The binding records and direct decisions preserve each complete source annotation and its zero-based review index. Methods distinguish purified interactions, co-association, screening, localization and inferred structural roles. Supported specific binding terms refine measured interactions, including the five BMP/GDF prodomains and the measured human fibronectin interaction; other retained generic protein-binding records remain non-core in this review. Further extracellular-matrix partner-class refinements were not adjudicated in this focused follow-up. Inaccessible target evidence remains undecided. No publication quotations are added.
Microfibril structure supports a matrix-level contribution to elasticity. The elasticity annotation is an IC inference, not a claim that the cited microscopy measured isolated fibril recoil. The broader structural-constituent role remains informative for elastin-free anchorage and growth-factor scaffolding. Integrin binding supplies an extracellular adhesive ligand; it is not merely a downstream perturbation phenotype.
Basement-membrane findings vary by tissue and assay. Microfibril insertion at the basal-lamina interface, noncollagenous basement-zone association and reported lamina-densa deposition should not be collapsed into either uniform residence or universal absence. The inaccessible epithelial paper retains its positive abstract and explicit access limit.
Proteomics evidence is evaluated at the target-record level. Human aortic and cultured-matrix main tables, colon/liver Additional File 2, atrial Table 1 and the breast/omental ACS workbook contain explicit fibrillin-1 records. Mixed-accession protein groups are preserved. The endothelial, cell-derived-matrix and vein papers retain uncertainty where exact supplementary records were inaccessible; this is not evidence of target absence. RCA structural classification is an inference consistent with independent scaffold biology, not a direct mechanics assay.
A novel mutation of the fibrillin gene causing ectopia lentis.
Read locus: Human family genetics; operative original unavailable.
Citation identity checked against the genuine fetched record. Human family FBN1 mutation cosegregates with ectopia lentis; abstract discusses skeletal manifestations. Cannot resolve source-specific skeletal-development IMP experiments from accessible material. Missing evidence is not proof that the annotation is false. Source guide records the bounded original read and any supplementary limits.
Ultrastructural distribution of 36-kD microfibril-associated glycoprotein (MAGP-36) in human and bovine tissues. — accessed original
Read locus: Human skin double immunogold electron microscopy; Methods and Figure 3.
Citation identity checked against the genuine fetched record. Human normal skin from the margin of a surgical specimen is distinguished from bovine specimens. Pre-embedding double immunogold identifies FBN1 on microfibrils. No complete paper or quantitative particle counting was performed; the MAGP36 elastin-interface pattern is not the distribution of all FBN1. Source guide records the bounded original read and any supplementary limits.
Latent transforming growth factor beta-binding protein 1 interacts with fibrillin and is a microfibril-associated protein. — accessed original
Read locus: Recombinant protein binding; Matrix immunolocalization.
Citation identity checked against the genuine fetched record. Recombinant human FBN1 N-terminal fragments bind human LTBP1 C-terminal fragments and human LTBP4 C-terminal fragment. Human tissue immunolocalization and extracted microfibrils independently support FBN1 as a microfibril component. LTBP1 nonretention in extracted microfibrils is not a negative FBN1 result. Partner accession B7ZLY3 maps to human LTBP1 in the genuine UniProt response; no separately demonstrated natural isoform-specific function is inferred from that identifier or Q14766-2. Source guide records the bounded original read and any supplementary limits.
Purification and partial characterization of fibrillin, a cysteine-rich structural component of connective tissue microfibrils. — accessed original
Read locus: Human fibroblast-medium purification; Monoclonal antibody electron microscopy; Figure 7.
Citation identity checked against the genuine fetched record. Purified human cell-medium FBN1 is characterized biochemically; two distinct monoclonal antibodies label tissue microfibrils in periodic single- and double-band patterns. Molecular dimensions and tissue labeling support a structural microfibril constituent, not a newly assigned enzymatic function. Separate full figure pixels not inspected. Source guide records the bounded original read and any supplementary limits.
Read locus: Human skin/fibroblast microscopy; Co-immunoprecipitation.
Citation identity checked against the genuine fetched record. Human dermal fibroblast FBN1 networks are detected with anti-human fibrillin-1 after MFAP4 perturbation; secreted FBN1 amount is distinguished from network assembly. Anti-MFAP4 immunoprecipitation from concentrated NHDF culture medium detects FBN1 by Western blot (Results/Figure 6, line 103; IP Methods line 203), with normal rabbit IgG control. The co-IP is association in culture medium, not a purified binary-binding experiment despite the paper discussion using direct-interaction language. Skin xenografts are human tissue in mice; MFAP4 perturbation outcomes are not automatically FBN1-specific process functions. Source guide records the bounded original read and any supplementary limits.
Fibrillin, a new 350-kD glycoprotein, is a component of extracellular microfibrils.
Read locus: Human protein immunoisolation; Human tissue immunoelectron microscopy; Figures 8–12.
Citation identity checked against the genuine fetched record. Human fibroblast medium immunoisolation and biochemical characterization establish secreted fibrillin; cultured human amniocyte/fibroblast/MG63 matrices stain positively. Human skin immunogold electron microscopy directly localizes fibrillin to approximately 10-nm microfibrils, both around elastin cores and in bundles lacking those cores. At the human dermal–epidermal junction, labeled microfibrillar bundles approach and appear to insert into the basal lamina. Figure 9 explicitly describes lamina densa and anchoring fibrils as unlabeled apart from the inserting labeled microfibrils. Do not restate broad basement-membrane source annotation as uniform fibrillin throughout lamina densa. Positive microfibril/basement-zone association remains real. Source guide records the bounded original read and any supplementary limits.
Read locus: Human tissue immunolocalization described in abstract; operative original unavailable.
Citation identity checked against the genuine fetched record. Human tissue study explicitly uses fibrillin antibody counterstaining alongside fibulin-1. Operative fibrillin Methods/Results and figures unavailable; title naming fibulin is not wrong-gene evidence. Source guide records the bounded original read and any supplementary limits.
Structure and expression of fibrillin-2, a novel microfibrillar component preferentially located in elastic matrices. — accessed original
Read locus: Human fetal tissue immunohistochemistry; Bovine ligament immunoelectron microscopy; Figures 5–9; IC structural inference.
Citation identity checked against the genuine fetched record. Human fetal tissues show FBN1 connective-tissue localization; bovine ligament Figure 5 demonstrates microfibril-associated FBN1 separately from amorphous elastin. The source discusses microfibrils as contributors to tissue biomechanical properties. Elasticity is an IC inference from the microfibrillar scaffold, not a direct force/recoil assay. GO:0030023 concerns matrix recoil and does not require isolated fibrillin itself to behave as elastin. Both fibrillins are tested; title emphasis on FBN2 is not a citation defect. Source guide records the bounded original read and any supplementary limits.
Cell adhesion to fibrillin-1 molecules and microfibrils is mediated by alpha 5 beta 1 and alpha v beta 3 integrins. — accessed original
Read locus: Recombinant human fragment cell-adhesion assays; Integrin-blocking antibodies and RGD-mutant controls.
Citation identity checked against the genuine fetched record. Human FBN1 PF9/PF11 fragments support attachment/spreading of human dermal fibroblasts and other human cell lines. RGD-mutant controls and function-blocking alpha5beta1/alphavbeta3 antibodies support integrin-dependent adhesion. Fibronectin-blocking controls and early time points distinguish the recombinant FBN1 interaction from an obligatory fibronectin bridge. Native microfibrils in the comparison are from bovine fetal aorta; recombinant human FBN1 assays are distinct. Bounded recovered operative text, not a complete downloaded original PDF. Source guide records the bounded original read and any supplementary limits.
Read locus: Human fragment structure; Purified human integrin surface plasmon resonance; Cell adhesion.
Citation identity checked against the genuine fetched record. Human FBN1 cbEGF22-TB4-cbEGF23 crystal structures directly resolve calcium binding; fragments were expressed/refolded in bacteria. SPR uses native human placental alpha-v-beta-3 and alpha-5-beta-1 integrins, with negative fragment/control subtraction. Alpha-v-beta-3 binding and differential dissociation are directly measured. The fibrillin-integrin complex is a docking model, not an experimentally resolved co-crystal. No alpha-5-beta-1 binding in these particular fragments/conditions does not negate binding by other FBN1 constructs in other papers. Source guide records the bounded original read and any supplementary limits.
Read locus: Integrin binding/adhesion described in abstract; operative original unavailable.
Citation identity checked against the genuine fetched record. Abstract reports alphaVbeta6 and alpha5beta1 receptor interactions and human keratinocyte/fibroblast comparisons. No original operative assay/control/target construct details were accessible; preserve source-specific uncertainty despite independent integrin evidence. Source guide records the bounded original read and any supplementary limits.
Proteomics characterization of extracellular space components in the human aorta.
Read locus: Human aortic fractionation and mass spectrometry; main Tables I/II.
Citation identity checked against the genuine fetched record. Human nonpathologic ascending-aorta ECM fractions contain FBN1_HUMAN: Table I reports 10 unique peptides and Table II 15, with spectra/coverage columns retained. Sequential NaCl/SDS/guanidine extraction and human-database mass spectrometry identify the matrix constituent. RCA structural-constituent classification is an inference from ECM identity and known scaffold biology, not a mechanical assay. Fractions are biochemical enrichments, not pure subcellular compartments. Source guide records the bounded original read and any supplementary limits.
Read locus: Human endothelial ECM proteomics; supplementary target unresolved.
Citation identity checked against the genuine fetched record. The paper directly isolates seven-day human endothelial-cell matrix and identifies proteins by mass spectrometry. Exact FBN1 supplementary target join is unresolved at this read checkpoint. Whole-cell SILAC and CLEC14A interaction assays are distinct and cannot substitute for a target ECM record. Source guide records the bounded original read and any supplementary limits.
Read locus: Human colon/liver ECM proteomics; Additional File 2, sheets A/B row 5.
Citation identity checked against the genuine fetched record. Serially enriched ECM from matched human colon/colon tumor/liver metastasis and pooled normal human liver is analyzed with a human protein database. Matrisome structural classification is not a direct recoil or mechanical assay. Exact supplementary accession groups must be retained; a group containing FBN2 is not uniquely discriminating FBN1 peptide evidence. Source guide records the bounded original read and any supplementary limits.
Glycoproteomics Reveals Decorin Peptides With Anti-Myostatin Activity in Human Atrial Fibrillation.
Read locus: Human atrial ECM glycoproteomics; main Table 1 Fibrillin-1 row.
Citation identity checked against the genuine fetched record. Human left/right atrial appendage ECM is isolated by NaCl/SDS/guanidine extraction and glycoprotein enrichment for proteomics. Decorin functional assays are not FBN1 functional assays. Lectin/solubility biases preclude interpreting missing fractions as negative localization. Source guide records the bounded original read and any supplementary limits.
Comprehensive proteomic characterization of stem cell-derived extracellular matrices.
Read locus: Human cell-derived matrix proteomics; Table I label ambiguity, exact supplementary target unresolved.
Citation identity checked against the genuine fetched record. Human bone/adipose mesenchymal stromal cells and neonatal dermal fibroblasts deposit matrices that are decellularized and analyzed by mass spectrometry. The preparation contains some insoluble intracellular contaminants. Main-table fibrillin/fibulin name/symbol inversion requires an exact accession join; do not infer wrong gene or reliable FBN1 detection from the ambiguous label alone. Source guide records the bounded original read and any supplementary limits.
Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics. — accessed original
Read locus: Human breast/omental ECM proteomics; original SI sheets B/C/D, including B row 4.
Citation identity checked against the genuine fetched record. Human ovarian omental metastasis/normal omentum and breast tumor/adjacent breast ECM are enriched and profiled by mass spectrometry. Crude and urea-soluble preparations differ. Matrisome classification does not establish a disease-specific FBN1 mechanism; mixed fibrillin protein groups must remain distinct from sole-FBN1 records. Source guide records the bounded original read and any supplementary limits.
Read locus: Calcium binding described in abstract; operative original unavailable.
Citation identity checked against the genuine fetched record. Abstract explicitly reports calcium binding of fibrillin and human FBN1 cDNA/domain characterization. The actual calcium-binding experiment was unavailable. Independent calcium evidence is not verification of this particular assay. No alternate-product function is inferred from 5-prime transcript variants. Source guide records the bounded original read and any supplementary limits.
Read locus: Human FBN1–bovine MAGP1/2 binding assays.
Citation identity checked against the genuine fetched record. Both MAGP1 and MAGP2 bind human FBN1 N-terminal fragments, so the MAGP2 title does not exclude the MAGP1 context. Human FBN1 constructs derive from placental cDNA and are expressed in 293-EBNA cells. Native MAGPs and tissue microfibrils are from bovine nuchal ligament; the GOA partners P27424/Q28022 are bovine MFAP2/MFAP5. Species remain explicit; no human-human native assay is inferred. Some fragment interactions are assay dependent (SDS-sensitive MAGP2 interaction); negative C-terminal fragment results do not negate positive N-terminal binding. Source guide records the bounded original read and any supplementary limits.
Molecular structure and interaction of recombinant human type XVI collagen.
Read locus: Human collagen XVI interaction described in abstract; operative original unavailable.
Citation identity checked against the genuine fetched record. Abstract explicitly reports recombinant human collagenXVI interaction with FBN1. Cannot inspect the binding assay or protein controls. An erratum is listed but was not read; no retraction or corrected-result claim is made. Source guide records the bounded original read and any supplementary limits.
Fibulin-5 interacts with fibrillin-1 molecules and microfibrils.
Read locus: Purified human solid-phase binding; Binding-inhibition assays.
Citation identity checked against the genuine fetched record. Human recombinant FBN1 fragments bind FBLN5 in solid-phase assays; the SPR negative is explicitly attributed to immobilization limitations. Human tropoelastin–FBN1 PF2/PF7 interaction is directly measured in the inhibition experiment, Figure 3C/D and Methods line 94. Zonule microfibril mass mapping supports additional fibulin binding; no simultaneous physiological ternary complex or new activity inferred. Source guide records the bounded original read and any supplementary limits.
LTBP-2 specifically interacts with the amino-terminal region of fibrillin-1 and competes with LTBP-1 for binding to this microfibrillar protein. — accessed original
Read locus: Purified human protein overlay; Radioligand binding; Figure 5.
Citation identity checked against the genuine fetched record. Purified human LTBP2 binds human FBN1 fragments by overlay/radioligand binding; human LTBP1 is also tested. Figure 5 distinguishes positive C-terminal binding and reported affinities. Competition and matrix association do not measure a direct TGF-beta signaling response. Tested recombinant fragments do not establish every natural splice-product function. Source guide records the bounded original read and any supplementary limits.
Targeting of bone morphogenetic protein growth factor complexes to fibrillin.
Read locus: Recombinant FBN1 and growth-factor-prodomain binding; original Results, Figure 6A–B caption and Table 3. The recovered author-uploaded original supplies these locators; the committed cache is abstract-only.
Citation identity checked against the genuine fetched record. Human FBN1 N-terminal recombinant rF23 binds BMP2/BMP4/BMP7/BMP10/GDF5 prodomains by SPR; Figure 6A–B identifies the constructs and interaction sensorgrams, and Table 3 lists the individual affinities. The caption/table text was read; no additional figure-pixel inspection is claimed. Human GDF5 prodomain is generated from human-cell cDNA (Table 1 NM_000557); purchased mature mouse GDF5 is a separate reagent. These are prodomain interactions, not proof of binding every mature free growth-factor dimer. Mouse tissue BMP localization is separate from recombinant human-binding data; no FBN1 growth-factor catalytic/receptor activity is inferred. Source guide records the bounded original read and any supplementary limits.
Read locus: Recombinant human protein surface plasmon resonance; Competition assays.
Citation identity checked against the genuine fetched record. Human FBN1 rF23 binds human fibulin2/4/5, LTBP1 rL1K and LTBP4 rL4K by SPR; Table 1 separately specifies every partner. The hybrid/EGF region changes affect the partners differently, and LTBP1 competes with fibulin binding. These are specific recombinant interactions, not evidence for a single simultaneous stable complex containing every listed partner. Mouse knockout matrix deposition is distinguished from purified human protein binding. Source guide records the bounded original read and any supplementary limits.
Differential regulation of elastic fiber formation by fibulin-4 and -5.
Read locus: Human purified-protein solid-phase binding; Surface plasmon resonance.
Citation identity checked against the genuine fetched record. Human FBN1 fragments bind human fibulin-4 by SPR/solid-phase and fibulin-5 by solid-phase assays. Human unprocessed LOX binds FBN1 in solid-phase assays (reported KD 26 ± 11 nM); SPR nonbinding is assay-orientation dependent. Purified binding does not confer lysyl-oxidase activity on FBN1. No native isoform specificity is inferred. Source guide records the bounded original read and any supplementary limits.
Read locus: Purified human overlay and reciprocal surface plasmon resonance; Human tissue immunolocalization.
Citation identity checked against the genuine fetched record. Purified human ADAMTS10 binds recombinant human FBN1 regions in overlay and reciprocal SPR; Table 1 distinguishes positive affinities and tested controls. Human skin/zonule immunolocalization supports association with FBN1 microfibrils. ADAMTS10 preparation includes oligomeric/processed forms; the assay does not confer protease function on FBN1. ADAMTS10 absence near the lamina densa is not FBN1 absence; FBN1 fibrils span the interface. Source guide records the bounded original read and any supplementary limits.
Fibrillin-1 directly regulates osteoclast formation and function by a dual mechanism.
Read locus: Soluble human FBN1 fragments in mouse osteoclast assays; RANKL binding and competition; Fragment/immobilization controls.
Citation identity checked against the genuine fetched record. Soluble human FBN1 N-terminal fragments inhibit mouse RAW264.7/marrow osteoclast differentiation; rF31 administration reduces TRAP-positive cells in mice. The N-terminal half binds GST-RANKL in a calcium-dependent solid-phase assay; excess RANKL reverses its inhibition. The shorter rF23 fragment does not bind RANKL and instead changes calcium/NFATc1 signaling. Mineral-immobilized N-terminal half does not inhibit differentiation; effects cannot be generalized to all assembled matrix. Source guide records the bounded original read and any supplementary limits.
Heparin/heparan sulfate controls fibrillin-1, -2 and -3 self-interactions in microfibril assembly.
Read locus: Original Methods 2.2 (human plasma fibronectin), Results 3.3 and Figure 3B caption (human FBN1 N- and C-terminal fragment binding). These passages were recovered from the indexed publisher original; the committed cache remains abstract-only.
Citation identity checked against the genuine fetched record. Recombinant human FBN1/FBN2 and human plasma fibronectin are tested in solid-phase homo/heterotypic binding assays. Figure 3A distinguishes fibrillin self/heterotypic interactions from Figure 3B fibronectin binding. The positive FBN1–fibronectin context is refined to GO:0001968 fibronectin binding. Heparin effects differ between fibrillin self/heterotypic interactions and fibronectin interaction. This is bounded original operative text; a complete original PDF was not recovered. Source guide records the bounded original read and any supplementary limits.
Read locus: Human purified-protein surface plasmon resonance; Table 2.
Citation identity checked against the genuine fetched record. Human MFAP4 and human FBN1 fragments rF11/rF87 bind in SPR, with Table 2 affinities and explicit controls. Binding is calcium independent in this assay; human FBN2 is a separate tested partner. Mouse GT8 skin localization is distinct from the purified human binary-binding assays. Source guide records the bounded original read and any supplementary limits.
A reference map of the human binary protein interactome.
Read locus: Human ORFeome yeast-two-hybrid; Exact original HuRI PSI target/partner joins.
Citation identity checked against the genuine fetched record. FBN1 clone70317 has explicit human target joins to SGTB/Q96EQ0, GET4/Q7L5D6-1 and HGS/O14964-1 in repeated yeast-two-hybrid records. Human ORFeome constructs are tested in yeast host4932; clone/partner accessions do not establish physiological colocalization or splice-specific function. Not all target pairs were independently validated by MAPPIT/GPCA. Source guide records the bounded original read and any supplementary limits.
Read locus: Human-cell secretion and coculture matrix assembly; Cleavage-site and truncation constructs.
Citation identity checked against the genuine fetched record. GFP-FBN1 secreted from human HEK293T cells is followed in human FS2 fibroblast matrix by nonpermeabilized immunofluorescence and medium immunoblotting. RR2730/2731AA protein is secreted but fails matrix incorporation; the S2732-stop construct is retained intracellularly. These are precursor-processing and assembly assays, not assays of the later asprosin endocrine function. No naturally active product is assigned to every construct. Source guide records the bounded original read and any supplementary limits.
Read locus: Human vein ECM proteomics; exact supplementary target unresolved.
Citation identity checked against the genuine fetched record. Normal and varicose human great-saphenous-vein matrix fractions are compared after three-step extraction. Exact FBN1 supplementary target join remains unresolved at this checkpoint. Main-table truncated portions were not read; collagen or other matrix changes cannot substitute for a FBN1 result. Source guide records the bounded original read and any supplementary limits.
Interactions of fibrillin-1 with heparin/heparan sulfate, implications for microfibrillar assembly. — accessed original
Read locus: Human fibroblast-conditioned medium binding; Human fragment heparin-affinity chromatography; Solid-phase binding and competition; Figures 1–5.
Citation identity checked against the genuine fetched record. Normal human skin fibroblasts secrete FBN1 into conditioned medium; the native secreted protein binds immobilized heparin with BSA controls. Human recombinant FBN1 fragments bind heparin by affinity chromatography and solid-phase assays; calcium dependence varies by region. Heparin is an experimental analog; highly sulfated heparan sulfate competes, but all tissue HS structures are not equivalent. Failed McGill PDF/local HTML and screenshot attempts do not constitute a successful PDF read. Source guide records the bounded original read and any supplementary limits.
Read locus: Primary human fibroblast conditioned-medium immunoprecipitation; Mass spectrometry; Figure 2.
Citation identity checked against the genuine fetched record. Endogenous human FBN1 is immunoprecipitated from seven-day conditioned medium of primary adult foreskin dermal fibroblasts; Figure 2 and mass-spectrometry Methods establish the secreted target. Recombinant HEK constructs and endogenous fibroblast FBN1 are distinguished. FBN1 is the glycosylation substrate, not the glycosyltransferase. Supplemental data were not comprehensively read. Source guide records the bounded original read and any supplementary limits.
Treatment of aortic disease in patients with Marfan syndrome.
Read locus: Clinical review citation/management excerpts; full source-specific evidence unavailable.
Citation identity checked against the genuine fetched record. Correct title/PMID identifies a clinical aortic-disease review. Full original and the source-specific heart-development experiment are unavailable. The review title alone does not establish experimental misattribution. Source guide records the bounded original read and any supplementary limits.
Read locus: Mouse and human cell matrix/gene-expression perturbations; Results Figures 3/6/7.
Citation identity checked against the genuine fetched record. Tsk mouse fibrillin overexpression and Smad3 perturbation associate with CCN3 changes; dox-regulated Marfan-like FBN1 construct disrupts wild-type fibrillin matrix and lowers CCN3 mRNA dose-dependently (Figure 3 Results, original line 103). CCN3 induction directly suppresses fibrillin network assembly without altering FBN1 mRNA/protein levels (Figure 6 Results, line 123). GO:0010467 definition is gene sequence conversion into mature RNA/protein; downstream CCN3 expression changes do not themselves identify FBN1 as executing those steps. GO:0030199 refers to collagen-fibril size/arrangement. The source directly measures fibrillin and elastic networks; fibrillin is not a synonym for collagen. Do not call the reference wrong-gene: FBN1 is genuinely tested. Source guide records the bounded original read and any supplementary limits.
Read locus: Human/mouse cell-matrix proteomics; exact main Table 1 FBN1 row.
Citation identity checked against the genuine fetched record. Detergent-isolated matrices from human cells contain FBN1; the exact Table 1 row distinguishes human ihPSF/HUES1 positive values from hPSF not detected. Mouse feeder rows are separate. FBN1 staining in hESC colonies is described as cell associated; do not describe all positive cultures as a uniform fibrillar network. Proteomic detection does not assign a developmental mechanism. Source guide records the bounded original read and any supplementary limits.
Read locus: Human fragment multimerization and self-binding; DLS/electron microscopy and matrix competition.
Citation identity checked against the genuine fetched record. Human C-terminal FBN1 fragments form disulfide-linked multimers with stronger N-terminal binding than monomers. Last three cbEGF domains contribute to the interaction; biochemical binding, DLS/EM and fibroblast matrix competition support an assembly mechanism. Multimerization is cell associated in this experiment; autonomous catalytic activity is not inferred. The source-fetched correct title explicitly replaces the seed TODO title, preserving PMID and annotations. Source guide records the bounded original read and any supplementary limits.
Read locus: Human fragment pull-down; Domain controls and NMR.
Citation identity checked against the genuine fetched record. Human N-terminal FUN-EGF3 residues 45–178 bind C-terminal cbEGF41–43 residues 2567–2687 by bead pull-down; unrelated control regions do not. NMR and mutations identify interacting regions, supporting FBN1 self-association. Recombinant bacterial/refolded fragments, not a complete native fibril, are tested. A resolved N-terminal–C-terminal complex structure is not established; precipitation and solubility limit the NMR comparison. Source guide records the bounded original read and any supplementary limits.
Human eye development is characterized by coordinated expression of fibrillin isoforms.
Read locus: Human fetal/juvenile eye immunohistochemistry; IEP.
Citation identity checked against the genuine fetched record. Monospecific antibodies with IgG controls map FBN1 in human fetal eyes at 5–6, 8 and 11 weeks and juvenile enucleated eyes at 1/3 years. FBN1 localization is stage/structure dependent, including strong juvenile zonule labeling. IEP localization is not a gene-specific knockout demonstration of developmental causality. The article uses isoforms for fibrillin paralogs; it does not establish FBN1 splice-product functions. Source guide records the bounded original read and any supplementary limits.
Assembly of epithelial cell fibrillins.
Read locus: Human epithelial localization described in abstract; operative original unavailable.
Citation identity checked against the genuine fetched record. Abstract positively reports FBN1 throughout the lamina densa and human epithelial-cell fibrillin deposition, explicitly addressing more than microfibril insertion sites. Do not extrapolate lamina sparing in other tissues/papers to a universal negative. Exact original epithelial localization assay remains inaccessible. Source guide records the bounded original read and any supplementary limits.
Microfibrils at basement membrane zones interact with perlecan via fibrillin-1.
Read locus: Human basement-membrane-zone immunolocalization; FBN1–perlecan binding.
Citation identity checked against the genuine fetched record. Human skin and ciliary-zonule/lens interface show FBN1/perlecan close association at basement-membrane zones. Recombinant human fibrillin N-terminal fragments interact with perlecan in SPR. Human tissue localization is distinguished from mouse perlecan experimental components and mouse Figure 7. Anchoring mechanism is an interpretation; no uniform distribution throughout all basement-membrane strata is asserted. Source guide records the bounded original read and any supplementary limits.
MatrisomeDB 2.0: 2023 updates to the ECM-protein knowledge database.
Read locus: ECM proteomics database methodology; exact FBN1 compartment record unresolved.
Citation identity checked against the genuine fetched record. The database integrates ECM-enriched human and mouse proteomics with explicit accession/sample mapping. A FBN1-specific database result establishing the noncollagenous interstitial-matrix compartment was not accessed. General database methodology is not an exact target join. Source guide records the bounded original read and any supplementary limits.
The source access limits above remain unchanged. Accessible independent evidence now resolves the gene-level skeletal-development, microfibril, alpha5beta1, calcium, integrin-adhesion and noncollagenous interstitial-matrix claims; see the feedback decisions and the integrated guide. This does not verify the unread original assays, alphaVbeta6 or collagen XVI partners, or unresolved proteomics accessions. Heparin binding and the tissue-elasticity inference remain positive but non-core. The decision table retains the original methods and adds the independent assay provenance where used.