{"gene":"MATN1","run_date":"2026-06-10T02:59:50","timeline":{"discoveries":[{"year":1999,"finding":"Cartilage matrix protein (CMP/matrilin-1) promotes cell adhesion and spreading of chondrocytes and fibroblasts via integrin α1β1. Monoclonal antibody to integrin α1 or β1 abolished CMP-induced cell adhesion, while antibodies to other integrin subunits had little effect. Co-immunoprecipitation of 125I-CMP with integrin α1 from cell lysates confirmed direct association with the α1 subunit. Synergistic spreading enhancement required native (not denatured) type II collagen.","method":"Cell adhesion assay on CMP-coated dishes, blocking antibodies to specific integrin subunits, co-immunoprecipitation of radiolabeled CMP with integrin α1 from cell lysates","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal binding confirmed by co-IP and competition assay, functional blocking by specific antibody, single lab with two orthogonal methods","pmids":["10196235"],"is_preprint":false}],"current_model":"Matrilin-1 (MATN1/CMP/CRTM) is a cartilage extracellular matrix protein that promotes chondrocyte and fibroblast adhesion and spreading by binding directly to integrin α1β1, with synergistic activity in the presence of native type II collagen; its coiled-coil domain mediates oligomerization, but the broader mechanistic understanding of its function in cartilage development and matrix assembly remains limited in the available literature."},"narrative":{"mechanistic_narrative":"Matrilin-1 (MATN1/CMP) is a cartilage extracellular matrix protein that promotes adhesion and spreading of chondrocytes and fibroblasts by binding directly to the integrin α1 subunit of α1β1 integrin [PMID:10196235]. This adhesive activity is integrin-specific: blocking antibodies against the α1 or β1 subunits abolish CMP-induced cell adhesion, whereas antibodies to other integrin subunits have little effect, and co-immunoprecipitation of radiolabeled CMP with integrin α1 confirms a direct association [PMID:10196235]. Its spreading-promoting function is synergistically enhanced in the presence of native, but not denatured, type II collagen [PMID:10196235]. Beyond this integrin-mediated adhesion role, no further mechanistic detail on matrilin-1 in cartilage matrix assembly has been characterized in the available corpus.","teleology":[{"year":1999,"claim":"Established that matrilin-1 is not merely a structural matrix component but an active adhesive ligand, identifying integrin α1β1 as its direct cell-surface receptor and pinpointing the α1 subunit as the binding partner.","evidence":"Cell adhesion/spreading assays on CMP-coated surfaces with integrin subunit-specific blocking antibodies, plus co-immunoprecipitation of radiolabeled CMP with integrin α1 and synergy assays with native type II collagen","pmids":["10196235"],"confidence":"Medium","gaps":["The CMP domain mediating integrin α1 binding was not mapped","The molecular basis of the synergy with native type II collagen was not defined","Single-lab finding without independent reciprocal confirmation of the direct α1 interaction"]},{"year":null,"claim":"How matrilin-1 contributes to cartilage matrix assembly and development at the molecular level, and the structural determinants of its receptor and collagen interactions, remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of the integrin α1β1 interaction surface","No in vivo phenotype linking the adhesive activity to cartilage development","Mechanism of collagen-dependent spreading synergy uncharacterized"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0098631","term_label":"cell adhesion mediator activity","supporting_discovery_ids":[0]}],"localization":[{"term_id":"GO:0031012","term_label":"extracellular matrix","supporting_discovery_ids":[0]}],"pathway":[],"complexes":[],"partners":["ITGA1","ITGB1","COL2A1"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"P21941","full_name":"Matrilin-1","aliases":["Cartilage matrix protein"],"length_aa":496,"mass_kda":53.7,"function":"A major component of the extracellular matrix of non-articular cartilage (By similarity). Binds to type 2 collagens and forms long concatenated protein networks as part of the extracellular matrix (By similarity). Required for the network-like organization and bundling of collagen fibrils surrounding chondrocytes in the zones of maturation and hypertrophy (By similarity). Required for mechanotransduction and adaption to mechanical loading in cartilage chondrocytes, resulting in an increase in expression of the extracellular matrix components ACAN and COL2A1 (By similarity). Acts as a moderator of angiogenesis in response to injury (By similarity)","subcellular_location":"Secreted, extracellular space, extracellular matrix","url":"https://www.uniprot.org/uniprotkb/P21941/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/MATN1","classification":"Not Classified","n_dependent_lines":41,"n_total_lines":1208,"dependency_fraction":0.03394039735099338},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/MATN1","total_profiled":1310},"omim":[{"mim_id":"610026","title":"COLLAGEN, TYPE XXII, ALPHA-1; COL22A1","url":"https://www.omim.org/entry/610026"},{"mim_id":"609996","title":"COLLAGEN, TYPE XXVIII, ALPHA-1; COL28A1","url":"https://www.omim.org/entry/609996"},{"mim_id":"602109","title":"MATRILIN 3; MATN3","url":"https://www.omim.org/entry/602109"},{"mim_id":"602108","title":"MATRILIN 2; MATN2","url":"https://www.omim.org/entry/602108"},{"mim_id":"115437","title":"MATRILIN 1; MATN1","url":"https://www.omim.org/entry/115437"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"","locations":[],"tissue_specificity":"Tissue enriched","tissue_distribution":"Detected in single","driving_tissues":[{"tissue":"retina","ntpm":4.6}],"url":"https://www.proteinatlas.org/search/MATN1"},"hgnc":{"alias_symbol":[],"prev_symbol":["CRTM","CMP"]},"alphafold":{"accession":"P21941","domains":[{"cath_id":"3.40.50.410","chopping":"36-223","consensus_level":"high","plddt":91.0644,"start":36,"end":223},{"cath_id":"2.10.25.10","chopping":"227-264","consensus_level":"high","plddt":77.9466,"start":227,"end":264},{"cath_id":"3.40.50.410","chopping":"273-449","consensus_level":"high","plddt":89.9428,"start":273,"end":449}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P21941","model_url":"https://alphafold.ebi.ac.uk/files/AF-P21941-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P21941-F1-predicted_aligned_error_v6.png","plddt_mean":83.12},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=MATN1","jax_strain_url":"https://www.jax.org/strain/search?query=MATN1"},"sequence":{"accession":"P21941","fasta_url":"https://rest.uniprot.org/uniprotkb/P21941.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P21941/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P21941"}},"corpus_meta":[{"pmid":"9751737","id":"PMC_9751737","title":"A 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biotechnology","url":"https://pubmed.ncbi.nlm.nih.gov/21968653","citation_count":30,"is_preprint":false},{"pmid":"35064842","id":"PMC_35064842","title":"Hesperidin inhibits biofilm formation, virulence and staphyloxanthin synthesis in methicillin resistant Staphylococcus aureus by targeting SarA and CrtM: an in vitro and in silico approach.","date":"2022","source":"World journal of microbiology & biotechnology","url":"https://pubmed.ncbi.nlm.nih.gov/35064842","citation_count":29,"is_preprint":false},{"pmid":"16537535","id":"PMC_16537535","title":"Expression of a functional Drosophila melanogaster CMP-sialic acid synthetase. Differential localization of the Drosophila and human enzymes.","date":"2006","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/16537535","citation_count":29,"is_preprint":false},{"pmid":"16343442","id":"PMC_16343442","title":"Expression of human CMP-N-acetylneuraminic acid synthetase and CMP-sialic acid transporter in tobacco suspension-cultured cell.","date":"2005","source":"Biochemical and biophysical research communications","url":"https://pubmed.ncbi.nlm.nih.gov/16343442","citation_count":29,"is_preprint":false},{"pmid":"6277336","id":"PMC_6277336","title":"Differential effects of various phosphodiesterase inhibitors, pyrimidine and purine compounds, and inorganic phosphates on cyclic CMP, cyclic AMP and cyclic GMP phosphodiesterases.","date":"1982","source":"Biochemical pharmacology","url":"https://pubmed.ncbi.nlm.nih.gov/6277336","citation_count":29,"is_preprint":false},{"pmid":"24141690","id":"PMC_24141690","title":"CMP-Sialic Acid Synthetase: The Point of Constriction in the Sialylation Pathway.","date":"2015","source":"Topics in current chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/24141690","citation_count":28,"is_preprint":false},{"pmid":"22221957","id":"PMC_22221957","title":"N and C control of ABC-type bicarbonate transporter Cmp and its LysR-type transcriptional regulator CmpR in a heterocyst-forming cyanobacterium, Anabaena sp.","date":"2012","source":"Environmental microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/22221957","citation_count":28,"is_preprint":false},{"pmid":"11827479","id":"PMC_11827479","title":"Sugar specificity of bacterial CMP kinases as revealed by crystal structures and mutagenesis of Escherichia coli enzyme.","date":"2002","source":"Journal of molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/11827479","citation_count":27,"is_preprint":false},{"pmid":"11545592","id":"PMC_11545592","title":"The structure of CMP:2-keto-3-deoxy-manno-octonic acid synthetase and of its complexes with substrates and substrate analogs.","date":"2001","source":"Journal of molecular biology","url":"https://pubmed.ncbi.nlm.nih.gov/11545592","citation_count":27,"is_preprint":false},{"pmid":"2753135","id":"PMC_2753135","title":"Transport of CMP-N-glycoloylneuraminic acid into mouse liver Golgi vesicles.","date":"1989","source":"FEBS letters","url":"https://pubmed.ncbi.nlm.nih.gov/2753135","citation_count":27,"is_preprint":false},{"pmid":"7074121","id":"PMC_7074121","title":"CMP-dependent incorporation of [14C]Glycerol 3-phosphate into phosphatidylglycerol and phosphatidylglycerol phosphate by rabbit lung microsomes.","date":"1982","source":"Biochimica et biophysica acta","url":"https://pubmed.ncbi.nlm.nih.gov/7074121","citation_count":27,"is_preprint":false},{"pmid":"10544289","id":"PMC_10544289","title":"Expression and activity of chimeric molecules between human UDP-galactose transporter and CMP-sialic acid transporter.","date":"1999","source":"Journal of biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/10544289","citation_count":26,"is_preprint":false},{"pmid":"6274851","id":"PMC_6274851","title":"A homogeneous cyclic CMP phosphodiesterase hydrolyzes both pyrimidine and purine cyclic 2':3'- and 3':5'-nucleotides.","date":"1982","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/6274851","citation_count":26,"is_preprint":false},{"pmid":"26478188","id":"PMC_26478188","title":"A Designed Angiopoietin-1 Variant, Dimeric CMP-Ang1 Activates Tie2 and Stimulates Angiogenesis and Vascular Stabilization in N-glycan Dependent Manner.","date":"2015","source":"Scientific reports","url":"https://pubmed.ncbi.nlm.nih.gov/26478188","citation_count":25,"is_preprint":false},{"pmid":"19890979","id":"PMC_19890979","title":"Human CMP-N-acetylneuraminic acid hydroxylase is a novel stem cell marker linked to stem cell-specific mechanisms.","date":"2010","source":"Stem cells (Dayton, Ohio)","url":"https://pubmed.ncbi.nlm.nih.gov/19890979","citation_count":25,"is_preprint":false},{"pmid":"32409965","id":"PMC_32409965","title":"Intraperitoneal CMP-001: A Novel Immunotherapy for Treating Peritoneal Carcinomatosis of Gastrointestinal and Pancreaticobiliary Cancer.","date":"2020","source":"Annals of surgical oncology","url":"https://pubmed.ncbi.nlm.nih.gov/32409965","citation_count":25,"is_preprint":false},{"pmid":"15550676","id":"PMC_15550676","title":"Phosphorylation of Cytidine, Deoxycytidine, and Their Analog Monophosphates by Human UMP/CMP Kinase Is Differentially Regulated by ATP and Magnesium.","date":"2004","source":"Molecular pharmacology","url":"https://pubmed.ncbi.nlm.nih.gov/15550676","citation_count":25,"is_preprint":false},{"pmid":"7875563","id":"PMC_7875563","title":"Isolation from recombinant Escherichia coli and characterization of CMP-Kdo synthetase, involved in the expression of the capsular K5 polysaccharide (K-CKS).","date":"1995","source":"FEMS microbiology letters","url":"https://pubmed.ncbi.nlm.nih.gov/7875563","citation_count":25,"is_preprint":false},{"pmid":"21350118","id":"PMC_21350118","title":"Pancreatic beta-cell failure in obese mice with human-like CMP-Neu5Ac hydroxylase deficiency.","date":"2011","source":"FASEB journal : official publication of the Federation of American Societies for Experimental Biology","url":"https://pubmed.ncbi.nlm.nih.gov/21350118","citation_count":24,"is_preprint":false},{"pmid":"1823161","id":"PMC_1823161","title":"CMP-N-acetylneuraminic acid synthetase of Escherichia coli: high level expression, purification and use in the enzymatic synthesis of CMP-N-acetylneuraminic acid and CMP-neuraminic acid derivatives.","date":"1991","source":"Glycobiology","url":"https://pubmed.ncbi.nlm.nih.gov/1823161","citation_count":24,"is_preprint":false},{"pmid":"2643517","id":"PMC_2643517","title":"In vitro synthesis of colominic acid by membrane-bound sialyltransferase of Escherichia coli K-235. Kinetic properties of this enzyme and inhibition by CMP and other cytidine nucleotides.","date":"1989","source":"European journal of biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/2643517","citation_count":24,"is_preprint":false},{"pmid":"22808067","id":"PMC_22808067","title":"Binding of regulatory subunits of cyclic AMP-dependent protein kinase to cyclic CMP agarose.","date":"2012","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/22808067","citation_count":24,"is_preprint":false},{"pmid":"32262095","id":"PMC_32262095","title":"A CMP-based method for tunable, cell-mediated gene delivery from collagen scaffolds.","date":"2014","source":"Journal of materials chemistry. B","url":"https://pubmed.ncbi.nlm.nih.gov/32262095","citation_count":23,"is_preprint":false},{"pmid":"15992295","id":"PMC_15992295","title":"Molecular typing of Campylobacter strains using the cmp gene encoding the major outer membrane protein.","date":"2005","source":"Foodborne pathogens and disease","url":"https://pubmed.ncbi.nlm.nih.gov/15992295","citation_count":23,"is_preprint":false},{"pmid":"1398032","id":"PMC_1398032","title":"Sequence and functional analysis of the cloned Neisseria meningitidis CMP-NeuNAc synthetase.","date":"1992","source":"FEMS microbiology letters","url":"https://pubmed.ncbi.nlm.nih.gov/1398032","citation_count":23,"is_preprint":false},{"pmid":"31141512","id":"PMC_31141512","title":"Lessening of porcine epidemic diarrhoea virus susceptibility in piglets after editing of the CMP-N-glycolylneuraminic acid hydroxylase gene with CRISPR/Cas9 to nullify N-glycolylneuraminic acid expression.","date":"2019","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/31141512","citation_count":21,"is_preprint":false},{"pmid":"25414257","id":"PMC_25414257","title":"Pen and Pal are nucleotide-sugar dehydratases that convert UDP-GlcNAc to UDP-6-deoxy-D-GlcNAc-5,6-ene and then to UDP-4-keto-6-deoxy-L-AltNAc for CMP-pseudaminic acid synthesis in Bacillus thuringiensis.","date":"2014","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/25414257","citation_count":21,"is_preprint":false},{"pmid":"9126287","id":"PMC_9126287","title":"Structural and catalytic properties of CMP kinase from Bacillus subtilis: a comparative analysis with the homologous enzyme from Escherichia coli.","date":"1997","source":"Archives of biochemistry and biophysics","url":"https://pubmed.ncbi.nlm.nih.gov/9126287","citation_count":20,"is_preprint":false},{"pmid":"9602145","id":"PMC_9602145","title":"Cloning, sequence analysis and expression of the basidiomycete Lentinus edodes gene uck1, encoding UMP-CMP kinase, the homologue of Saccharomyces cerevisae URA6 gene.","date":"1998","source":"Gene","url":"https://pubmed.ncbi.nlm.nih.gov/9602145","citation_count":20,"is_preprint":false},{"pmid":"16118285","id":"PMC_16118285","title":"Functional expression of the CMP-sialic acid transporter in Escherichia coli and its identification as a simple mobile carrier.","date":"2005","source":"Glycobiology","url":"https://pubmed.ncbi.nlm.nih.gov/16118285","citation_count":20,"is_preprint":false},{"pmid":"15452776","id":"PMC_15452776","title":"IR and Raman study on the interactions of the 5'-GMP and 5'-CMP phosphate groups with Mg(II), Ca(II), Sr(II), Ba(II), Cr(III), Co(II), Cu(II), Zn(II), Cd(II), Al(III) and Ga(III).","date":"2004","source":"Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/15452776","citation_count":20,"is_preprint":false},{"pmid":"33396746","id":"PMC_33396746","title":"Novel Insights into Selected Disease-Causing Mutations within the SLC35A1 Gene Encoding the CMP-Sialic Acid Transporter.","date":"2020","source":"International journal of molecular sciences","url":"https://pubmed.ncbi.nlm.nih.gov/33396746","citation_count":19,"is_preprint":false},{"pmid":"24737687","id":"PMC_24737687","title":"Fluorescent mimetics of CMP-Neu5Ac are highly potent, cell-permeable polarization probes of eukaryotic and bacterial sialyltransferases and inhibit cellular sialylation.","date":"2014","source":"Angewandte Chemie (International ed. in English)","url":"https://pubmed.ncbi.nlm.nih.gov/24737687","citation_count":19,"is_preprint":false},{"pmid":"1820197","id":"PMC_1820197","title":"Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.","date":"1991","source":"Glycobiology","url":"https://pubmed.ncbi.nlm.nih.gov/1820197","citation_count":19,"is_preprint":false},{"pmid":"31681287","id":"PMC_31681287","title":"N-Glycolylneuraminic Acid (Neu5Gc) Null Large Animals by Targeting the CMP-Neu5Gc Hydroxylase (CMAH).","date":"2019","source":"Frontiers in immunology","url":"https://pubmed.ncbi.nlm.nih.gov/31681287","citation_count":18,"is_preprint":false},{"pmid":"32971290","id":"PMC_32971290","title":"Unliganded and CMP-Neu5Ac bound structures of human α-2,6-sialyltransferase ST6Gal I at high resolution.","date":"2020","source":"Journal of structural biology","url":"https://pubmed.ncbi.nlm.nih.gov/32971290","citation_count":18,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":53491,"output_tokens":665,"usd":0.085224,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6727,"output_tokens":1022,"usd":0.029593,"stage2_stop_reason":"end_turn"},"total_usd":0.114817,"stage1_batch_id":"msgbatch_01BbTCMyrRPyhtEq6b1MdwCN","stage2_batch_id":"msgbatch_011dEed5bbxYvTAaQWKJevxu","note":"batch pricing = 50% of standard"},"stage1_raw":"Looking through the abstracts, I need to identify papers about MATN1 (also known as CRTM or CMP - cartilage matrix protein/matrilin-1). Most papers in this corpus are about completely different molecules that share the \"CMP\" abbreviation (CMP-sialic acid, cytidine monophosphate, etc.) or other unrelated genes.\n\nPapers relevant to MATN1:\n- Paper [28]: About CMP/Matrilin-1 (cartilage matrix protein) - directly relevant, describes integrin binding\n- Paper [54]: About CRTM gene and osteoarthritis association - genetic association, no mechanism\n- Paper [45]: About MATN1 gene and scoliosis - linkage study, no mechanism\n- Paper [39]: MATN1 SNP association - no mechanism\n- Paper [78]: Uses CMP coiled-coil domain of cartilage matrix protein as an engineering tool - provides some structural/functional info about the CMP domain\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 1999,\n      \"finding\": \"Cartilage matrix protein (CMP/matrilin-1) promotes cell adhesion and spreading of chondrocytes and fibroblasts via integrin α1β1. Monoclonal antibody to integrin α1 or β1 abolished CMP-induced cell adhesion, while antibodies to other integrin subunits had little effect. Co-immunoprecipitation of 125I-CMP with integrin α1 from cell lysates confirmed direct association with the α1 subunit. Synergistic spreading enhancement required native (not denatured) type II collagen.\",\n      \"method\": \"Cell adhesion assay on CMP-coated dishes, blocking antibodies to specific integrin subunits, co-immunoprecipitation of radiolabeled CMP with integrin α1 from cell lysates\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal binding confirmed by co-IP and competition assay, functional blocking by specific antibody, single lab with two orthogonal methods\",\n      \"pmids\": [\"10196235\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"Matrilin-1 (MATN1/CMP/CRTM) is a cartilage extracellular matrix protein that promotes chondrocyte and fibroblast adhesion and spreading by binding directly to integrin α1β1, with synergistic activity in the presence of native type II collagen; its coiled-coil domain mediates oligomerization, but the broader mechanistic understanding of its function in cartilage development and matrix assembly remains limited in the available literature.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"Matrilin-1 (MATN1/CMP) is a cartilage extracellular matrix protein that promotes adhesion and spreading of chondrocytes and fibroblasts by binding directly to the integrin α1 subunit of α1β1 integrin [#0]. This adhesive activity is integrin-specific: blocking antibodies against the α1 or β1 subunits abolish CMP-induced cell adhesion, whereas antibodies to other integrin subunits have little effect, and co-immunoprecipitation of radiolabeled CMP with integrin α1 confirms a direct association [#0]. Its spreading-promoting function is synergistically enhanced in the presence of native, but not denatured, type II collagen [#0]. Beyond this integrin-mediated adhesion role, no further mechanistic detail on matrilin-1 in cartilage matrix assembly has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 1999,\n      \"claim\": \"Established that matrilin-1 is not merely a structural matrix component but an active adhesive ligand, identifying integrin α1β1 as its direct cell-surface receptor and pinpointing the α1 subunit as the binding partner.\",\n      \"evidence\": \"Cell adhesion/spreading assays on CMP-coated surfaces with integrin subunit-specific blocking antibodies, plus co-immunoprecipitation of radiolabeled CMP with integrin α1 and synergy assays with native type II collagen\",\n      \"pmids\": [\n        \"10196235\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"The CMP domain mediating integrin α1 binding was not mapped\",\n        \"The molecular basis of the synergy with native type II collagen was not defined\",\n        \"Single-lab finding without independent reciprocal confirmation of the direct α1 interaction\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How matrilin-1 contributes to cartilage matrix assembly and development at the molecular level, and the structural determinants of its receptor and collagen interactions, remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structural model of the integrin α1β1 interaction surface\",\n        \"No in vivo phenotype linking the adhesive activity to cartilage development\",\n        \"Mechanism of collagen-dependent spreading synergy uncharacterized\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0098631\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0031012\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"pathway\": [],\n    \"complexes\": [],\n    \"partners\": [\n      \"ITGA1\",\n      \"ITGB1\",\n      \"COL2A1\"\n    ],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":2,"faith_total":3,"faith_pct":66.66666666666667}}