an earlier experiment. Its Methods use sequence-verified human ORF baits with C-terminal HA/FLAG tags in U2OS cells and CompPASS-based interaction filtering. The result supports a cellular complex association, not an isolated binary interface or partner-derived DMD activity. Retain the supported generic association as non-core under the project instruction.

Summary: Dystrophin associates with HAUS1 in the 2025 U2OS AP-MS network.

Reason: The actual PMID:40205054 deposited AP-MS network contains the exact DMD–HAUS1 edge; this is source-specific support rather than substitution of an earlier experiment. Its Methods use sequence-verified human ORF baits with C-terminal HA/FLAG tags in U2OS cells and CompPASS-based interaction filtering. The result supports a cellular complex association, not an isolated binary interface or partner-derived DMD activity. Retain the supported generic association as non-core under the project instruction.

Summary: Dystrophin associates with CTNNAL1 in the 2025 U2OS AP-MS network.

Reason: The actual PMID:40205054 deposited AP-MS network contains the exact DMD–CTNNAL1 edge; this is source-specific support rather than substitution of an earlier experiment. Its Methods use sequence-verified human ORF baits with C-terminal HA/FLAG tags in U2OS cells and CompPASS-based interaction filtering. The result supports a cellular complex association, not an isolated binary interface or partner-derived DMD activity. Retain the supported generic association as non-core under the project instruction.

Summary: Dystrophin associates with DTNA in the 2025 U2OS AP-MS network.

Reason: The actual PMID:40205054 deposited AP-MS network contains the exact DMD–DTNA edge; this is source-specific support rather than substitution of an earlier experiment. Its Methods use sequence-verified human ORF baits with C-terminal HA/FLAG tags in U2OS cells and CompPASS-based interaction filtering. The result supports a cellular complex association, not an isolated binary interface or partner-derived DMD activity. Retain the supported generic association as non-core under the project instruction.

Summary: Dystrophin binds the syntrophin scaffold SNTB1.

Reason: PMID:7844150 explicitly reports dystrophin–syntrophin binding, corroborated by the literal in vitro interaction record for SNTB1. The abstract identifies exon 74 as necessary and sufficient for the measured syntrophin association. Syntrophins are multipartner membrane-signaling scaffolds, so scaffold protein binding is more informative than generic binding. This does not assert recognition of a syntrophin PDZ domain: the scaffold is the binding partner. Full original Methods were not independently recovered, so finer assay/construct details remain limited to the inspected abstract and curated pair.

Proposed replacements: scaffold protein binding

Summary: Dystrophin binds the syntrophin scaffold SNTB2.

Reason: PMID:8576247 explicitly reports dystrophin–syntrophin binding, corroborated by the literal in vitro interaction record for SNTB2. The abstract describes radiolabeled syntrophins binding in-vitro-translated human dystrophin peptides, with the major site in the exon-74/adjacent region. Syntrophins are multipartner membrane-signaling scaffolds, so scaffold protein binding is more informative than generic binding. This does not assert recognition of a syntrophin PDZ domain: the scaffold is the binding partner. Full original Methods were not independently recovered, so finer assay/construct details remain limited to the inspected abstract and curated pair.

Proposed replacements: scaffold protein binding

Summary: Dystrophin binds the syntrophin scaffold SNTB1.

Reason: PMID:8576247 explicitly reports dystrophin–syntrophin binding, corroborated by the literal in vitro interaction record for SNTB1. The abstract describes radiolabeled syntrophins binding in-vitro-translated human dystrophin peptides, with the major site in the exon-74/adjacent region. Syntrophins are multipartner membrane-signaling scaffolds, so scaffold protein binding is more informative than generic binding. This does not assert recognition of a syntrophin PDZ domain: the scaffold is the binding partner. Full original Methods were not independently recovered, so finer assay/construct details remain limited to the inspected abstract and curated pair.

Proposed replacements: scaffold protein binding

Summary: Dystrophin binds the alpha-syntrophin scaffold through its C-terminal region.

Reason: The recovered PMID:9356463 original and literal two-hybrid record support direct human dystrophin–SNTA1 binding, with a dystrophin C-terminal sufficient region including exon 74. Independent SNTA1 function and DAPC studies identify a multipartner signaling scaffold. Scaffold protein binding refines the demonstrated partner class without assigning a PDZ-domain contact or claiming all 17 natural DMD products share this interaction.

Proposed replacements: scaffold protein binding

Summary: Dystrophin binds alpha-dystrobrevin through complementary coiled coils.

Reason: PMID:9356463 directly tests human dystrophin and alpha-dystrobrevin constructs by controlled two-hybrid and reciprocal in vitro co-immunoprecipitation. Minimal binding maps to their first coiled-coil helices; homodimerization was not detected in the tested two-hybrid conditions. This establishes a specific DGC interaction but does not justify an additional partner-class activity or generic coiled-coil-binding annotation without a verified suitable term. Preserve the positive association as non-core under the project instruction.

Summary: Dp71 associates with lamin B1 in a nuclear complex.

Reason: The rat donor is grounded by PMID:21886794. Rat PC12 co-immunoprecipitation and pull-down using bacterially expressed human GST-Dp71 with nuclear extract support a lamin B1 association; the assay is not a purified two-component affinity measurement. Retain the contextual lamin-binding assertion with that directness limit, rather than inferring a universal lamin interaction or a separate core activity.

Summary: Short dystrophin products can occupy a nuclear pool.

Reason: The rat neuronal Dp71 evidence includes nuclear immunolocalization in PMID:11326752 and nuclear Dp71/lamin B1 complex experiments in PMID:21886794. Retain nuclear localization as a contextual pool. These observations do not establish that every human product is nuclear, and the imported broad nuclear observation is not sharpened to an unmeasured subnuclear site.

Summary: Mitochondrial association does not yet resolve an outer-membrane location.

Reason: The rat donor derives from PMID:10411999, whose accessible abstract reports dystrophin-family immunoreactivity in perivascular astrocytes and ribosomal apparatus but does not resolve the mitochondrial outer-membrane assay. The full original was unavailable. Independent human mitochondrial fractionation in PMID:34575126 supports a mitochondrial Dp71-family pool, with purification controls, but does not locate it specifically on the outer membrane. Preserve the source claim as unresolved, not as a demonstrated absence.

Summary: Dystrophin occupies the cytosolic side of its membrane-associated complexes.

Reason: An explicit participant path from Reactome R-HSA-390593 reaches human DMD P11532, residues 1–3685, in the cytosol. The model includes DMD within sarcomeric complexes; ATP hydrolysis and troponin calcium binding are performed by the relevant contractile components, not by dystrophin. The location does not imply exclusive free solubility and is compatible with sarcolemmal attachment. Retain this positive, broad compartment annotation as contextual evidence; the integrated core is localized to the sarcolemmal DGC rather than treating cytosol as a separate functional unit.

Summary: Dystrophin occupies the cytosolic side of its membrane-associated complexes.

Reason: An explicit participant path from Reactome R-HSA-390595 reaches human DMD P11532, residues 1–3685, in the cytosol. The model includes DMD within sarcomeric complexes; ATP hydrolysis and troponin calcium binding are performed by the relevant contractile components, not by dystrophin. The location does not imply exclusive free solubility and is compatible with sarcolemmal attachment. Retain this positive, broad compartment annotation as contextual evidence; the integrated core is localized to the sarcolemmal DGC rather than treating cytosol as a separate functional unit.

Summary: Dystrophin occupies the cytosolic side of its membrane-associated complexes.

Reason: An explicit participant path from Reactome R-HSA-390597 reaches human DMD P11532, residues 1–3685, in the cytosol. The model includes DMD within sarcomeric complexes; ATP hydrolysis and troponin calcium binding are performed by the relevant contractile components, not by dystrophin. The location does not imply exclusive free solubility and is compatible with sarcolemmal attachment. Retain this positive, broad compartment annotation as contextual evidence; the integrated core is localized to the sarcolemmal DGC rather than treating cytosol as a separate functional unit.

Summary: Dystrophin occupies the cytosolic side of its membrane-associated complexes.

Reason: An explicit participant path from Reactome R-HSA-390598 reaches human DMD P11532, residues 1–3685, in the cytosol. The model includes DMD within sarcomeric complexes; ATP hydrolysis and troponin calcium binding are performed by the relevant contractile components, not by dystrophin. The location does not imply exclusive free solubility and is compatible with sarcolemmal attachment. Retain this positive, broad compartment annotation as contextual evidence; the integrated core is localized to the sarcolemmal DGC rather than treating cytosol as a separate functional unit.

Summary: Dystrophin occupies the cytosolic side of its membrane-associated complexes.

Reason: An explicit participant path from Reactome R-HSA-9913333 reaches human DMD P11532, residues 1–3685, in the cytosol. The model places cytosolic DMD within, or recruited to, a plasma-membrane DGC; extracellular laminin, agrin and perlecan recognition belongs to the appropriate extracellular components. The location does not imply exclusive free solubility and is compatible with sarcolemmal attachment. Retain this positive, broad compartment annotation as contextual evidence; the integrated core is localized to the sarcolemmal DGC rather than treating cytosol as a separate functional unit.

Summary: Dystrophin occupies the cytosolic side of its membrane-associated complexes.

Reason: An explicit participant path from Reactome R-HSA-9913339 reaches human DMD P11532, residues 1–3685, in the cytosol. The model places cytosolic DMD within, or recruited to, a plasma-membrane DGC; extracellular laminin, agrin and perlecan recognition belongs to the appropriate extracellular components. The location does not imply exclusive free solubility and is compatible with sarcolemmal attachment. Retain this positive, broad compartment annotation as contextual evidence; the integrated core is localized to the sarcolemmal DGC rather than treating cytosol as a separate functional unit.

Summary: Dystrophin occupies the cytosolic side of its membrane-associated complexes.

Reason: An explicit participant path from Reactome R-HSA-9914537 reaches human DMD P11532, residues 1–3685, in the cytosol. The model places cytosolic DMD within, or recruited to, a plasma-membrane DGC; extracellular laminin, agrin and perlecan recognition belongs to the appropriate extracellular components. The location does not imply exclusive free solubility and is compatible with sarcolemmal attachment. Retain this positive, broad compartment annotation as contextual evidence; the integrated core is localized to the sarcolemmal DGC rather than treating cytosol as a separate functional unit.

Summary: Dystrophin occupies the cytosolic side of its membrane-associated complexes.

Reason: An explicit participant path from Reactome R-NUL-9913739 reaches human DMD P11532, residues 1–3685, in the cytosol. This event is explicitly chimeric: human DMD with bovine actin evidence. It must not be described as a wholly human binding experiment. The location does not imply exclusive free solubility and is compatible with sarcolemmal attachment. Retain this positive, broad compartment annotation as contextual evidence; the integrated core is localized to the sarcolemmal DGC rather than treating cytosol as a separate functional unit.

Summary: Dystrophin-family immunoreactivity is associated with the ribosomal apparatus in rat astrocytes.

Reason: The accessible PMID:10411999 abstract explicitly reports strong ribosomal-apparatus immunostaining by Dys2, which recognizes long and short dystrophin products. Retain this contextual association with curator deference. It does not identify a particular human product, demonstrate a constitutive ribosomal subunit or establish translation catalysis.

Summary: Dystrophin has supported cortical and neuronal cytoskeletal pools, including a muscle costameric distribution.

Reason: The curated cytoskeleton location is consistent with the gene’s membrane-linking role. More informative supported pools include costameres in the human-construct/rat-muscle study PMID:16000376 and Dp71d-associated neurofilaments in the rat-cell study PMID:11326752. Use these anatomical refinements without asserting that they exhaust all cytoskeletal locations or that costamere is a typed GO descendant of cytoskeleton. Cortical cytoskeleton (GO:0030863) additionally preserves the cytoskeletal location itself as a verified descendant of GO:0005856; the submembranous pool is supported by the same sarcolemmal localization evidence. Costamere remains a complementary anatomical term, not a claimed ontology descendant.

Proposed replacements: cortical cytoskeleton costamere neurofilament

Summary: The muscle-associated claim is refined to cortical cytoskeleton and its costameric distribution.

Reason: PMID:3282674 predicts the rod-like human cytoskeletal architecture; it is not itself a costamere imaging experiment. The independent targeted study PMID:16000376 establishes dystrophin-dependent costameric organization and the supporting human N-terminal interaction. Use costamere as the anatomical refinement of this muscle-associated claim, explicitly relying on that additional evidence rather than rewriting the original citation. Retain cortical cytoskeleton (GO:0030863), a verified descendant of GO:0005856, alongside costamere so the cytoskeletal location is not replaced solely by a non-descendant anatomical term. The independent sarcolemmal evidence supports this cortical pool without excluding other locations.

Proposed replacements: cortical cytoskeleton costamere

Summary: A Dp71 isoform associates with neuronal neurofilaments.

Reason: The rat donor’s PMID:11326752 abstract explicitly distinguishes Dp71d in cytoplasmic neurofilaments from Dp71f, while both products occur in neuronal nuclei and Golgi. Retain the contextual location and the isoform distinction; the historical names were not mapped to a single current human accession solely by their labels.

Summary: Dystrophin occupies specialized muscle and postsynaptic plasma-membrane regions.

Reason: The mouse transfer is consistent with direct human sarcolemmal localization and ortholog postsynaptic localization. Sarcolemma and postsynaptic membrane provide supported, nonexclusive specialized membrane pools. The replacement does not mean that dystrophin spans the lipid bilayer or that all products share both locations.

Proposed replacements: sarcolemma postsynaptic membrane

Summary: Dystrophin contributes the structural linkage needed for muscle contraction.

Reason: The matched ARBA00043367 branch is consistent with the established long-product role in maintaining the membrane–cytoskeleton linkage during contraction. Human localization and targeted costameric interaction studies support a structural contribution to this process. Dystrophin is not the ATP-driven motor, calcium channel or troponin switch.

Summary: Dystrophin organizes membrane-associated cytoskeletal connections.

Reason: The source is an inference from structural-constituent activity. Human N-terminal interactions and the displacement of the costameric network in PMID:16000376, together with native DGC architecture, support an organizing structural role rather than mere coincidental colocalization. This does not confer actin polymerase or motor activity.

Summary: The cited recombinant-expression study does not by itself resolve muscle-organ development.

Reason: PMID:1824797 reports expression of full-length mouse dystrophin in COS cells and its membrane localization. Its full original was not recovered, and the accessible abstract does not establish a developmental assay. Other ortholog studies support muscle development, but the source-specific developmental inference from this NAS reference remains unresolved; no wrong-gene or wrong-species accusation is made.

Summary: The inherited skeletal-muscle-development assertion has a legitimate PAINT origin.

Reason: The literal IBD is at Euteleostomi PTN008535380 on the human target lineage, with mouse and zebrafish descendants. Mouse developmental and regenerative perturbation records provide experimental grounding. Retain this developmental consequence as non-core relative to the membrane-linking activity; donor number is not used to judge the phylogenetic inference, and no target-specific loss is inferred.

Summary: Dystrophin supports localization of associated proteins at the plasma membrane.

Reason: The mouse source includes PMID:7545544, which reports loss of membrane-associated neuronal nitric-oxide synthase in dystrophin-deficient muscle. Protein localization to plasma membrane is a verified typed descendant of intracellular protein localization and captures the supported recruitment outcome. This is scaffold-mediated positioning, not transport motor activity or proof of direct dystrophin–NOS1 binding.

Proposed replacements: protein localization to plasma membrane

Summary: Dystrophin-dependent scaffolding localizes a signaling protein to the sarcolemma.

Reason: PMID:7545544 establishes loss of membrane-associated nNOS in mdx muscle and human DMD, supporting a performed structural localization role for dystrophin-containing assemblies. Refine intracellular localization to protein localization to plasma membrane, a verified is_a/part_of descendant. This is scaffold-mediated organization, not motor transport or nitric-oxide catalysis. The original Methods were not recovered; the positive abstract and independent complex evidence support the location function without resolving a binary NOS-binding interface.

Proposed replacements: protein localization to plasma membrane

Summary: The ZZ domain supplies a structural zinc-binding site.

Reason: InterPro IPR000433 is a ZZ-type zinc-finger domain with an explicit zinc-binding description, and the actual target match spans residues 3307–3364 of the canonical human sequence. Native-complex structural evidence supports the cysteine-rich region’s folded interaction role. Retain structural zinc binding as non-core rather than treating it as a separate catalytic function or extending it to products lacking the domain.

Summary: Dp71 supports proliferation in a neuronal cell model.

Reason: PMID:21886794 compares stable Dp71-reduced rat PC12 clones and controls, with proliferation, BrdU and cell-cycle assays plus lamin B1 complex changes. Retain the contextual positive-proliferation assertion. These experiments do not establish a direct cell-cycle enzyme or make proliferation the principal molecular role of all human dystrophin products.

Summary: Dystrophin contributes to the structural integrity of muscle fibers.

Reason: PMID:16000376 directly analyzes human dystrophin N-terminal interaction with keratin 19 and tests the costameric network in rat muscle. The results support the structural-constituent-of-muscle definition. They do not demonstrate synthesis of the interacting peptide or a catalytic muscle activity.

Summary: Human muscle dystrophin is a sarcolemmal structural protein.

Reason: PMID:3287171 directly reports dystrophin immunolocalization in normal human skeletal-muscle sarcolemma and reduced or absent staining in DMD biopsies. Later binding and native-complex work establishes the cytoskeletal anchoring mechanism. Retain the structural role without misdescribing the original paper’s proposed anchoring model as a purified reconstitution.

Summary: The observed muscle-cell boundary pool is sarcolemmal.

Reason: PMID:10867799 explicitly describes immunogold observations at the inner surface of the plasma membrane in normal human quadriceps, including aciculin–dystrophin epitope proximity. Current GO:0009986 denotes the external part of the cell wall or plasma membrane. Sarcolemma better captures the supported muscle-membrane location without placing dystrophin extracellularly or treating proximity as a complete direct-binding interface.

Proposed replacements: sarcolemma

Summary: Dystrophin deficiency alters sarcoplasmic-reticulum calcium release.

Reason: PMID:20080623 tests mdx mouse cardiomyocytes and hearts. RyR2 S-nitrosylation, calstabin2 depletion and abnormal calcium release accompany dystrophin deficiency; S107 or antioxidant treatment corrects parts of this downstream phenotype without restoring dystrophin. This supports a contextual regulatory consequence of dystrophin-dependent muscle integrity, not calcium transport or a direct RyR2 enzyme activity by DMD.

Summary: Dystrophin deficiency alters sarcoplasmic-reticulum calcium release.

Reason: PMID:20080623 tests mdx mouse cardiomyocytes and hearts. RyR2 S-nitrosylation, calstabin2 depletion and abnormal calcium release accompany dystrophin deficiency; S107 or antioxidant treatment corrects parts of this downstream phenotype without restoring dystrophin. This supports a contextual regulatory consequence of dystrophin-dependent muscle integrity, not calcium transport or a direct RyR2 enzyme activity by DMD.

Summary: Cardiac calcium-release regulation is a contextual dystrophin-dependent phenotype.

Reason: PMID:20080623 tests mdx mouse cardiomyocytes and hearts. RyR2 S-nitrosylation, calstabin2 depletion and abnormal calcium release accompany dystrophin deficiency; S107 or antioxidant treatment corrects parts of this downstream phenotype without restoring dystrophin. This supports a contextual regulatory consequence of dystrophin-dependent muscle integrity, not calcium transport or a direct RyR2 enzyme activity by DMD. The result is not a separate core molecular mechanism.

Summary: Cardiac calcium-release regulation is a contextual dystrophin-dependent phenotype.

Reason: PMID:20080623 tests mdx mouse cardiomyocytes and hearts. RyR2 S-nitrosylation, calstabin2 depletion and abnormal calcium release accompany dystrophin deficiency; S107 or antioxidant treatment corrects parts of this downstream phenotype without restoring dystrophin. This supports a contextual regulatory consequence of dystrophin-dependent muscle integrity, not calcium transport or a direct RyR2 enzyme activity by DMD. The result is not a separate core molecular mechanism.

Summary: Dp71 supports neuronal projection development in PC12 cells.

Reason: The literal rat donor is grounded by PMID:15149856: antisense Dp71 suppresses neurite outgrowth after NGF or dibutyryl-cAMP induction, while early ERK activation and cessation of proliferation remain intact. Retain the contextual positive developmental role without treating the perturbation as identification of a direct growth-factor-signaling activity.

Summary: Dystrophin products associate with a postsynaptic-density fraction.

Reason: PMID:10545507 demonstrates brain DGC-like complexes and PSD enrichment of long dystrophin and a Dp71 signal. Its Discussion explicitly cautions that some glial proteins can adsorb to PSD preparations. Independent rat-brain fractionation in PMID:1454857 supports the long dystrophin PSD pool. Retain this contextual location without assigning every short product to neuronal PSDs from fractionation alone.

Summary: Dystrophin-dependent muscle integrity affects skeletal-muscle calcium-release control.

Reason: PMID:19198614 studies mdx mouse skeletal muscle. RyR1 modification and calstabin1 depletion accompany calcium leak; S107 acts on the downstream channel complex. Retain the physiological regulatory contribution while distinguishing dystrophin’s membrane/cytoskeleton role from the ryanodine-receptor channel and the downstream pharmacological rescue.

Summary: Dystrophin-dependent muscle integrity affects skeletal-muscle calcium-release control.

Reason: PMID:19198614 studies mdx mouse skeletal muscle. RyR1 modification and calstabin1 depletion accompany calcium leak; S107 acts on the downstream channel complex. Retain the physiological regulatory contribution while distinguishing dystrophin’s membrane/cytoskeleton role from the ryanodine-receptor channel and the downstream pharmacological rescue.

Summary: The source resolves a calcium-release-dependent component of skeletal-muscle contraction regulation.

Reason: PMID:19198614 studies mdx mouse skeletal muscle. RyR1 modification and calstabin1 depletion accompany calcium leak; S107 acts on the downstream channel complex. Retain the physiological regulatory contribution while distinguishing dystrophin’s membrane/cytoskeleton role from the ryanodine-receptor channel and the downstream pharmacological rescue. The calcium-release-dependent regulatory term is a verified descendant of the imported broader regulation-of-skeletal-muscle-contraction term and captures the measured mechanism.

Proposed replacements: regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion

Summary: The source resolves a calcium-release-dependent component of skeletal-muscle contraction regulation.

Reason: PMID:19198614 studies mdx mouse skeletal muscle. RyR1 modification and calstabin1 depletion accompany calcium leak; S107 acts on the downstream channel complex. Retain the physiological regulatory contribution while distinguishing dystrophin’s membrane/cytoskeleton role from the ryanodine-receptor channel and the downstream pharmacological rescue. The calcium-release-dependent regulatory term is a verified descendant of the imported broader regulation-of-skeletal-muscle-contraction term and captures the measured mechanism.

Proposed replacements: regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion

Summary: Dystrophin distribution changes during the denervation response.

Reason: The rat donor’s PMID:8906620 reports dystrophin redistribution associated with acetylcholine-receptor clusters after denervation. Retain the contextual expression/localization response under the known muscle-adaptation context. This is not evidence that dystrophin senses denervation or catalyzes the signaling response, and the IEP provenance is not discarded merely because it is observational.

Summary: DGC membership is inherited within the target’s supported PAINT lineage.

Reason: The exact IBD is placed at Eumetazoa PTN000937183, an ancestor of human DMD. Descendant grounding includes target human DMD and ortholog/paralog complex evidence. Target self-evidence is legitimate input to the ancestral judgment, not circularity. Targeted human-construct binding and native mammalian structures independently support DMD as a DGC component.

Summary: Dystrophin is a component of the dystrophin-associated glycoprotein complex.

Reason: PMID:17993586 reports a purified native dystrophin-glycoprotein complex and its structural organization. This agrees with targeted dystroglycan binding and the later native rabbit and mouse complex structures. Retain complex membership while keeping the experimental species and the long-product structural mechanism distinct from automatic functional assignment to all human isoforms.

Summary: The electronic DGC assignment agrees with directly established complex membership.

Reason: ARBA00028743 has an actual matching target branch, and the mouse and rat donor records independently place dystrophin in DGC-like complexes. Human construct binding and native-complex structures substantiate the biological assertion; the rule match alone is not treated as an assay.

Summary: Dystrophin is an integral structural participant in the DGC.

Reason: Human dystrophin–dystroglycan fragment binding in PMID:7592992 supports the source complex assignment, and native rabbit and mouse DGC structures independently establish dystrophin within the cytoplasmic subcomplex. Retain the original NAS evidence code without converting a native ortholog structure into an assay of all human alternative products.

Summary: DGC membership is established despite limited access to the short historical commentary.

Reason: The cached PMID:8282811 record is a short commentary without an abstract, so no detailed experimental claim is attributed to it. The gene-level complex assertion is independently supported by PMID:7592992 and later native-complex structures. Retain the curator’s membership claim with that access distinction, rather than rejecting it because the original commentary is not informative in the cache.

Summary: Dystrophin participates in a syntrophin-associated cardiac sodium-channel complex.

Reason: The PMID:21164104 abstract explicitly reports dystrophin and syntrophin with Nav1.5 at cardiomyocyte lateral membranes, with reduced lateral Nav1.5 in mdx hearts. Retain the contextual syntrophin-complex assignment. The channel’s PDZ ligand binds syntrophin; this does not establish that dystrophin itself recognizes the channel’s PDZ-binding motif.

Summary: Dystrophin has a lateral-membrane pool in cardiomyocytes.

Reason: PMID:21164104 reports the dystrophin/syntrophin-associated lateral pool of Nav1.5, distinct from the SAP97-associated intercalated-disc pool. Retain this source-supported specialized location with the mouse-deficiency context explicit; no exclusive localization or new ion-channel activity is inferred.

Summary: The source-specific myosin-binding assertion remains unresolved.

Reason: PMID:16803572 is available only as an abstract despite original-recovery attempts. It supports short dystrophin-complex participation in platelet actin organization, but the individual myosin experiment and its interaction controls were not accessible. Preserve the curator assertion as unresolved; neither myosin motor activity nor absence of the interaction is inferred.

Summary: The matched electronic vinculin-binding rule does not independently resolve the original assay.

Reason: The current ARBA00085907 branch matches the target’s official domains and primate lineage. Its corresponding experimental context is the platelet study PMID:16803572, whose full pair-specific data were not recovered. The abstract names vinculin in the tested adhesion system but does not resolve its binding relationship to dystrophin. Leave the claim unresolved without calling the rule match an independent experiment.

Summary: The curated dystrophin–vinculin interaction awaits source-specific adjudication.

Reason: PMID:16803572 names vinculin among the adhesion-system proteins examined by immunofluorescence and immunoprecipitation, but the full target-pair data were unavailable. Retain the exact positive IPI source and partner, while leaving the binding assertion unresolved rather than claiming that a short dystrophin product could not associate with vinculin.

Summary: Dystrophin expression changes during cortical synaptic maturation.

Reason: The complete original PMID:1454857 shows rat cortical PSD dystrophin increasing approximately ninefold between postnatal days 7 and 10, and loss of the long dystrophin signal in mdx mouse PSDs. Retain the existing developmental-expression inference as contextual and observational. The paper does not demonstrate a DMD-specific cortical patterning mechanism or assign the smaller immunoreactive bands to current human isoforms.

Summary: A myofibrillar dystrophin pool has been reported under ischemic conditions.

Reason: The literal rat donor PMID:12890920 reports dystrophin redistribution toward a myofibrillar fraction during ischemia rather than constitutive equivalence of all membrane and myofibrillar pools. ARBA00028265 has a matching current target branch, but that does not remove the source’s condition dependence. Retain non-core localization with the pathological redistribution limit.

Summary: The specific Z-disc assertion remains unresolved from the accessible aciculin study.

Reason: The mouse source is PMID:7890770. Its accessible abstract positively supports aciculin–dystrophin association and localization at sarcolemmal/myotendinous regions, but does not resolve the Z-disc observation or distinguish the dystrophin signal from the associated protein. The full original was not recovered. Preserve the curated source and uncertainty rather than infer absence of a Z-disc pool from the abstract.

Summary: The specific Z-disc assertion remains unresolved from the accessible aciculin study.

Reason: The mouse source is PMID:7890770. Its accessible abstract positively supports aciculin–dystrophin association and localization at sarcolemmal/myotendinous regions, but does not resolve the Z-disc observation or distinguish the dystrophin signal from the associated protein. The full original was not recovered. Preserve the curated source and uncertainty rather than infer absence of a Z-disc pool from the abstract.

Summary: A short dystrophin product has been observed in lamellipodium-like regions.

Reason: PMID:11368101 describes rat brain Dp71f immunolocalization, including actin-positive lamellipodium-like regions. Retain the contextual location with the original morphology-based qualification. Historical Dp71f naming is not sufficient to assign this localization uniquely to one current human accession.

Summary: The inspected donor experiment resolves a muscle plasma-membrane pool.

Reason: The actual PMID:25139234 Methods and Results use dystrophin immunostaining in wild-type and mTOR-deficient mouse heart and report decreased, uneven dystrophin distribution with membrane leakage. They support the sarcolemmal pool rather than a specifically identified cell-junction structure. Refine to sarcolemma using the observed compartment and independent human muscle evidence, without attributing the mTOR perturbation to a DMD-specific signaling experiment.

Proposed replacements: sarcolemma

Summary: Dystrophin participates in a muscle cell–substrate attachment region.

Reason: The mouse source PMID:7890770 reports aciculin–dystrophin association and enrichment at myotendinous junctions. Retain the contextual cell–substrate-junction localization with curator deference; the accessible abstract does not require equating all sarcolemmal staining with a focal adhesion or assigning the binding interface to every product.

Summary: Dystrophin participates in a muscle cell–substrate attachment region.

Reason: The mouse source PMID:7890770 reports aciculin–dystrophin association and enrichment at myotendinous junctions. Retain the contextual cell–substrate-junction localization with curator deference; the accessible abstract does not require equating all sarcolemmal staining with a focal adhesion or assigning the binding interface to every product.

Summary: Short dystrophin products associate with neurosecretory granules.

Reason: The rat source PMID:9858364 reports Dp71/Dp140-related signals on secretory granules in neurohypophysial axonal swellings, with a distinct distribution from nerve endings. Retain this contextual granule association; it is not evidence for a universal secretory-granule structural subunit or a DMD-catalyzed secretion reaction.

Summary: The observed differentiation context is neuronal.

Reason: PMID:22008482 reports an alternatively spliced Dp71e transcript and increased mRNA/protein during NGF-driven rat PC12 differentiation, also detecting the transcript in human cell lines. Refine the broad differentiation term to neuron differentiation, a verified descendant, while retaining the expression-pattern evidence and not claiming that this source establishes a direct catalytic differentiation mechanism or an exact current-human-product assignment.

Proposed replacements: neuron differentiation

Summary: PDZ-domain recognition remains unresolved despite a positive fragment-binding report.

Reason: PMID:15024025 tests Kir-channel-tail capture of rat-tissue dystrophin-associated assemblies, with syntrophin supplying the PDZ recognition interface; this does not itself show DMD binding a PDZ domain. PMID:26378238 reports binding of purified dystrophin R16–17 fragments to an immobilized nNOS PDZ construct by biolayer interferometry, with an equilibrium dissociation constant of about 50 micromolar and multiphasic kinetics; the atomic interface is modeled. PMID:29790927 independently shows that human dystrophin-repeat peptides capture syntrophins from mouse muscle and that microdystrophin restores sarcolemmal nNOS only when alpha-syntrophin is present. That physiological recruitment experiment does not repeat or refute the earlier purified-fragment binding assay. The contribution of a direct contact in the native human complex remains unresolved.

Summary: The platelet filopodium observation could not be independently resolved.

Reason: The accessible PMID:16803572 abstract describes short dystrophin-associated complexes and platelet cytoskeletal remodeling, but does not provide the filopodial image or precise protein distribution. The full original was not recovered. Preserve the IDA assertion as unresolved rather than infer a location from general actin-network participation.

Summary: Dp71 expression accompanies neuronal differentiation.

Reason: PMID:8858620 measures increased Dp71 RNA and protein during NGF-driven PC12 differentiation. Retain the contextual IEP assertion, supported independently by neurite perturbation results in PMID:15149856. The expression increase alone is not treated as identification of a differentiation enzyme or a signaling-catalytic function.

Summary: Short dystrophin products occupy an axonal pool.

Reason: PMID:9858364 localizes rat Dp71/Dp140-associated signals to neurohypophysial axonal swellings and reports redistribution after dehydration. Retain the axonal localization while preserving the paper’s distinction from nerve endings and avoiding an exact human isoform assignment from historical molecular masses.

Summary: The actual fractionation supports postsynaptic density rather than synaptic-vesicle membrane.

Reason: All three pages of PMID:1454857 were inspected. Adult rat brain homogenate, synaptic-membrane and highly purified postsynaptic-density fractions were compared; the long dystrophin signal was strongly enriched in PSDs and absent from mdx mouse PSDs. No synaptic-vesicle fraction is identified in these experiments. Replace the mislocalized membrane term with the directly supported postsynaptic-density term, retaining the original rat electronic source identity.

Proposed replacements: postsynaptic density

Summary: The precise filopodium-membrane assignment remains unresolved from the accessible source.

Reason: The PMID:16803572 abstract does not provide the target-specific membrane-localization observation, and the full original remained unavailable. Short-product participation in the platelet actin network is not by itself a demonstration of this specific membrane pool. Preserve the curated positive assertion without asserting either an erroneous annotation or exclusive localization.

Summary: The matched rule retains an unverified source-specific filopodial membrane claim.

Reason: ARBA00085514 matches the target’s official FunFam and primate conditions, reproducing the electronic provenance. The underlying platelet localization context in PMID:16803572 remains abstract-only, so the mapping does not independently resolve the precise filopodium-membrane claim. This uncertainty does not imply a target-specific evolutionary loss.

Summary: The recovered dystrophin-containing complex is a DGC-like assembly.

Reason: PMID:18468998 uses tandem-affinity purification in human HEK293 cells to recover dystrophin-associated protein assemblies. The identified partners and established complex architecture support refinement from an unspecified protein-containing complex to the dystrophin-associated glycoprotein complex. This does not imply that every recovered AP-MS partner contacts dystrophin directly or that the cultured-cell assembly has the exact stoichiometry of native skeletal muscle.

Proposed replacements: dystrophin-associated glycoprotein complex

Summary: Dystrophin-associated scaffolding is implicated in blood–brain-barrier maintenance.

Reason: PMID:30280653 is a review, not a new DMD perturbation study. Its indexed Figure 2 caption identifies a dystrophin scaffold connecting actin/vinculin in the endothelial cytoskeletal network; the normal cache contains only introductory sections despite its full-text flag. Retain the contextual NAS claim with that actual-access distinction and with independent perivascular dystrophin observations in PMID:10411999. This does not establish that all DMD products are endothelial or that the review newly proves a barrier-specific molecular activity.

Summary: Dystrophin contributes to the mechanical response of muscle.

Reason: PMID:14718391 compares diaphragm fibers from mdx and control mice, measuring altered length–tension relationships and stretch-evoked signaling. The evidence supports a load-bearing contribution to stretch responses, without conferring stretch-gated ion-channel or MAP-kinase activity on dystrophin. Retain this physiological function as non-core relative to its anchoring mechanism.

Summary: Sarcolemmal localization is phylogenetically and experimentally supported.

Reason: The literal sarcolemma IBD at Euteleostomi PTN008535380 lies on the human DMD lineage. Its descendant evidence includes the target itself, which is valid experimental grounding rather than circularity. Direct human muscle localization and native DGC structures support a cytoplasmic-face sarcolemmal pool, without implying that all natural short products are muscle-restricted.

Summary: Endogenous human atrial dystrophin is sarcolemmal.

Reason: PMID:27225184 directly examines human atrial tissue, including dystrophin/nNOS immunolocalization and reciprocal co-immunoprecipitation with controls. Retain the sarcolemmal location. The association assays do not by themselves prove a purified binary dystrophin–NOS interface.

Summary: Dystrophin occupies the muscle sarcolemma.

Reason: PMID:7545544 positively establishes the dystrophin-containing sarcolemmal signaling assembly in human DMD and mdx contexts. Independent direct human skeletal and atrial muscle localization supports the compartment. Defer to the experimental curator while retaining the original paper’s Methods-access limit; this does not assign the same localization to every short product.

Summary: The electronic sarcolemma assertion agrees with direct human evidence.

Reason: The target matches the current ARBA00087592 branch, and the source also includes ortholog and curated subcellular-location mappings. Direct human skeletal and atrial muscle observations independently establish the sarcolemmal pool. Rule matching is provenance, not a substitute for those experiments.

Summary: Dystrophin expression marks muscle-cell differentiation in a regenerative model.

Reason: The rat donor PMID:19903098 uses dystrophin expression among muscle differentiation readouts in an intervention/transplantation setting. Retain the contextual IEP assertion with its observational scope. It does not establish that dystrophin is the upstream inducer of myogenesis or that altered expression proves a new catalytic function.

Summary: Dystrophin products have neuronal cell-body pools.

Reason: The rat donor records include PMID:10359335 and PMID:11368101, which distinguish retinal or brain dystrophin products and report broad neuronal/glial cytoplasmic distributions. Retain the contextual cell-body location; neither historical Dp nomenclature nor antibody recognition alone identifies all current human products.

Summary: Dystrophin contributes to the costameric network.

Reason: PMID:16000376 combines human N-terminal binding assays with muscle localization and perturbation of the keratin-linked costameric network in rat muscle. The actual evidence supports costamere localization and mechanical linkage; it is not evidence that dystrophin is a peptide-producing enzyme.

Summary: The original experiments support dystrophin binding and structural organization, not participation in peptide biosynthesis.

Reason: The complete relevant Methods and Results of PMID:16000376 concern expressed human dystrophin fragments, keratin 19 binding, microscopy and costameric perturbation. GO:0043043 describes reactions and pathways forming peptides. Production of experimental constructs is performed by the expression system, and the assayed dystrophin fragments perform binding and structural linkage. The source therefore does not establish a peptide-biosynthetic role for DMD; the positive binding and muscle-structure results are retained elsewhere.

Summary: Dystrophin is re-expressed during skeletal-muscle regeneration.

Reason: PMID:12086334 follows rat muscle after cardiotoxin-induced myonecrosis. Sarcolemmal dystrophin staining returns during regenerating-fiber maturation, with a time course distinct from other DGC components. Retain the developmental-expression annotation as contextual; it is not a demonstration that dystrophin initiates the regenerative program or catalyzes regeneration.

Summary: The broad system-process regulation is resolved into supported muscle calcium-control contexts.

Reason: The current ARBA00026855 branch matches DMD but supplies a broad regulatory label. The source-specific mouse studies PMID:19198614 and PMID:20080623 substantiate skeletal and cardiac contraction regulation through calcium-release phenotypes. Use those two verified descendants to retain both physiological contexts, without making dystrophin a calcium channel or a direct ryanodine-receptor regulator.

Proposed replacements: regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

Summary: Dystrophin is present at a retinal neuronal-terminal compartment.

Reason: The mouse donor PMID:12115694 examines retinal dystrophin localization relative to neuronal/synaptic markers, supporting the terminal compartment in the original context. Retain this non-core location without conflating photoreceptor terminals with every neuronal or glial product pool.

Summary: Dystrophin is present at a retinal neuronal-terminal compartment.

Reason: The mouse donor PMID:12115694 examines retinal dystrophin localization relative to neuronal/synaptic markers, supporting the terminal compartment in the original context. Retain this non-core location without conflating photoreceptor terminals with every neuronal or glial product pool.

Summary: Dystrophin associates with keratin-containing cytoskeletal assemblies.

Reason: The rat source PMID:15247274 reports K8/K19 in striated muscle, dystrophin–K19 co-immunoprecipitation/co-purification and construct association. This supports the existing complex-binding assertion in context. It does not imply that DMD binds every macromolecular complex or identify all components as direct interfaces; the independently demonstrated human keratin-binding activity is represented separately.

Summary: A dystrophin-containing complex partitions with membrane rafts.

Reason: PMID:11259414 analyzes caveolin-3-deficient mouse muscle and the exclusion of dystrophin-complex components from raft fractions; PMID:8663016 independently describes muscle DGC/caveolin co-fractionation and association. Retain the contextual raft-associated pool without assigning caveolin activity or interpreting detergent fractionation as an exclusive membrane topology.

Summary: A dystrophin-containing complex partitions with membrane rafts.

Reason: PMID:11259414 analyzes caveolin-3-deficient mouse muscle and the exclusion of dystrophin-complex components from raft fractions; PMID:8663016 independently describes muscle DGC/caveolin co-fractionation and association. Retain the contextual raft-associated pool without assigning caveolin activity or interpreting detergent fractionation as an exclusive membrane topology.

Summary: The synaptic inheritance is supported with a more precise postsynaptic localization.

Reason: The literal synapse IBD at PTN008535380 lies on the target lineage and is grounded in mouse/rat experimental descendants. Rat PSD fractionation and mouse postsynaptic localization support the more informative postsynaptic-density and postsynaptic-membrane pools, both within synapse by typed ancestry. Preserve the inherited synaptic function while avoiding a presynaptic-vesicle inference or assignment of all products to one synapse class.

Proposed replacements: postsynaptic density postsynaptic membrane

Summary: The muscle-synapse context supports a postsynaptic membrane pool.

Reason: The mouse donor PMID:10995443 examines neuromuscular synapses in alpha-syntrophin deficiency, alongside dystrophin/utrophin complex organization. The established dystrophin postsynaptic pool is more informative than generic synapse, with independent localization corroboration. Do not attribute the alpha-syntrophin knockout phenotype specifically to DMD or conflate utrophin loss with absence of dystrophin.

Proposed replacements: postsynaptic membrane

Summary: The muscle-synapse context supports a postsynaptic membrane pool.

Reason: The mouse donor PMID:10995443 examines neuromuscular synapses in alpha-syntrophin deficiency, alongside dystrophin/utrophin complex organization. The established dystrophin postsynaptic pool is more informative than generic synapse, with independent localization corroboration. Do not attribute the alpha-syntrophin knockout phenotype specifically to DMD or conflate utrophin loss with absence of dystrophin.

Proposed replacements: postsynaptic membrane

Summary: Dystrophin has a postsynaptic membrane pool.

Reason: The curated subcellular-location mapping is consistent with mammalian postsynaptic localization studies, including PMID:9284362 and the product-resolved mouse study PMID:35098363. Retain the contextual neural pool while distinguishing long and short products and not imposing one neuronal subtype or inhibitory-synapse assignment on every product.

Summary: Postsynaptic membrane association is supported in the ortholog source.

Reason: PMID:9284362 reports electron-microscopic dystrophin-family localization in mouse superior cervical ganglion, including postsynaptic and adherens-junction regions and residual short-product signals in mdx animals. Retain the contextual transfer with product and tissue limits, not an exclusive localization or proof that every antibody signal is the full-length product.

Summary: The direction of the neuronal-differentiation effect cannot be generalized from the accessible engineered-product study.

Reason: PMID:21668890 reports faster differentiation after overexpression of engineered Dp71 lacking exons 78–79, with changes in endogenous dystrophin/utrophin and other markers. The complete original was not recovered. These observations are compatible with context-dependent regulation but do not resolve whether a native human DMD product negatively regulates differentiation. Preserve the curator claim and engineered positive result as unresolved rather than declaring it a contradiction of the positive Dp71 loss-of-function studies.

Summary: Dp71 supports neuronal differentiation under the tested induction conditions.

Reason: PMID:15149856 reports that reducing Dp71 in rat PC12 cells suppresses neurite outgrowth and late differentiation-marker induction while leaving early NGF responses intact. Retain the contextual positive role without assigning a growth-factor receptor, kinase or universal neurodevelopmental mechanism.

Summary: Dystrophin contributes to muscle-cell integrity and homeostasis.

Reason: The literal mouse experimental grounding includes the mdx phenotype in PMID:6583703; the conserved membrane–cytoskeleton anchoring role provides a coherent structural basis for muscle-cell homeostasis. Retain this physiological consequence as non-core relative to the molecular anchor, without treating every downstream metabolic or inflammatory change as a distinct DMD activity.

Summary: A short dystrophin product is enriched in perinuclear cytoplasm.

Reason: PMID:11368101 explicitly reports stronger rat-brain Dp71f cytoplasmic labeling near the nucleus, diminishing toward the cell periphery. Retain the contextual perinuclear location; do not convert it into nuclear localization or assign a precise current human isoform from the historical name alone.

Summary: The inherited neuronal-development role can be represented by projection morphogenesis.

Reason: The literal IBD at PTN008535380 is on the target lineage, with rat descendant experimental grounding rather than a pairwise donor-count argument. Rat Dp71 perturbation studies PMID:15149856 and PMID:15706226 specifically resolve neurite/projection development and morphology. Neuron projection morphogenesis is a verified descendant of neuron development and retains the supported structural developmental role without inventing a neuronal fate-specification activity.

Proposed replacements: neuron projection morphogenesis

Summary: Dp71 supports neuronal projection morphology through a cellular adhesion context.

Reason: PMID:15706226 compares rat PC12 cells with reduced Dp71 and reports deficient neurite outgrowth, reduced attachment to integrin-dependent substrates and loss of filopodial projections. Retain this contextual morphogenesis role, while recognizing that the study links adhesion and morphology rather than resolving a direct actin-polymerization or growth-factor-transduction mechanism.

Summary: Native direct nNOS binding is unresolved alongside positive human complex association.

Reason: PMID:27225184 establishes reciprocal co-immunoprecipitation and colocalization of dystrophin and nNOS in human atrial material, which does not isolate a binary interface. PMID:26378238 reports binding of purified dystrophin R16–17 fragments to an immobilized nNOS PDZ construct by biolayer interferometry, with an equilibrium dissociation constant of about 50 micromolar and multiphasic kinetics; the atomic interface is modeled. PMID:29790927 independently shows that human dystrophin-repeat peptides capture syntrophins from mouse muscle and that microdystrophin restores sarcolemmal nNOS only when alpha-syntrophin is present. That physiological recruitment experiment does not repeat or refute the earlier purified-fragment binding assay. The contribution of a direct contact in the native human complex remains unresolved.

Summary: The direct NOS-binding mechanism remains unresolved across source and construct contexts.

Reason: The positive PMID:7545544 abstract establishes DGC-associated nNOS and dystrophin-dependent sarcolemmal localization, while its original Methods remain inaccessible. Human atrial co-immunoprecipitation in PMID:27225184 corroborates association. PMID:26378238 reports binding of purified dystrophin R16–17 fragments to an immobilized nNOS PDZ construct by biolayer interferometry, with an equilibrium dissociation constant of about 50 micromolar and multiphasic kinetics; the atomic interface is modeled. PMID:29790927 independently shows that human dystrophin-repeat peptides capture syntrophins from mouse muscle and that microdystrophin restores sarcolemmal nNOS only when alpha-syntrophin is present. That physiological recruitment experiment does not repeat or refute the earlier purified-fragment binding assay. The contribution of a direct contact in the native human complex remains unresolved.

Summary: The inherited muscle-cell-development claim is retained as a developmental context.

Reason: The exact IBD at PTN008535380 lies on the human target lineage and was placed using mouse/zebrafish descendant evidence. Mouse genetic and dystrophic-muscle studies provide developmental/maintenance context, including PMID:8007658. Retain the curator’s ancestral judgment without treating the number of current donor rows as its strength or assigning a direct differentiation enzyme to DMD.

Summary: Muscle-cell development is a supported ortholog context rather than a distinct DMD activity.

Reason: The mouse donor has genetic/dystrophic-muscle evidence, including PMID:8007658 and PMID:20716577. Their accessible abstracts describe complex disease and genetic-interaction contexts, not a purified DMD developmental mechanism. Retain the physiologically coherent source assertion with curator deference and keep it non-core relative to dystrophin’s structural linkage.

Summary: The precise contraction assertion remains unresolved from the accessible clinical source.

Reason: PMID:19027585 reports ECG abnormalities in mutation-positive young DMD patients. The full original was unavailable, so the measured contractility endpoint underlying this IMP annotation could not be inspected. Clinical cardiac involvement is real, but electrical abnormalities are not silently substituted for a directly inspected contraction assay. Retain uncertainty without rejecting the curator’s full-text judgment.

Summary: Dystrophin acts as a molecular adaptor in the membrane–cytoskeleton assembly.

Reason: The literal IBD for molecular adaptor activity lies at Eukaryota PTN000263007 on the target lineage, with rat beta-dystrobrevin descendant grounding. This is a considered ancestral placement, not a single-pair transfer. Independent human dystrophin domain binding and native DGC architecture establish that DMD links multiple components into a coordinated structural assembly. Retain the broad adaptor function without treating every high-throughput partner as a functional signaling interface or requiring the target to be the same protein as the donor.

Summary: Dystrophin organizes a membrane-associated protein assembly, while the cited channel-complex phenotype is downstream.

Reason: PMID:19198614 measures RyR/calstabin-complex remodeling after dystrophin loss and its pharmacological stabilization; it does not identify DMD as the assembler of that channel complex. Independent targeted experiments in PMID:9214383 show that a Δ71–74 dystrophin transgene in mdx muscle restores sarcolemmal dystrobrevin and α1/β1-syntrophins, which co-purify in the restored complex. Together with mapped dystrophin binding interfaces, this supports a structural recruitment/organization role in DGC assembly at gene level. Retain the broad assembly claim as non-core on that independent basis, while preserving the original source identity and its downstream channel-specific limit. Exact syntrophin stoichiometry and the proposed recruitment arrangement were not established by purified ternary reconstitution.

Summary: Dystrophin organizes a membrane-associated protein assembly, while the cited channel-complex phenotype is downstream.

Reason: PMID:19198614 measures RyR/calstabin-complex remodeling after dystrophin loss and its pharmacological stabilization; it does not identify DMD as the assembler of that channel complex. Independent targeted experiments in PMID:9214383 show that a Δ71–74 dystrophin transgene in mdx muscle restores sarcolemmal dystrobrevin and α1/β1-syntrophins, which co-purify in the restored complex. Together with mapped dystrophin binding interfaces, this supports a structural recruitment/organization role in DGC assembly at gene level. Retain the broad assembly claim as non-core on that independent basis, while preserving the original source identity and its downstream channel-specific limit. Exact syntrophin stoichiometry and the proposed recruitment arrangement were not established by purified ternary reconstitution.

Summary: Dystrophin organizes a membrane-associated protein assembly, while the cited channel-complex phenotype is downstream.

Reason: PMID:20080623 measures RyR/calstabin-complex remodeling after dystrophin loss and its pharmacological stabilization; it does not identify DMD as the assembler of that channel complex. Independent targeted experiments in PMID:9214383 show that a Δ71–74 dystrophin transgene in mdx muscle restores sarcolemmal dystrobrevin and α1/β1-syntrophins, which co-purify in the restored complex. Together with mapped dystrophin binding interfaces, this supports a structural recruitment/organization role in DGC assembly at gene level. Retain the broad assembly claim as non-core on that independent basis, while preserving the original source identity and its downstream channel-specific limit. Exact syntrophin stoichiometry and the proposed recruitment arrangement were not established by purified ternary reconstitution.

Summary: Dystrophin deficiency changes cardiac electrical behavior.

Reason: PMID:21677768 provides mouse cardiac electrophysiological evidence linking dystrophin deficiency to altered electrical behavior. The source distinguishes ion-channel current/gating and arrhythmia outcomes from the membrane structural protein itself. Retain the contextual action-potential role without assigning channel conductance, voltage sensing or autonomous electrogenic activity to DMD.

Summary: Dystrophin deficiency changes cardiac electrical behavior.

Reason: PMID:20080623 provides mouse cardiac electrophysiological evidence linking dystrophin deficiency to altered electrical behavior. The source distinguishes ion-channel current/gating and arrhythmia outcomes from the membrane structural protein itself. Retain the contextual action-potential role without assigning channel conductance, voltage sensing or autonomous electrogenic activity to DMD.

Summary: Dystrophin deficiency changes cardiac electrical behavior.

Reason: PMID:21677768 provides mouse cardiac electrophysiological evidence linking dystrophin deficiency to altered electrical behavior. The source distinguishes ion-channel current/gating and arrhythmia outcomes from the membrane structural protein itself. Retain the contextual action-potential role without assigning channel conductance, voltage sensing or autonomous electrogenic activity to DMD.

Summary: The inherited muscle-regulatory role has supported cardiac and skeletal calcium-control refinements.

Reason: The exact IBD at PTN008535380 is on the target lineage with mouse/rat descendant grounding. Source-specific studies PMID:19198614 and PMID:20080623 resolve skeletal and cardiac contraction regulation through altered calcium release. Both proposed terms are typed descendants of regulation of muscle system process. The refinement preserves both physiological contexts while keeping the direct molecular core as membrane–cytoskeleton linkage.

Proposed replacements: regulation of skeletal muscle contraction by regulation of release of sequestered calcium ion regulation of cardiac muscle contraction by regulation of the release of sequestered calcium ion

Summary: Dp71 affects a late cellular response to neuronal differentiation stimuli.

Reason: PMID:15149856 explicitly separates normal early NGF responses, including ERK1/2 activation and growth arrest, from defective neurite outgrowth and late MAP2 induction in Dp71-reduced PC12 cells. Retain the broad contextual regulation-of-response claim with that timing distinction; do not assert direct NGF receptor signaling, impaired early ERK activation or a newly identified kinase activity.

Summary: Dystrophin-family proteins occupy perivascular astrocytic processes.

Reason: PMID:10411999 uses light/electron microscopy with a long-and-short-product-reactive antibody in rat brain and reports strong pericapillary endfoot staining. Retain the contextual astrocyte-projection location, without resolving the signal to one current human product or inferring a specific mitochondrial membrane site.

Summary: The ortholog evidence identifies a product- and cell-type-specific inhibitory postsynapse pool.

Reason: PMID:35098363 uses a Dp71-specific HA knock-in mouse and distinguishes Dp71 at dentate-granule inhibitory postsynapses from Dp427 at CA1 inhibitory postsynapses. Retain postsynaptic localization with these product and neuronal-type limits. It is not a claim that every human product is restricted to inhibitory synapses.

Summary: A dystrophin-product pool participates in a GABAergic synaptic compartment.

Reason: PMID:35098363 directly distinguishes inhibitory postsynaptic Dp71/Dp427 pools in mouse hippocampal cell types. Retain the contextual GABAergic-synapse assignment, without converting colocalization/complex membership into GABA-receptor activity or assigning the same pool to all natural products.

Summary: The postsynaptic specialization is more precisely represented as a postsynaptic density.

Reason: The mouse source PMID:9284362 identifies postsynaptic specializations by electron microscopy; independent rat PSD fractionation in PMID:1454857 corroborates dystrophin within that structure. Postsynaptic density is a typed descendant of postsynaptic specialization. Retain the finer supported compartment, with tissue/product limits and without confusing it with synaptic-vesicle membrane.

Proposed replacements: postsynaptic density

Summary: The exact matrix-facing inner-membrane topology is unresolved.

Reason: The rat donor PMID:10913331 explicitly describes an immunoreactive mitochondrial Dp71f-like protein whose identity was not established as Dp71f, with persistence in mdx3Cv. Its full topology experiment was not recovered. The independent human mitochondrial-fraction study PMID:34575126 strengthens the case for a mitochondrial dystrophin-family pool but does not resolve which membrane face it occupies. Preserve the precise source claim as unresolved; neither a universal absence nor a false identification is asserted.

Summary: Dystrophin-dependent membrane organization affects sodium currents.

Reason: PMID:21677768 compares mouse mdx, mdx/utrophin-deficient and control cardiomyocytes. It measures reduced sodium-current density and altered calcium-current behavior, with additional utrophin-dependent effects distinguished from dystrophin loss. Retain the physiological regulatory contribution without assigning ion conductance to DMD or attributing every double-mutant gating change to dystrophin alone.

Summary: Dystrophin-dependent membrane organization affects sodium currents.

Reason: PMID:21677768 compares mouse mdx, mdx/utrophin-deficient and control cardiomyocytes. It measures reduced sodium-current density and altered calcium-current behavior, with additional utrophin-dependent effects distinguished from dystrophin loss. Retain the physiological regulatory contribution without assigning ion conductance to DMD or attributing every double-mutant gating change to dystrophin alone.

Summary: Dystrophin-dependent membrane organization affects calcium currents.

Reason: PMID:21677768 compares mouse mdx, mdx/utrophin-deficient and control cardiomyocytes. It measures reduced sodium-current density and altered calcium-current behavior, with additional utrophin-dependent effects distinguished from dystrophin loss. Retain the physiological regulatory contribution without assigning ion conductance to DMD or attributing every double-mutant gating change to dystrophin alone.

Summary: Dystrophin-dependent membrane organization affects calcium currents.

Reason: PMID:21677768 compares mouse mdx, mdx/utrophin-deficient and control cardiomyocytes. It measures reduced sodium-current density and altered calcium-current behavior, with additional utrophin-dependent effects distinguished from dystrophin loss. Retain the physiological regulatory contribution without assigning ion conductance to DMD or attributing every double-mutant gating change to dystrophin alone.