This guide distinguishes original-access scope, database provenance and scientific interpretation. It contains paraphrased assessments and exact table/record locators, with no new publication quotations. A normal-cache availability flag does not claim that every operative original or supplement was available.
The actual mouse donor source and organism are retained. Source-specific original evidence and independent human matrix/ligand work are assessed separately; curator transfer is not treated as an isolated human experiment.
The literal PTHR15427 tree, 1016-residue target MSA and all relevant IBD records were reconstructed. Self-donor evidence is valid. The signed angiogenesis donor conflict and inherited/current ligand-node discrepancy are explicit; donor count is not an evidential metric.
Exact Q99K41/ENSMUSP00000031055 donor tuples and current source records were joined. The matrix and contextual phenotype transfers are evaluated against actual originals; no silent qualifier, species or source-field rewrite.
The broad parent annotations are assessed against the actual supporting specific function and current typed ontology, retaining the positive matrix and adhesion contexts.
The actual CPX-438 mouse EMILIN2 to CPX-421 human EMILIN1 provenance and broad family statements were checked. This does not resolve an EMILIN1 coagulation experiment; that source remains UNDECIDED rather than a declared biological contradiction.
The actual ARBA rule has a satisfied target condition set 16, supported by the literal FunFam and taxonomic fields. This confirms current applicability; biological interpretation also uses independent fiber evidence.
Authentic metadata/abstract and selected original Methods, adhesion Results and Figures 7/8 captions were read. Human recombinant gC1q adhesion is distinct from avian native-protein purification. Historical construct numbering is not silently assigned to a complete current product; no complete-paper or figure-pixel claim.
Original access and assay locators: author-deposited original text. The selected indexed Methods describe human-sequence expression constructs and separate bacterial and 293-EBNA preparations. Table I contains the two-hybrid self-association tests; Figure 3 concerns native gC1q oligomeric mass, Figures 4–6 stability and digestion of domain constructs, and Figures 7–8 full-length extracellular multimers versus the engineered truncation/comparator. This was original-text/caption access, not new figure-pixel inspection or evidence that every natural product has identical stoichiometry.
Selected original Methods, Results, Discussion and captions establish self-association, trimer measurements and full-length extracellular assemblies using human-sequence constructs in distinct expression systems. Engineered truncations and native preparations are kept separate. No figure pixels or universal natural-product stoichiometry claim.
The original selected Methods and Results explicitly contain the reciprocal positive EMILIN1-gC1q/EMILIN2-fragment yeast two-hybrid pair, despite the EMILIN2-focused title. This supports bounded association, not a demonstrated native full-length heterotrimer. No figure pixels read.
Exact PMID/partner-positive IntAct records were verified for the imported screen pairs. These source-scoped positive interactions support non-core generic binding under the campaign policy. Full operative bodies and every supplement were not reread, and direct binary contact, native stoichiometry or natural-product equivalence is not inferred.
Citation identity and the imported broad elastic-fiber statement are retained, but the original review body was not recovered. The location is independently supported by the 2004 primary matrix study and the typed Reactome component chain. A similarly titled later review was not substituted.
Authentic abstract and metadata report a positive antitoxin context, but the operative toxin-inhibition Methods and Results remain unavailable. The source annotation is UNDECIDED, with no wrong-gene or inactivity inference from the access limitation.
Original access and assay locators: publisher DOI, author-deposited original PDF, and PDB 2OII. The original was available through indexed author-PDF text; direct publisher/author byte downloads were denied. Figures 1–2 describe the NMR-constrained domain model; Figure 3 concerns domain mutations/stability; Figure 4 assays mutant-dependent adhesion and haptotaxis; Figure 5 assays Jurkat attachment under flow. The Methods specify the recombinant domain, and the PDB entity sequence supplies the tag/natural-residue boundary used for current-product mapping. No ligand–integrin co-complex or 2008 figure-pixel inspection is claimed.
The genuine original, structural deposition and operative domain/adhesion evidence were independently assessed. Human recombinant gC1q is a trimeric integrin ligand; paper residues 846–995/Glu933 map to current long-product 867–1016/Glu954, with twelve tag/cloning residues separate. No solved integrin-bound complex, receptor-subunit membership or demonstrated molecular-adaptor bridge is claimed.
Exact PMID/partner-positive IntAct records were verified for the imported smart-pooling screen pairs. These source-scoped positive interactions support non-core generic binding under the campaign policy. Full operative bodies and every supplement were not reread, and direct binary contact, native stoichiometry or natural-product equivalence is not inferred.
Original access and assay locators: complete PMC original, experimental procedures for sequential aortic extraction and mass spectrometry, and Table II, EMILIN-1/EMIL1_HUMAN row. The exact row reports eight unique peptides, eight unique spectra, 3.0% coverage and 30 total spectra. Figure-based validation of other matrix proteins does not become EMILIN1 imaging evidence.
Original Methods and Table II directly identify EMILIN-1 in sequential human aortic-matrix extracts: eight unique peptides, eight unique spectra, 3.0% coverage and 30 total spectra. The source qualifier colocalizes_with is preserved. Orthogonal imaging in this paper targets other proteins; no EMILIN1 image or elasticity assay is claimed.
Operative main text, table and figure legends identify human trabecular-meshwork vesicle EMILIN1 by proteomics and specific immunoblot/density-gradient association. The cultured-cell location is non-core and is not generalized to aqueous-humor or urinary exosomes. Figure pixels were not inspected.
BioGRID 1438356 explicitly records human EMILIN1–MTMR9 high-throughput yeast two-hybrid support. These source-scoped positive interactions support non-core generic binding under the campaign policy. Full operative bodies and every supplement were not reread, and direct binary contact, native stoichiometry or natural-product equivalence is not inferred.
Selected authentic review sections on EMILIN1 assembly/vascular signaling and family hemostasis were read. The operative coagulation account concerns multimerin-1 and does not resolve the EMILIN1 claim propagated through homologous-complex metadata. The review is not treated as a new target experiment.
Original ECM Methods/Table 1 and genuine supplemental Protein Reports identify human EMILIN1 in HUES1 and placental-fibroblast-derived matrices. Human IPI00013079 is separated from mouse IPI00115516; no hPSF replicate 1 detection is invented. Protein records, not all automatically located peptide/spectrum rows, were manually inspected; no natural-product assignment.
Original Methods and ECM Results explicitly link PXD000359. Author-deposited txtECM/proteinGroups.txt line 2296 has majority Q9Y6C2, 47 unique peptides overall and positive intensity in all three experiments. Published S6 itself was not recovered; the authentic deposited output supplies the target check. Its 1016/347/347-residue group does not resolve a natural product, and raw spectra were not re-searched.
Original access and assay locators: complete PMC original and additional files. The author workbook contains the target Q9Y6C2/Q96IH6 row at row 8 of sheets A and B; read that row together with the first three header rows. The 16 columns are samples or pools, and the unique-peptide field reports 87. The table locators and the frozen-data replay retain these distinctions rather than treating columns as independent donors.
Genuine workbook sheets A/B row 8 identify Q9Y6C2|Q96IH6 with 87 reported unique peptides and 16 positive sample-or-pool measurements. These are not 16 donors. Original enrichment/threshold scope was assessed; the data support broad matrix detection without an isoform-specific, disease-causal or mechanical-recoil claim.
Exact IntAct PMID/partner matches were verified, including the separate self pair EBI-10488347/IM-23318-29257. These source-scoped positive interactions support non-core generic binding under the campaign policy. Full operative bodies and every supplement were not reread, and direct binary contact, native stoichiometry or natural-product equivalence is not inferred.
Genuine original Methods, Results/captions and selected Discussion support human EMILIN1 secretion/matrix deposition in distinct human and mouse systems. Opposite short N-terminal sequence assignments in Results and Discussion are retained as a source inconsistency and do not overwrite official product metadata. No figure pixels or supplement contents were assessed.
The genuine original Table 1 explicitly lists EMILIN1 with 62 sample versus 21 control peptide hits (ratio 2.95) in bacterial Efb pull-downs with human platelet material and fibrinogen. This is proteomic association; the individual SPR/immunoblot validation of other proteins is not attributed to EMILIN1. The bacterial partner identity is preserved.
Original main Methods and independently recovered genuine OUP supplement resolve Q9Y6C2 in human-vein matrix. Visually checked S4 header/target gives 24/11 unique peptides in complementary guanidine workflows; supplementary quantifications do not show differential EMILIN1 abundance. Earlier 403 routes are preserved historically. No peptide reanalysis, natural-product specificity or recoil assay is claimed.
Genuine Tables I/II contain EMILIN1 in all six marrow-stromal donors and adipose/dermal matrix preparations. Adjacent ITIH2 cells are excluded and fractional peptide summaries remain as reported. Decellularization, serum carryover and human/bovine shared-peptide limitations are explicit; no isoform-specific or recoil inference.
The genuine workbook has 20 EMILIN1 protein-summary records, 19 Q9Y6C2-only and one mixed Q9Y6C2/ERC1 group. Alternate-search entries are excluded as additional observations. Original ECM-enrichment/threshold scope is retained; neither raw spectra nor natural-product-specific peptides were reanalysed.
Exact IntAct PMID/partner-positive records were verified; the screen context is not an isolated biochemical mechanism. These source-scoped positive interactions support non-core generic binding under the campaign policy. Full operative bodies and every supplement were not reread, and direct binary contact, native stoichiometry or natural-product equivalence is not inferred.
Exact IntAct PMID/partner-positive records were verified without converting perturbation-screen associations into a functional subclass. These source-scoped positive interactions support non-core generic binding under the campaign policy. Full operative bodies and every supplement were not reread, and direct binary contact, native stoichiometry or natural-product equivalence is not inferred.
Author BioPlex HEK293T output line 53439 explicitly contains EMILIN1 bait 11117 and TAX1BP1 prey 8887. These source-scoped positive interactions support non-core generic binding under the campaign policy. Full operative bodies and every supplement were not reread, and direct binary contact, native stoichiometry or natural-product equivalence is not inferred.
The original-linked author NDEx network contains the LAIR2–EMILIN1 AP-MS edge 567376 in U2OS; endpoint order is not reinterpreted as bait/prey. These source-scoped positive interactions support non-core generic binding under the campaign policy. Full operative bodies and every supplement were not reread, and direct binary contact, native stoichiometry or natural-product equivalence is not inferred.
The typed Reactome component/member/repeated-unit chain reaches human Q9Y6C2 as three mature-chain 22–1016 monomers in an EMILIN1 trimer/polymer within elastic fiber. Numeric component references and repeated multiplicity are preserved. This is structural participation, not EMILIN1 enzymatic crosslinking; the short natural product is not inferred.
Original access and assay locators: publisher original and the recovered original PDF. Journal pages 6161–6162 (PDF pages 2–3) contain recombinant-protein, cell-adhesion and purified-integrin binding Methods. Figure 5C, including its inset, reports the purified-receptor binding and soluble-integrin competition; Figure 5D specifically tests gC1q adhesion of alpha4-transfected K562 cells under TPA activation. Figure 7 concerns HT1080 migration. The publisher download was denied during retrieval, but the mirror supplied the complete original with matching title, authors, DOI and journal pagination; no normal-cache flag is changed.
The genuine full original was independently recovered and its operative evidence assessed: human recombinant full-length/gC1q preparations, purified human placental alpha4beta1 solid-phase binding, blocking and alpha4-transfected cell adhesion. Receptor binding and ligand-mediated adhesion are distinguished from receptor-subunit membership.
Original access and assay locators: complete PMC original. Results and Figures 4–5 describe mouse aortic/skin architecture and vascular-cell anchorage; Figures 6–7 concern elastogenesis and fibulin-5 deposition in mouse embryonic fibroblasts. Figure 8A is the elastin solid-phase interaction assay, while Figure 8B contains separate co-immunoprecipitation evidence. Figure 9 concerns extracted tropoelastin-related peptides. Methods distinguish the human recombinant EMILIN1/elastin and rat fibulin-5 constructs. The separately recovered original supplies this detail even though the normal cache remains abstract-only.
Operative original Methods, Results, Discussion and captions were recovered and read separately from the abstract-only normal cache. Mouse knockout matrix architecture and deposition are combined with distinct human recombinant EMILIN1/elastin and rat fibulin-5 constructs. Supports structural organization and assembly; no figure-pixel or isolated recoil-mechanics claim.
Authenticated abstract and publisher metadata support the mouse pro-TGF-beta maturation/blood-pressure mechanism at abstract scope. The full operative original was unavailable. Substrate shielding from furin processing is not EMILIN1 protease activity, and direct human or natural-product-specific assays are not established here.
Selected original Methods and Results were recovered separately from the abstract-only normal cache. The mouse extracellular-protein screen and current donor record are authentic, but the exact EMILIN1 supplemental entry remains unavailable. Independent human integrin-adhesion evidence supports the retained broad biology; no donor-specific result is invented.
Original access and assay locators: complete PMC original and its Supplementary Material. Figure 5A–C distinguishes proliferation, receptor expression and integrin-dependent adhesion in the human cell lines; Figure 5D–G tests receptor/blocking-antibody and domain-mutant effects on proliferation. Figure 7E–H tests PTEN perturbation and downstream Erk responses. Supplementary Figure S3 contains domain-mutant adhesion controls. These are separate from the native mouse skin and primary mouse cell observations. The original XML and genuine supplementary archive were recovered; only the previously listed main Figures 5/7 and supplementary Figure S3 were visually assessed.
The genuine original and supplement were independently assessed. Human cell-line integrin-blocking/proliferation and signaling experiments are distinct from mouse skin and contact-culture findings. The inhibitory proliferation effect is context-bound; neither an autonomous intracellular enzyme nor universal response is inferred.
Original access and assay locators: publisher original and publisher PDF. The retrieved publisher-indexed Methods cover blood-pressure evaluation, pressure-myograph vascular-function measurements and TGF-beta antibody infusion. Figure 3 concerns antibody treatment and blood pressure; Figure 4 distinguishes smooth-muscle and endothelial transgene rescue of the myogenic response; Figure 5A–B concerns chronic and directly applied TGF-beta neutralization. Direct downloads were denied: the operative access was selected indexed publisher text, not a locally recovered complete PDF, supplement or figure-pixel inspection.
Authenticated abstract plus selected original publisher-indexed Methods and Results/Figures3–5 text were read separately from the abstract-only normal cache. Mouse cell-type rescue, pressure myography and TGF-beta blockade support a contextual vascular role. No complete PDF, supplement, human perturbation or figure-pixel claim.
Original access and assay locators: complete PMC original and its Supplementary Material. Figure 2 and its Results establish the angiogenesis phenotype. The fibrosis/inflammation Results and Figure 5C–D contain the Mac-3-positive accumulation observation; the Discussion paragraph on non-resident cells gives alternative routes of tissue entry rather than a migration assay. Figure 5 also contains collagen deposition and transcript measurements. Supplementary Figure S2M and its legend identify heterogeneous aortic collagen fibrils. The complete main Methods and genuine supplementary legends were read; the previously inspected pixels were main Figures 2/5 and supplementary S2.
Operative original Methods, Results, Discussion and genuine supplement were read, with selected Figure 2/Figure 5/S2 pixels inspected. Mouse Emilin1 loss increases angiogenesis and later fibrosis/infiltration; opposite current donor signs are explicitly retained for correction queries. Collagen quantity and organization are separated in the review: the organization rows use unsigned regulation after integrating the later human/mouse evidence. Infiltration versus migration remains scientifically unresolved despite access.
Original access and assay locators: complete PMC original. Figure 4 and its Results separate impaired fibulin-4 deposition from continued secretion after EMILIN1 depletion. Figure 5A–B contains co-precipitation, Figure 5C the purified binding assay, and Figure 5D supplementation rescue of deposition in mouse osteoblast cultures. The solid-phase binding Methods identify coated human EMILIN1; the protein-preparation and co-precipitation Methods identify murine fibulin-4 and the distinct murine tagged constructs. These experiments support matrix-organizing work without assigning LOX catalysis to EMILIN1.
Selected genuine original Methods/Results and captions independently establish direct human EMILIN1–murine fibulin-4 solid-phase binding, distinct mouse co-IP, and deposition rescue in mouse osteoblast cultures. Species combinations and cell-type dependence remain explicit. EMILIN1 organizes matrix deposition rather than catalyzing LOX crosslinking.
Original access and assay locators: complete PMC original. Figure 4 and the EFEMP2-deposition Results address matrix targeting; Figure 5A–F and the LOX/collagen-network Results distinguish LOX abundance/activity, fibril architecture and mouse collagen crosslinks. Figure 6A supplies direct human collagen-synthesis support; Figure 6D shows disorganized aortic collagen deposits. Figure 7A–D and the associated Results report fibril-size distributions, with no significant change in fibril-occupied area for EMILIN1-deficient skin. The Discussion qualifies negative-staining morphology by acid stability and distinguishes synthesis from crosslinking. Figure 8C and the three-point-bending Methods concern mouse femur stiffness. The Results/Figure 6C pSMAD2 wording remains qualified. No complete-supplement or all-figure-pixel claim is made.
Selected genuine human/mouse structural-assembly and matrix Results/Methods/captions were independently assessed. The study includes actual femur three-point bending and altered knockout stiffness, not a direct reversible-recoil test. EFEMP2 deposition and downstream LOX effects support matrix organization; the nuanced Results/Figure 6C pSMAD2 account is not flattened. No complete supplement or all-pixel claim.
| Source | Exact target locator | Interpretation limit |
|---|---|---|
| 20551380 | Original Table II, EMILIN-1/EMIL1_HUMAN; eight unique peptides, 30 total spectra | Human aortic fraction; no target-specific imaging |
| 23658023 | Table 1; supplementary Protein Reports, human IPI00013079 in HUES1 replicates 1/2, ihPSF 1/2 and hPSF 2 | Mouse IPI00115516 is separate; no hPSF 1 claim |
| 23979707 | PXD000359, txtECM.zip, proteinGroups.txt line 2296 | Author output, not recovered S6 or a raw-spectrum reanalysis; group lengths 1016/347/347 |
| 25037231 | Additional-file workbook sheets A/B, row 8 | Q9Y6C2 with Q96IH6; 16 measurements are samples/pools, not donors |
| 27068509 | OUP cvw075supp.pdf, S4 header page 25/target page 27 | Complementary workflows, not independent donors; no differential abundance established |
| 28327460 | Table I row 10 and Table II row 9, A:E | Adjacent ITIH2 excluded; fractional counts retained |
| 28675934 | Twenty protein-summary records; D2164 is the mixed Q9Y6C2/ERC1 group | F50/F66 alternate searches excluded; no isoform assignment |
| 21362503 | Original Table 1, Q9Y6C2; Methods and Figure 2 density-gradient caption | Cultured human trabecular-meshwork context; pixels not inspected |
The PAINT reconstruction uses the literal PTHR15427 tree, target PTN002495974 and its exact 1,016-residue MSA sequence, plus the complete saved IBD scan. Target self-donor evidence is expected and valid. The positive angiogenesis IBD is genuinely on the target path; the correction concerns the conflicting signed donor interpretation. The inherited ligand node PTN002692991 differs from the saved current IBD at PTN000396133 in the MMRN2 branch; this version discrepancy is not treated as proof that EMILIN1 lacks ligand activity.
Reactome R-HSA-2161282 reaches EMILIN1 through input complex 2396077, Emilin set 2161303, member polymer 2161354, repeated trimer 2161295 and three components 2161355 referencing Q9Y6C2. Component multiplicity and mature-chain coordinates 22–1016 are preserved. The current ARBA rule has a literally satisfied condition set 16. CPX-438 is mouse EMILIN2 with an inferred-from link to human EMILIN1 CPX-421; its broad coagulation attribution remains unresolved.
The exact three unreported source queries concern QuickGO records Q9Y6C2!118992744 (CAFA, receptor-complex term), !118992708 (GO Central, signed PAINT transfer) and !118992709 (Ensembl, signed orthology transfer). The mouse donor records !178640421 and !178640431 cite the same original with opposite signs. These record locators explain the requested checks; they do not alter the imported dictionaries or imply that an upstream report has been sent.
The visible Python script and input manifest reconstruct frozen machine-source, phylogenetic, interaction and selected author-tabular evidence. Article XML/HTML/PDF, original figure images and provider logs are private and excluded. Original-body interpretation is documented here and in the reference assessments; the data replay does not automate biological judgment or claim complete original-paper reproduction.