FGB direct evidence guide

The review YAML is the decision authority. The source records retain every direct source key, zero-based index, method and locator without duplicating decision prose. Product boundaries distinguish parent-source identities from curated processing metadata; literature notes explain the biological synthesis.

Evidence is assessed at the claim's actual scope. Human beta-chain assembly supports structural complex participation. Intact-fibrinogen receptor or cellular responses are not isolated beta-chain activities. Positive matrix classification can be supported independently at gene level while a particular unavailable high-throughput target/sample record remains uncertain. The external platelet-surface location is more precise than its cell-surface parent (GO:0009897 part_of GO:0009986); the broader structural molecular function still covers soluble-complex assembly beyond matrix incorporation.

For generic binding, the positive cellular association is retained as non-core unless a more informative function is demonstrated. GO:0046790 requires a virion, so an expressed core-protein construct does not establish it. GO:0051087 describes binding to a chaperone and is compatible with the beta chain being a client. These decisions follow the project's curation instructions; no new publication quotations are introduced.

Exact proteomic target scope

• PMID:25037231(https://doi.org/10.1186/1471-2407-14-518), Additional File 2, sheets A and B row 14: FGB/Entrez 2244, principal P02675, full accession group P02675|Q32Q65|B4E1D3|D3DP13. The matrisome sheet is a subset of the same measurements. Cleavage labels in database descriptions do not establish a measured free peptide.
• PMID:28675934(https://doi.org/10.1021/acs.jproteome.7b00191), SI002: breast rows 558, 731, 984, 1358, 1576 and 1751; omentum unfractionated rows 6, 180, 623, 793, 1288, 1785, 1842 and 1988; omentum fractionated rows 22, 1191, 2172, 4783, 5846, 6247, 6498 and 7045. All 22 main records identify human FGB/P02675. Clinical normal omentum is not labeled healthy-donor tissue. Hydroxylation-list entries are not additional functional assays.
• PMID:24769233(https://www.ebi.ac.uk/pride/archive/projects/PXD000608), deposited MaxQuantOutPut/proteinGroups.txt line 692, group 703: P02675;D6REL8, 47 group-unique peptides overall, positive exo_A/exo_G and soluble sn_B/sn_H measurements, blank reverse/contaminant/site-only flags. These are deposited processed results, not a new spectral reanalysis. Neither free fibrinopeptide B nor intravesicular topology is resolved.
• PMID:28344315, 28327460, 16502470, 23533145 and 22516433 retain unresolved exact FGB target records. Original bodies or Methods were read where available, but no missing table was reconstructed from another gene, abstract, or proteomics study. The Figure 5B FGA label in PMID:28344315 is not a FGB match. Failed HTTP 500 JSON and HTTP 403 HTML artifacts were explicitly excluded as original articles or workbooks.

Primary-source locators and limits

• PMID:10903502(https://pubmed.ncbi.nlm.nih.gov/10903502/): Publisher source segment 0 only; Adhesion assay, Table 1, ERK and survival text. The recovered body is a bounded selection, not a claim that every original figure was inspected. The γ-chain peptide and whole-complex design do not isolate an autonomous β-chain receptor-binding or survival activity. Adjacent search results from other articles are excluded.
• PMID:8910396(https://pubmed.ncbi.nlm.nih.gov/8910396/): Original Methods lines 461–531; Results lines 684–808, 943–1036 and 1112–1227; Figures 1–5 captions. BHK recipients are not human cells. These are chain-combination studies, not natural splice or released fibrinopeptide-B comparisons. Only the original article portions specified were used; later citing items on the hosting page were excluded.
• PMID:28344315(https://pubmed.ncbi.nlm.nih.gov/28344315/): Original Methods, manuscript lines 139–200; Tables S1–S3 not recovered; Figure 5B is a transcript panel. No FGB absence inference from inaccessible supplements. No transcript heatmap is substituted for proteomics or a structural-function measurement. The prior unverified MassIVE task-URL failure is excluded; only original accession MSV000080451 is established.
• PMID:25037231(https://pubmed.ncbi.nlm.nih.gov/25037231/): Additional File 2, sheets A/B row 14; original ECM-enrichment and mass-spectrometry Methods. Matrisome membership is a classification and fraction measurement; it is not a dedicated mechanical structural-function assay. BU14 cleavage labels are database descriptions, not measured free fibrinopeptide B or cleavage boundaries. Grouped accessions do not establish natural splice-specific detection. Both extension-distinct raw pairs that project to the two target annotations remain unchanged in the intake sidecar.
• PMID:28327460(https://pubmed.ncbi.nlm.nih.gov/28327460/): Methods 2.1–2.3, cell-derived ECM preparation and mass spectrometry; supplemental composition tables unavailable. No FGB absence or wrong-species assertion from failed table access. Without the exact target record and peptides, endogenous human deposition versus medium-associated protein cannot be resolved for FGB. No mechanical structural-function assertion is inferred from whole-matrix culture responses. The EPMC .xml file is HTTP 500 JSON and is excluded as original text; the successful PMC HTML is used.
• PMID:28675934(https://pubmed.ncbi.nlm.nih.gov/28675934/): SI002 sheets B/C/D, the 22 FGB rows listed above; sample legends on supplement page S2. Normal omentum is not described as healthy-donor tissue. Classification/fraction detection is distinct from a dedicated mechanical-function assay. No natural splice or processed peptide is resolved. Hydroxylation-list presence is not promoted into a new functional assertion.
• PMID:12706644(https://pubmed.ncbi.nlm.nih.gov/12706644/): Original abstract; DOI 10.1016/S0049-3848(03)00114-2. No FGB-specific curated interaction record was independently retrieved in this lane. The alpha-chain variant emphasis does not prove misattribution. Binding remains source-specific UNDECIDED; generic polymerization is supported independently by actual human-chain assembly and structure, without claiming a re-read of the unavailable variant assay.
• PMID:20162731(https://pubmed.ncbi.nlm.nih.gov/20162731/): Interaction Methods; Results lines 136–140; Figure 2A–B. The assessment is bounded to the imported interaction. Tagged core-protein association is not binding to an intact virion, a purified binary-affinity measurement, or evidence for a new regulatory process. The subsequent response experiments are not used to create FGB annotations.
• PMID:10074346(https://pubmed.ncbi.nlm.nih.gov/10074346/): Original abstract; DOI 10.1021/bi982626w; publisher-linked PDB identities 1FZE/1FZF/1FZG. The original full Methods/Results remain inaccessible. No coordinate analysis was performed and the PDB metadata are not a claimed structural reanalysis. Broad extracellular localization is independently supported by human plasma-purification and secretion experiments; no natural free-peptide or splice activity is inferred.
• PMID:19296670(https://pubmed.ncbi.nlm.nih.gov/19296670/): Printed pages 3878–3882; Materials and Methods; Figure 2; Overall Structure, Crystal Packing and Carbohydrate Clusters. Some alpha-chain proteolysis and minor fibrinopeptide cleavage occurred during crystallization. Crystal contacts are not treated as a direct in-solution polymerization or mechanical assay; synthetic peptide ligands are not natural-product evidence. No independently measured free fibrinopeptide-B location or activity is inferred.
• PMID:9628725(https://pubmed.ncbi.nlm.nih.gov/9628725/): Accepted normal, complete original abstract. The full original experimental article was not recovered. The generic extracellular location is retained using independent human plasma-fibrinogen and secretion evidence; no unexamined fragment-specific claim is asserted.
• PMID:16502470(https://pubmed.ncbi.nlm.nih.gov/16502470/): Original abstract and University of Manchester bibliographic record; publisher full text and target table unavailable. Repository metadata and abstract are not a full original or protein-table read. Do not infer absence, wrong-gene attribution, or product identity from failed full-text access.
• PMID:19996109(https://pubmed.ncbi.nlm.nih.gov/19996109/): Original PMC lines 90–122 Methods; 145–194 Results/Table 1/Figures 3–6; 201–215 Discussion. The 150-byte EPMC XML-path artifact is HTTP 500 JSON and is excluded as article evidence. The successful indexed PMC original supplies the operative reading. Heterogeneous assemblies/fragments are not purified beta-chain binary affinity; denaturing elution prevents simple stoichiometric interpretation. Methods describe room-temperature control storage while the Figure 6 caption says 4 C; no quantitative in-vivo inference is drawn from that difference.
• PMID:6777381(https://pubmed.ncbi.nlm.nih.gov/6777381/): Original Methods lines 417–625; Results 905–919, 940–1018, 1202–1221 and 1460–1522; Figures 1–3; Discussion 1590–1617. The paper foregrounds thrombospondin but directly assays fibrin chains too. α-Granule origin relies partly on prior cited work, not a new FGB-specific granule-localization image. Calcium dependence does not establish FGB as a calcium sensor or the secretion machinery.
• PMID:14718574(https://pubmed.ncbi.nlm.nih.gov/14718574/): Accepted normal, complete original abstract. The underlying target list was not recovered. Broad extracellular localization is independently supported by direct human plasma-fibrinogen evidence; the compilation is not presented as a new target-localization assay.
• PMID:16846481(https://pubmed.ncbi.nlm.nih.gov/16846481/): Accepted normal abstract; genuine failed publisher artifact and author-page availability record. The full operative variant assay is inaccessible. Independently read alpha-C oligomer experiments do not isolate beta-chain cofactor activity. Plasminogen activation and fibrinolysis therefore remain source-specific UNDECIDED; generic complex membership and clot structure are independently supported. All FGB machine annotations name parent P02675, with no processed-product remapping.
• PMID:18676163(https://pubmed.ncbi.nlm.nih.gov/18676163/): Accepted normal and original publisher/PubMed abstract. Full operative Methods/Results were not recovered. Complex membership and assembly are accepted only at the same generic claim level using independently read human-chain evidence, without certifying the specific variant mechanism.
• PMID:6688356(https://pubmed.ncbi.nlm.nih.gov/6688356/): Original abstract; DOI 10.1021/bi00282a032. Operative full Methods/Results were not recovered. Generic beta-chain complex membership is independently supported by actual human assembly/structure studies. Neither the bovine probe nor the historical sequence discussion supplies a current natural-product processing boundary.
• PMID:8100742(https://pubmed.ncbi.nlm.nih.gov/8100742/): Original abstract; DOI 10.1016/0092-8674(93)90367-Y. The operative full Methods/Results were not recovered. Other ICAM-1 binding or endothelial survival papers do not substitute for this heterotypic adhesion assay. No wrong-gene or negative-result inference is made.
• PMID:24367264(https://pubmed.ncbi.nlm.nih.gov/24367264/): Accepted full cache, Results lines 100–105 and Figure 2 context. The experiment concerns intact human fibrinogen as a host ligand. It does not isolate an autonomous β-chain site or establish an antimicrobial enzymatic function. This assessment is limited to the agglutination claim.
• PMID:15739255(https://pubmed.ncbi.nlm.nih.gov/15739255/): Original publisher Methods, Materials; Results and Figures 6–8; Discussion. The recipient vessels are rat, not an in-vivo human experiment. Fragment D contains contributions from all three chains, and the data do not isolate a β-chain contractile activity or an exclusive receptor mechanism. Later papers appearing in search output are not evidence from this source.
• PMID:19193866(https://pubmed.ncbi.nlm.nih.gov/19193866/): Accepted full cache, endothelial Methods and release/ERK Results. These are ligand-induced endothelial responses, not FGB operation of vesicle-fusion machinery. Endothelin-1 is the secreted peptide hormone; fibrinogen is not thereby assigned hormone activity. Whole-complex and species limits apply to all four owned annotations.
• PMID:9182580(https://pubmed.ncbi.nlm.nih.gov/9182580/): Original Methods lines 315–710; Figure 1B caption 1321–1352; Results, Fibrinogen binding to Raji cells. Gamma-chain recognition and intact-complex binding are distinguished from an autonomous beta-chain ICAM-1 site. The imported contributes_to assertion is assessed as a structural-subunit contribution to the assembled ligand. Later citing material and unexamined beta-peptide claims are excluded.
• PMID:23533145(https://pubmed.ncbi.nlm.nih.gov/23533145/): Original Methods and Results; Supplemental Table 2 target record unavailable. No FGB absence or sample-specific distribution claim. The prior epmc.xml file is HTTP 500 JSON, not an original; actual Methods are read from the genuine accepted full cache. No vesicle membrane topology or natural cleavage-product inference.
• PMID:6281794(https://pubmed.ncbi.nlm.nih.gov/6281794/): Original Methods lines 1101–1296 and 1447–1627; Results 1738–2251; Table 1 lines 2779–2954; Figure 1 caption 3512–3613; Discussion 4653–4953. The modified isolated-chain result is retained explicitly. A non-core process judgment refers only to beta chain as a structural component of intact fibrinogen, independently supported by human-chain assembly; it does not claim that isolated beta chain directly stimulates or bridges platelets. Chain self-association limits are preserved.
• PMID:22516433(https://pubmed.ncbi.nlm.nih.gov/22516433/): Original abstract; publisher full text and target table unavailable. No FGB absence or wrong-gene assertion. No microparticle localization mechanism or processed-product identity inferred from inaccessible data.
• PMID:36399478(https://pubmed.ncbi.nlm.nih.gov/36399478/): Original database Methods and data-integration description. No exact current FGB interstitial-matrix target record was recovered. The specific compartment annotation remains UNDECIDED, without inferring an erroneous gene assignment.
• PMID:24041635(https://pubmed.ncbi.nlm.nih.gov/24041635/): Original abstract and limited publisher Discussion excerpt. The operative spreading Methods/figures and specific β-chain contribution were not recovered. This particular annotation remains UNDECIDED; generic fibrin biology is not substituted for the unavailable target-cell experiment.
• PMID:24769233(https://pubmed.ncbi.nlm.nih.gov/24769233/): PXD000608, MaxQuantOutPut/proteinGroups.txt line 692, group 703, and experimentalDesignTemplate.txt. These are deposited processed results, not a newly acquired journal supplement or reprocessed spectra. 47 is a protein-group metric, not a number of unique natural-product peptides. Protein-name metadata mentioning fibrinopeptide B does not show measured free peptide or cleavage boundaries. Positive vesicle and soluble fractions do not resolve intravesicular versus external/co-isolated association. Publisher original access remained HTTP 403; source Methods scope is limited to official deposit metadata and experimental-design files.