{"gene":"VIM","run_date":"2026-06-11T09:02:06","timeline":{"discoveries":[{"year":2017,"finding":"BPIFB1 physically interacts with vimentin (VIM) in NPC cells, as demonstrated by co-immunoprecipitation coupled with mass spectrometry, and this interaction attenuates VIM-induced epithelial-mesenchymal transition, thereby inhibiting nasopharyngeal carcinoma cell migration and invasion.","method":"Co-immunoprecipitation with mass spectrometry, western blotting, immunofluorescence, in vitro migration/invasion assays","journal":"British journal of cancer","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — single lab, Co-IP/MS identification of interaction with functional follow-up by migration assays, but no reconstitution or structural validation","pmids":["29123267"],"is_preprint":false},{"year":2018,"finding":"FSTL1 interacts with vimentin (VIM) as identified by co-immunoprecipitation, and this interaction promotes colorectal cancer cell migration, invasion, and cytoskeletal rearrangement via activation of the focal adhesion signaling pathway.","method":"Co-immunoprecipitation to identify VIM as FSTL1-binding partner, functional assays (migration, invasion), western blotting","journal":"Cell death & disease","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — single lab, Co-IP identification with functional phenotypic follow-up, no reconstitution","pmids":["29844309"],"is_preprint":false},{"year":2019,"finding":"Autophagy induction in synovial fibroblasts promotes citrullination of vimentin (VIM), generating citrullinated VIM (cVIM), and cVIM physically interacts with MHC class II molecules as demonstrated by co-immunoprecipitation and proximity ligation assay, suggesting a mechanism by which autophagy promotes autoantigen presentation in rheumatoid arthritis.","method":"Co-immunoprecipitation, proximity ligation assay, immunoblotting with ACPA-positive RA patient sera, autophagy inhibitor (3-MA) experiments","journal":"Autophagy","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP plus proximity ligation assay in single lab, two orthogonal methods confirming interaction","pmids":["31486697"],"is_preprint":false},{"year":2015,"finding":"WWOX expression in endometrial cancer cells inversely correlates with VIM protein expression and positively with CDH1, placing VIM downstream of WWOX in the regulation of EMT; WWOX overexpression suppressed mesenchymal markers including VIM while altering cell adhesion and migration.","method":"Retroviral WWOX overexpression in ECC1 cells, western blotting for VIM/CDH1/ZEB1/SNAI1 protein levels, RT-qPCR, functional assays (adhesion, migration, MMP activity), DNA microarray","journal":"International journal of oncology","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single OE system, VIM regulation inferred from expression changes without direct mechanistic link to WWOX","pmids":["25892250"],"is_preprint":false},{"year":2022,"finding":"Genetic deletion of vimentin (VIM) in mice results in failure to complete vascular remodeling and closure of the ductus arteriosus. Single-cell RNA-sequencing and transgenic mouse studies showed that vimentin-null mice phenocopy patent ductus arteriosus associated with Jagged1/Notch3 pathway disruption, placing VIM upstream of Notch3 signaling in ductal closure.","method":"Vimentin knockout mouse model, single-cell RNA-sequencing of ductus arteriosus at E18.5/P0.5/P5, immunohistochemistry, genetic epistasis with Jagged1-deleted mice","journal":"Arteriosclerosis, thrombosis, and vascular biology","confidence":"High","confidence_rationale":"Tier 2 / Strong — genetic KO with defined vascular phenotype, scRNA-seq pathway analysis, epistasis with Jagged1/Notch3 pathway, multiple orthogonal methods in one study","pmids":["35443793"],"is_preprint":false},{"year":2023,"finding":"METTL3-mediated m6A modification downregulates VIM expression in neurons; EGR1 transcriptionally activates METTL3, which in turn suppresses VIM, reducing hippocampal neuron injury and apoptosis in an epilepsy model. Knockdown of VIM reduced neuronal injury and inflammatory response in vivo.","method":"Loss- and gain-of-function experiments (VIM knockdown), mechanistic assays linking EGR1 → METTL3 → VIM via m6A modification, in vivo kainic acid epilepsy model, immunofluorescence, western blotting","journal":"Neurochemical research","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — single lab, VIM KD with defined neuronal injury phenotype, pathway placement via EGR1/METTL3/m6A axis, multiple methods but not independently replicated","pmids":["37268752"],"is_preprint":false},{"year":2020,"finding":"LINC01503 functions as a competing endogenous RNA (ceRNA) by sponging miR-133a-5p to upregulate VIM expression, promoting epithelial-mesenchymal transition and progression in gastric cardia adenocarcinoma cells.","method":"Luciferase reporter assay, RNA immunoprecipitation (RIP) assay, qRT-PCR, gain-of-function (LINC01503 knockdown), western blotting for VIM and EMT markers","journal":"Digestive diseases and sciences","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, ceRNA mechanism established by luciferase/RIP but VIM regulation is indirect (upstream lncRNA/miRNA), no direct VIM protein mechanistic study","pmids":["33200343"],"is_preprint":false}],"current_model":"Vimentin (VIM) is a type III intermediate filament protein that functions as a structural component regulating cell migration and EMT (interacting with partners such as BPIFB1 and FSTL1 via direct protein-protein interactions), undergoes citrullination during autophagy to form complexes with MHC class II in synovial fibroblasts (potentially driving autoimmune antigen presentation in RA), and plays an essential role in vascular remodeling of the ductus arteriosus through a mechanism involving the Notch3/Jagged1 signaling pathway, as established by genetic knockout studies in mice."},"narrative":{"mechanistic_narrative":"Vimentin (VIM) is a type III intermediate filament protein that acts as a structural and signaling node in epithelial-mesenchymal transition (EMT), cell migration, and tissue remodeling, and its level is a frequent target of upstream transcriptional and post-transcriptional control [PMID:29123267, PMID:35443793]. In cancer cells VIM drives a mesenchymal, migratory phenotype: this program is restrained when BPIFB1 physically binds VIM to attenuate VIM-induced EMT and suppress nasopharyngeal carcinoma migration and invasion [PMID:29123267], whereas FSTL1 binding to VIM promotes colorectal cancer migration, invasion, and cytoskeletal rearrangement through focal adhesion signaling [PMID:29844309]. VIM abundance is controlled upstream by multiple regulators, including METTL3-mediated m6A modification that suppresses VIM in neurons downstream of EGR1, limiting hippocampal neuronal injury [PMID:37268752]. Beyond its cancer/cytoskeletal roles, genetic deletion of VIM in mice causes failure of vascular remodeling and patent ductus arteriosus, placing VIM upstream of Jagged1/Notch3 signaling in ductal closure [PMID:35443793]. VIM also undergoes citrullination during autophagy in synovial fibroblasts, and citrullinated VIM physically associates with MHC class II molecules, a mechanism linked to autoantigen presentation in rheumatoid arthritis [PMID:31486697].","teleology":[{"year":2015,"claim":"Established that VIM sits within a regulated EMT program rather than acting autonomously, by showing its expression is inversely coupled to the tumor suppressor WWOX and to the epithelial marker CDH1.","evidence":"Retroviral WWOX overexpression in endometrial cancer cells with western blotting and functional adhesion/migration assays","pmids":["25892250"],"confidence":"Low","gaps":["VIM regulation inferred from expression correlation, not a direct mechanistic link to WWOX","no demonstration that VIM is required for the WWOX migratory phenotype"]},{"year":2017,"claim":"Identified BPIFB1 as a direct VIM-binding partner that suppresses VIM-induced EMT, defining a protein-protein interaction that restrains the pro-migratory function of VIM.","evidence":"Co-immunoprecipitation/mass spectrometry and in vitro migration/invasion assays in nasopharyngeal carcinoma cells","pmids":["29123267"],"confidence":"Medium","gaps":["no reconstitution or structural mapping of the interaction interface","single-lab finding without reciprocal validation in other tumor types"]},{"year":2018,"claim":"Showed that a different partner, FSTL1, binds VIM to promote migration and cytoskeletal rearrangement, establishing VIM as a bidirectional effector whose output depends on its interacting partner.","evidence":"Co-immunoprecipitation and migration/invasion assays in colorectal cancer cells, with focal adhesion pathway readouts","pmids":["29844309"],"confidence":"Medium","gaps":["interaction not validated by reconstitution","molecular basis linking VIM-FSTL1 binding to focal adhesion activation not resolved"]},{"year":2019,"claim":"Linked a post-translational modification of VIM to immune function, demonstrating that autophagy-driven citrullination of VIM generates a form that physically associates with MHC class II, providing a mechanism for autoantigen presentation.","evidence":"Reciprocal Co-IP, proximity ligation assay, and ACPA-positive RA sera with autophagy inhibitor experiments in synovial fibroblasts","pmids":["31486697"],"confidence":"Medium","gaps":["does not establish the citrullination sites or enzyme responsible","MHC class II association not shown to functionally drive T-cell activation in this study"]},{"year":2020,"claim":"Placed VIM under post-transcriptional control by a ceRNA circuit, showing LINC01503 sponges miR-133a-5p to upregulate VIM and promote EMT.","evidence":"Luciferase reporter and RNA immunoprecipitation assays with knockdown in gastric cardia adenocarcinoma cells","pmids":["33200343"],"confidence":"Low","gaps":["VIM regulation is indirect via the lncRNA/miRNA axis","no direct study of VIM protein function in this context"]},{"year":2022,"claim":"Demonstrated an in vivo developmental requirement for VIM, showing that knockout causes failed vascular remodeling and patent ductus arteriosus, and genetically placed VIM upstream of Jagged1/Notch3 signaling.","evidence":"Vimentin knockout mouse, single-cell RNA-sequencing of the ductus arteriosus, immunohistochemistry, and epistasis with Jagged1-deleted mice","pmids":["35443793"],"confidence":"High","gaps":["molecular mechanism by which a cytoskeletal protein controls Notch3 ligand signaling is not defined","cell-type-autonomous versus systemic contribution not dissected"]},{"year":2023,"claim":"Extended upstream regulation of VIM to the nervous system, showing EGR1-induced METTL3 deposits m6A on VIM to suppress its expression and limit neuronal injury, establishing VIM as a damage-promoting effector in epilepsy.","evidence":"VIM knockdown and EGR1/METTL3/m6A pathway assays in a kainic acid epilepsy model with immunofluorescence and western blotting","pmids":["37268752"],"confidence":"Medium","gaps":["specific m6A sites on VIM mRNA not mapped","not independently replicated"]},{"year":null,"claim":"How VIM's cytoskeletal/filament structure mechanistically couples to its diverse partner-dependent signaling outputs (EMT regulation, Notch3 control, MHC class II presentation) remains unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["no structural model linking partner binding to filament dynamics in the corpus","the unifying biochemical mechanism across cancer, vascular, immune, and neuronal contexts is not established"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0005198","term_label":"structural molecule activity","supporting_discovery_ids":[0,1]},{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[1]}],"localization":[{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[1]}],"pathway":[{"term_id":"R-HSA-1266738","term_label":"Developmental Biology","supporting_discovery_ids":[4]}],"complexes":[],"partners":["BPIFB1","FSTL1","MHC CLASS II"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"P08670","full_name":"Vimentin","aliases":[],"length_aa":466,"mass_kda":53.7,"function":"Vimentins are class-III intermediate filaments found in various non-epithelial cells, especially mesenchymal cells. Vimentin is attached to the nucleus, endoplasmic reticulum, and mitochondria, either laterally or terminally. Plays a role in cell directional movement, orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity). Protects SCRIB from proteasomal degradation and facilitates its localization to intermediate filaments in a cell contact-mediated manner (By similarity). May promote axon outgrowth and motor fiber repair via DSP-mediated recruitment to outgrowth tips (By similarity) Involved with LARP6 in the stabilization of type I collagen mRNAs for CO1A1 and CO1A2","subcellular_location":"Cytoplasm; Cytoplasm, cytoskeleton; Nucleus matrix; Cell membrane; Cell projection, axon","url":"https://www.uniprot.org/uniprotkb/P08670/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/VIM","classification":"Not Classified","n_dependent_lines":0,"n_total_lines":1208,"dependency_fraction":0.0},"opencell":{"profiled":true,"resolved_as":"","ensg_id":"ENSG00000026025","cell_line_id":"CID000838","localizations":[{"compartment":"cytoskeleton","grade":3},{"compartment":"membrane","grade":1}],"interactors":[{"gene":"RAB11A","stoichiometry":10.0},{"gene":"CALD1","stoichiometry":0.2},{"gene":"CALM3","stoichiometry":0.2},{"gene":"CAPZB","stoichiometry":0.2},{"gene":"CTTN","stoichiometry":0.2},{"gene":"HSPBP1","stoichiometry":0.2},{"gene":"LMNB1","stoichiometry":0.2},{"gene":"MAPRE1","stoichiometry":0.2},{"gene":"NES","stoichiometry":0.2},{"gene":"NEFM","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/target/CID000838","total_profiled":1310},"omim":[{"mim_id":"621465","title":"ITPRIP-LIKE PROTEIN 2; ITPRIPL2","url":"https://www.omim.org/entry/621465"},{"mim_id":"620162","title":"ZINC FINGER PROTEIN 471; ZNF471","url":"https://www.omim.org/entry/620162"},{"mim_id":"619982","title":"VIM ANTISENSE RNA 1; VIMAS1","url":"https://www.omim.org/entry/619982"},{"mim_id":"619713","title":"CADHERIN-RELATED FAMILY, MEMBER 2; CDHR2","url":"https://www.omim.org/entry/619713"},{"mim_id":"618993","title":"RING FINGER PROTEIN 208; RNF208","url":"https://www.omim.org/entry/618993"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Intermediate filaments","reliability":"Supported"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in all","driving_tissues":[{"tissue":"blood vessel","ntpm":5524.1}],"url":"https://www.proteinatlas.org/search/VIM"},"hgnc":{"alias_symbol":[],"prev_symbol":[]},"alphafold":{"accession":"P08670","domains":[],"viewer_url":"https://alphafold.ebi.ac.uk/entry/P08670","model_url":"https://alphafold.ebi.ac.uk/files/AF-P08670-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-P08670-F1-predicted_aligned_error_v6.png","plddt_mean":77.06},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=VIM","jax_strain_url":"https://www.jax.org/strain/search?query=VIM"},"sequence":{"accession":"P08670","fasta_url":"https://rest.uniprot.org/uniprotkb/P08670.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/P08670/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/P08670"}},"corpus_meta":[{"pmid":"10722487","id":"PMC_10722487","title":"Characterization of VIM-2, a carbapenem-hydrolyzing metallo-beta-lactamase and its plasmid- and integron-borne gene from a Pseudomonas aeruginosa clinical 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microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/21449842","citation_count":27,"is_preprint":false},{"pmid":"37471423","id":"PMC_37471423","title":"In silico designing and immunoinformatics analysis of a novel peptide vaccine against metallo-beta-lactamase (VIM and IMP) variants.","date":"2023","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/37471423","citation_count":27,"is_preprint":false},{"pmid":"29979638","id":"PMC_29979638","title":"High Prevalence of VIM, KPC, and NDM Expression among Surgical Site Infection Pathogens in Patients Having Emergency Surgery.","date":"2018","source":"Surgical infections","url":"https://pubmed.ncbi.nlm.nih.gov/29979638","citation_count":25,"is_preprint":false},{"pmid":"1690317","id":"PMC_1690317","title":"Distribution of VIM-2 and SSEA-1 glycoconjugate epitopes among human leukocytes and leukemia cells.","date":"1990","source":"Leukemia research","url":"https://pubmed.ncbi.nlm.nih.gov/1690317","citation_count":25,"is_preprint":false},{"pmid":"18519714","id":"PMC_18519714","title":"VIM-15 and VIM-16, two new VIM-2-like metallo-beta-lactamases in Pseudomonas aeruginosa isolates from Bulgaria and Germany.","date":"2008","source":"Antimicrobial agents and chemotherapy","url":"https://pubmed.ncbi.nlm.nih.gov/18519714","citation_count":25,"is_preprint":false},{"pmid":"31744917","id":"PMC_31744917","title":"A Single Salt Bridge in VIM-20 Increases Protein Stability and Antibiotic Resistance under Low-Zinc Conditions.","date":"2019","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/31744917","citation_count":24,"is_preprint":false},{"pmid":"33957287","id":"PMC_33957287","title":"First report of a blaVIM-1 metallo-β-lactamase-possessing Klebsiella michiganensis.","date":"2021","source":"Journal of global antimicrobial 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Tunisian hospital.","date":"2011","source":"APMIS : acta pathologica, microbiologica, et immunologica Scandinavica","url":"https://pubmed.ncbi.nlm.nih.gov/21917010","citation_count":22,"is_preprint":false},{"pmid":"30589602","id":"PMC_30589602","title":"Identification of blaVIM-1 Gene in ST307 and ST661 Klebsiella pneumoniae Clones in Italy: Old Acquaintances for New Combinations.","date":"2018","source":"Microbial drug resistance (Larchmont, N.Y.)","url":"https://pubmed.ncbi.nlm.nih.gov/30589602","citation_count":22,"is_preprint":false},{"pmid":"33173977","id":"PMC_33173977","title":"lncRNA VIM‑AS1 promotes cell proliferation, metastasis and epithelial‑mesenchymal transition by activating the Wnt/β‑catenin pathway in gastric cancer.","date":"2020","source":"Molecular medicine reports","url":"https://pubmed.ncbi.nlm.nih.gov/33173977","citation_count":21,"is_preprint":false},{"pmid":"24763874","id":"PMC_24763874","title":"Microbiological and molecular detection of VIM-1 metallo beta 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NDM-1 and VIM-2 Metallo-β-Lactamases in Myanmar.","date":"2019","source":"Antimicrobial agents and chemotherapy","url":"https://pubmed.ncbi.nlm.nih.gov/31138570","citation_count":21,"is_preprint":false},{"pmid":"25601024","id":"PMC_25601024","title":"Structural and biochemical characterization of VIM-26 shows that Leu224 has implications for the substrate specificity of VIM metallo-β-lactamases.","date":"2015","source":"The FEBS journal","url":"https://pubmed.ncbi.nlm.nih.gov/25601024","citation_count":21,"is_preprint":false},{"pmid":"26638216","id":"PMC_26638216","title":"Nosocomial dissemination of VIM-2-producing ST235 Pseudomonas aeruginosa in Lithuania.","date":"2015","source":"European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/26638216","citation_count":21,"is_preprint":false},{"pmid":"24390932","id":"PMC_24390932","title":"Emergence of VIM-producing Aeromonas caviae in Israeli hospitals.","date":"2014","source":"The Journal of antimicrobial chemotherapy","url":"https://pubmed.ncbi.nlm.nih.gov/24390932","citation_count":20,"is_preprint":false},{"pmid":"17341470","id":"PMC_17341470","title":"Characterization of In3Mor, a new integron carrying VIM-1 metallo-beta-lactamase and sat1 gene, from Morganella morganii.","date":"2007","source":"The Journal of antimicrobial chemotherapy","url":"https://pubmed.ncbi.nlm.nih.gov/17341470","citation_count":20,"is_preprint":false},{"pmid":"34961397","id":"PMC_34961397","title":"Discovery of phyto-compounds as novel inhibitors against NDM-1 and VIM-1 protein through virtual screening and molecular modelling.","date":"2021","source":"Journal of biomolecular structure & dynamics","url":"https://pubmed.ncbi.nlm.nih.gov/34961397","citation_count":19,"is_preprint":false},{"pmid":"34861315","id":"PMC_34861315","title":"Nosocomial outbreak of monoclonal VIM carbapenemase-producing Enterobacter cloacae complex in an intensive care unit during the COVID-19 pandemic: an integrated approach.","date":"2021","source":"The Journal of hospital infection","url":"https://pubmed.ncbi.nlm.nih.gov/34861315","citation_count":19,"is_preprint":false},{"pmid":"33526490","id":"PMC_33526490","title":"Epidemic Territorial Spread of IncP-2-Type VIM-2 Carbapenemase-Encoding Megaplasmids in Nosocomial Pseudomonas aeruginosa Populations.","date":"2021","source":"Antimicrobial agents and chemotherapy","url":"https://pubmed.ncbi.nlm.nih.gov/33526490","citation_count":19,"is_preprint":false},{"pmid":"34954336","id":"PMC_34954336","title":"Emergence of ST39 carbapenem-resistant Klebsiella pneumoniae producing VIM-1 and KPC-2.","date":"2021","source":"Microbial pathogenesis","url":"https://pubmed.ncbi.nlm.nih.gov/34954336","citation_count":18,"is_preprint":false},{"pmid":"33418979","id":"PMC_33418979","title":"Genomic Characterization of VIM and MCR Co-Producers: The First Two Clinical Cases, in Italy.","date":"2021","source":"Diagnostics (Basel, Switzerland)","url":"https://pubmed.ncbi.nlm.nih.gov/33418979","citation_count":18,"is_preprint":false},{"pmid":"37195077","id":"PMC_37195077","title":"Antimicrobial Activity of Cefiderocol against the Carbapenemase-Producing Enterobacter cloacae Complex and Characterization of Reduced Susceptibility Associated with Metallo-β-Lactamase VIM-1.","date":"2023","source":"Antimicrobial agents and chemotherapy","url":"https://pubmed.ncbi.nlm.nih.gov/37195077","citation_count":18,"is_preprint":false},{"pmid":"25897818","id":"PMC_25897818","title":"Inhibiting the VIM-2 Metallo-β-Lactamase by Graphene Oxide and Carbon Nanotubes.","date":"2015","source":"ACS applied materials & interfaces","url":"https://pubmed.ncbi.nlm.nih.gov/25897818","citation_count":18,"is_preprint":false},{"pmid":"37004745","id":"PMC_37004745","title":"Single-cell RNA sequencing reveals that VIM and IFITM3 are vital targets of Dengzhan Shengmai capsule to protect against cerebral ischemic injury.","date":"2023","source":"Journal of ethnopharmacology","url":"https://pubmed.ncbi.nlm.nih.gov/37004745","citation_count":17,"is_preprint":false},{"pmid":"24762702","id":"PMC_24762702","title":"VIM proteins regulate transcription exclusively through the MET1 cytosine methylation pathway.","date":"2014","source":"Epigenetics","url":"https://pubmed.ncbi.nlm.nih.gov/24762702","citation_count":17,"is_preprint":false},{"pmid":"31685789","id":"PMC_31685789","title":"Long Noncoding RNA VIM Antisense RNA 1 (VIM-AS1) Plays an Important Role in Development of Preeclampsia by Regulation of Epithelial Mesenchymal Transition.","date":"2019","source":"Medical science monitor : international medical journal of experimental and clinical research","url":"https://pubmed.ncbi.nlm.nih.gov/31685789","citation_count":17,"is_preprint":false},{"pmid":"37268752","id":"PMC_37268752","title":"EGR1-Driven METTL3 Activation Curtails VIM-Mediated Neuron Injury in Epilepsy.","date":"2023","source":"Neurochemical research","url":"https://pubmed.ncbi.nlm.nih.gov/37268752","citation_count":16,"is_preprint":false},{"pmid":"36734275","id":"PMC_36734275","title":"VIM‑AS1 promotes proliferation and drives enzalutamide resistance in prostate cancer via IGF2BP2‑mediated HMGCS1 mRNA stabilization.","date":"2023","source":"International journal of oncology","url":"https://pubmed.ncbi.nlm.nih.gov/36734275","citation_count":16,"is_preprint":false},{"pmid":"36924802","id":"PMC_36924802","title":"Insight into phylogenomic bias of blaVIM-2 or blaNDM-1 dissemination amongst carbapenem-resistant Pseudomonas aeruginosa.","date":"2023","source":"International journal of antimicrobial agents","url":"https://pubmed.ncbi.nlm.nih.gov/36924802","citation_count":16,"is_preprint":false},{"pmid":"33902589","id":"PMC_33902589","title":"The VIM-AS1/miR-655/ZEB1 axis modulates bladder cancer cell metastasis by regulating epithelial-mesenchymal transition.","date":"2021","source":"Cancer cell international","url":"https://pubmed.ncbi.nlm.nih.gov/33902589","citation_count":16,"is_preprint":false},{"pmid":"31189558","id":"PMC_31189558","title":"Detection of VIM-1-Producing Enterobacter cloacae and Salmonella enterica Serovars Infantis and Goldcoast at a Breeding Pig Farm in Germany in 2017 and Their Molecular Relationship to Former VIM-1-Producing S. Infantis Isolates in German Livestock Production.","date":"2019","source":"mSphere","url":"https://pubmed.ncbi.nlm.nih.gov/31189558","citation_count":16,"is_preprint":false},{"pmid":"23791387","id":"PMC_23791387","title":"Probe ligation and real-time detection of KPC, OXA-48, VIM, IMP, and NDM carbapenemase genes.","date":"2013","source":"Diagnostic microbiology and infectious disease","url":"https://pubmed.ncbi.nlm.nih.gov/23791387","citation_count":16,"is_preprint":false},{"pmid":"32633376","id":"PMC_32633376","title":"Knockdown of long non-coding RNA VIM-AS1 inhibits glioma cell proliferation and migration, and increases the cell apoptosis via modulation of WEE1 targeted by miR-105-5p.","date":"2020","source":"European review for medical and pharmacological sciences","url":"https://pubmed.ncbi.nlm.nih.gov/32633376","citation_count":15,"is_preprint":false},{"pmid":"17944487","id":"PMC_17944487","title":"Molecular cloning and biochemical characterization of VIM-12, a novel hybrid VIM-1/VIM-2 metallo-beta-lactamase from a Klebsiella pneumoniae clinical isolate, reveal atypical substrate specificity.","date":"2007","source":"Biochemistry","url":"https://pubmed.ncbi.nlm.nih.gov/17944487","citation_count":15,"is_preprint":false},{"pmid":"27873597","id":"PMC_27873597","title":"Detection of NDM-2-producing Acinetobacter baumannii and VIM-producing Pseudomonas aeruginosa in Palestine.","date":"2013","source":"Journal of global antimicrobial resistance","url":"https://pubmed.ncbi.nlm.nih.gov/27873597","citation_count":15,"is_preprint":false},{"pmid":"31786880","id":"PMC_31786880","title":"Long non-coding RNA VIM-AS1 promotes prostate cancer growth and invasion by regulating epithelial-mesenchymal transition.","date":"2019","source":"Journal of B.U.ON. : official journal of the Balkan Union of Oncology","url":"https://pubmed.ncbi.nlm.nih.gov/31786880","citation_count":14,"is_preprint":false},{"pmid":"34922269","id":"PMC_34922269","title":"Evaluation of DNA methylation in promoter regions of hTERT, TWIST1, VIM and NID2 genes in Moroccan bladder cancer patients.","date":"2021","source":"Cancer genetics","url":"https://pubmed.ncbi.nlm.nih.gov/34922269","citation_count":14,"is_preprint":false},{"pmid":"31647552","id":"PMC_31647552","title":"Occurrence of intI1-associated VIM-5 carbapenemase and co-existence of all four classes of β-lactamase in carbapenem-resistant clinical Pseudomonas aeruginosa DMC-27b.","date":"2020","source":"The Journal of antimicrobial chemotherapy","url":"https://pubmed.ncbi.nlm.nih.gov/31647552","citation_count":14,"is_preprint":false},{"pmid":"32447557","id":"PMC_32447557","title":"Long non-coding RNA VIM Antisense RNA 1 (VIM-AS1) sponges microRNA-29 to participate in diabetic retinopathy.","date":"2020","source":"Acta diabetologica","url":"https://pubmed.ncbi.nlm.nih.gov/32447557","citation_count":13,"is_preprint":false},{"pmid":"35047418","id":"PMC_35047418","title":"Occurrence of NDM-1, VIM-1, and OXA-10 Co-Producing Providencia rettgeri Clinical Isolate in China.","date":"2022","source":"Frontiers in cellular and infection microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/35047418","citation_count":13,"is_preprint":false},{"pmid":"30829272","id":"PMC_30829272","title":"Examination of methylation changes of VIM, CXCR4, DOK7, and SPDEF genes in peripheral blood DNA in breast cancer patients.","date":"2018","source":"Indian journal of cancer","url":"https://pubmed.ncbi.nlm.nih.gov/30829272","citation_count":13,"is_preprint":false},{"pmid":"22391550","id":"PMC_22391550","title":"Detection and characterization of VIM-31, a new variant of VIM-2 with Tyr224His and His252Arg mutations, in a clinical isolate of Enterobacter cloacae.","date":"2012","source":"Antimicrobial agents and chemotherapy","url":"https://pubmed.ncbi.nlm.nih.gov/22391550","citation_count":13,"is_preprint":false},{"pmid":"27341161","id":"PMC_27341161","title":"Dissemination of a Multidrug-Resistant VIM-1- and CMY-99-Producing Proteus mirabilis Clone in Bulgaria.","date":"2016","source":"Microbial drug resistance (Larchmont, N.Y.)","url":"https://pubmed.ncbi.nlm.nih.gov/27341161","citation_count":12,"is_preprint":false},{"pmid":"25535506","id":"PMC_25535506","title":"Epidemiology of VIM-1-imipenem resistant Pseudomonas aeruginosa in Iran: A systematic review and meta-analysis.","date":"2014","source":"Journal of research in medical sciences : the official journal of Isfahan University of Medical Sciences","url":"https://pubmed.ncbi.nlm.nih.gov/25535506","citation_count":12,"is_preprint":false},{"pmid":"30403360","id":"PMC_30403360","title":"Emergence of blaVEB and blaGES among VIM-producing Pseudomonas aeruginosa clinical isolates in Alexandria, Egypt.","date":"2018","source":"Acta microbiologica et immunologica Hungarica","url":"https://pubmed.ncbi.nlm.nih.gov/30403360","citation_count":12,"is_preprint":false},{"pmid":"35443793","id":"PMC_35443793","title":"Transcriptional Evaluation of the Ductus Arteriosus at the Single-Cell Level Uncovers a Requirement for Vim (Vimentin) for Complete Closure.","date":"2022","source":"Arteriosclerosis, thrombosis, and vascular biology","url":"https://pubmed.ncbi.nlm.nih.gov/35443793","citation_count":12,"is_preprint":false},{"pmid":"28739428","id":"PMC_28739428","title":"Novel class 1 Integrons and sequence types in VIM-2 and VIM-11-producing clinical strains of Enterobacter cloacae.","date":"2017","source":"Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases","url":"https://pubmed.ncbi.nlm.nih.gov/28739428","citation_count":11,"is_preprint":false},{"pmid":"18757180","id":"PMC_18757180","title":"Characterisation of the metallo-beta-lactamase VIM-6 and its genetic support.","date":"2008","source":"International journal of antimicrobial agents","url":"https://pubmed.ncbi.nlm.nih.gov/18757180","citation_count":11,"is_preprint":false},{"pmid":"29978304","id":"PMC_29978304","title":"Characterisation of VIM-2-producing Pseudomonas aeruginosa isolates from lower tract respiratory infections in a Spanish hospital.","date":"2018","source":"European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/29978304","citation_count":11,"is_preprint":false},{"pmid":"39350171","id":"PMC_39350171","title":"DNA methylation analysis of the SDC2, SEPT9 and VIM genes in fecal DNA for colorectal cancer diagnosis.","date":"2024","source":"BMC cancer","url":"https://pubmed.ncbi.nlm.nih.gov/39350171","citation_count":10,"is_preprint":false},{"pmid":"33200343","id":"PMC_33200343","title":"Long Non-coding RNA LINC01503 Promotes Gastric Cardia Adenocarcinoma Progression via miR-133a-5p/VIM Axis and EMT Process.","date":"2020","source":"Digestive diseases and sciences","url":"https://pubmed.ncbi.nlm.nih.gov/33200343","citation_count":10,"is_preprint":false},{"pmid":"39394195","id":"PMC_39394195","title":"An outbreak of blaKPC-4- and blaVIM-1-producing Klebsiella pneumoniae and Klebsiella variicola at a single hospital in South Korea.","date":"2024","source":"Antimicrobial resistance and infection control","url":"https://pubmed.ncbi.nlm.nih.gov/39394195","citation_count":10,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":57415,"output_tokens":2275,"usd":0.103185,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":8780,"output_tokens":2593,"usd":0.054363,"stage2_stop_reason":"end_turn"},"total_usd":0.157548,"stage1_batch_id":"msgbatch_01UT1AahFPCAyn2uVweS7A9z","stage2_batch_id":"msgbatch_01HuKWtKNT4Pqj1bc8eEP5RV","note":"batch pricing = 50% of standard"},"stage1_raw":"Looking at the 100 papers retrieved, I need to classify each one to determine if it's about the canonical human VIM (vimentin) protein or something else.\n\nThe corpus is heavily dominated by papers about:\n1. **VIM metallo-β-lactamases** (bacterial resistance enzymes - \"Verona Integron-encoded Metallo-β-lactamase\") - Papers 1-3, 5-6, 8-9, 11-14, 16, 18, 20-26, 29, 31-35, 37-38, 40-42, 46-49, 51-55, 57-62, 64, 66-70, 77, 79-80, 82-83, 85-86, 88, 90-93, 95-97, 100\n2. **lncRNA VIM-AS1** (non-coding RNA, not the protein) - Papers 30, 39, 56, 74, 76, 78, 81, 84, 87\n3. **circRNA circ-VIM** - Paper 27\n4. **Arabidopsis ORTH/VIM proteins** (plant DNA methylation regulators - symbol collision) - Papers 17, 73\n5. **VIM-2 ganglioside antigen** (carbohydrate epitope, not vimentin protein) - Paper 45\n6. **Human/mammalian vimentin (VIM)** - Papers 7, 10, 28, 50, 72, 75, 94, 99\n\nLet me extract mechanistic discoveries only from papers about canonical human/mammalian vimentin (VIM protein).\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2017,\n      \"finding\": \"BPIFB1 physically interacts with vimentin (VIM) in NPC cells, as demonstrated by co-immunoprecipitation coupled with mass spectrometry, and this interaction attenuates VIM-induced epithelial-mesenchymal transition, thereby inhibiting nasopharyngeal carcinoma cell migration and invasion.\",\n      \"method\": \"Co-immunoprecipitation with mass spectrometry, western blotting, immunofluorescence, in vitro migration/invasion assays\",\n      \"journal\": \"British journal of cancer\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — single lab, Co-IP/MS identification of interaction with functional follow-up by migration assays, but no reconstitution or structural validation\",\n      \"pmids\": [\"29123267\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"FSTL1 interacts with vimentin (VIM) as identified by co-immunoprecipitation, and this interaction promotes colorectal cancer cell migration, invasion, and cytoskeletal rearrangement via activation of the focal adhesion signaling pathway.\",\n      \"method\": \"Co-immunoprecipitation to identify VIM as FSTL1-binding partner, functional assays (migration, invasion), western blotting\",\n      \"journal\": \"Cell death & disease\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — single lab, Co-IP identification with functional phenotypic follow-up, no reconstitution\",\n      \"pmids\": [\"29844309\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2019,\n      \"finding\": \"Autophagy induction in synovial fibroblasts promotes citrullination of vimentin (VIM), generating citrullinated VIM (cVIM), and cVIM physically interacts with MHC class II molecules as demonstrated by co-immunoprecipitation and proximity ligation assay, suggesting a mechanism by which autophagy promotes autoantigen presentation in rheumatoid arthritis.\",\n      \"method\": \"Co-immunoprecipitation, proximity ligation assay, immunoblotting with ACPA-positive RA patient sera, autophagy inhibitor (3-MA) experiments\",\n      \"journal\": \"Autophagy\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP plus proximity ligation assay in single lab, two orthogonal methods confirming interaction\",\n      \"pmids\": [\"31486697\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2015,\n      \"finding\": \"WWOX expression in endometrial cancer cells inversely correlates with VIM protein expression and positively with CDH1, placing VIM downstream of WWOX in the regulation of EMT; WWOX overexpression suppressed mesenchymal markers including VIM while altering cell adhesion and migration.\",\n      \"method\": \"Retroviral WWOX overexpression in ECC1 cells, western blotting for VIM/CDH1/ZEB1/SNAI1 protein levels, RT-qPCR, functional assays (adhesion, migration, MMP activity), DNA microarray\",\n      \"journal\": \"International journal of oncology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single OE system, VIM regulation inferred from expression changes without direct mechanistic link to WWOX\",\n      \"pmids\": [\"25892250\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"Genetic deletion of vimentin (VIM) in mice results in failure to complete vascular remodeling and closure of the ductus arteriosus. Single-cell RNA-sequencing and transgenic mouse studies showed that vimentin-null mice phenocopy patent ductus arteriosus associated with Jagged1/Notch3 pathway disruption, placing VIM upstream of Notch3 signaling in ductal closure.\",\n      \"method\": \"Vimentin knockout mouse model, single-cell RNA-sequencing of ductus arteriosus at E18.5/P0.5/P5, immunohistochemistry, genetic epistasis with Jagged1-deleted mice\",\n      \"journal\": \"Arteriosclerosis, thrombosis, and vascular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — genetic KO with defined vascular phenotype, scRNA-seq pathway analysis, epistasis with Jagged1/Notch3 pathway, multiple orthogonal methods in one study\",\n      \"pmids\": [\"35443793\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"METTL3-mediated m6A modification downregulates VIM expression in neurons; EGR1 transcriptionally activates METTL3, which in turn suppresses VIM, reducing hippocampal neuron injury and apoptosis in an epilepsy model. Knockdown of VIM reduced neuronal injury and inflammatory response in vivo.\",\n      \"method\": \"Loss- and gain-of-function experiments (VIM knockdown), mechanistic assays linking EGR1 → METTL3 → VIM via m6A modification, in vivo kainic acid epilepsy model, immunofluorescence, western blotting\",\n      \"journal\": \"Neurochemical research\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — single lab, VIM KD with defined neuronal injury phenotype, pathway placement via EGR1/METTL3/m6A axis, multiple methods but not independently replicated\",\n      \"pmids\": [\"37268752\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"LINC01503 functions as a competing endogenous RNA (ceRNA) by sponging miR-133a-5p to upregulate VIM expression, promoting epithelial-mesenchymal transition and progression in gastric cardia adenocarcinoma cells.\",\n      \"method\": \"Luciferase reporter assay, RNA immunoprecipitation (RIP) assay, qRT-PCR, gain-of-function (LINC01503 knockdown), western blotting for VIM and EMT markers\",\n      \"journal\": \"Digestive diseases and sciences\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, ceRNA mechanism established by luciferase/RIP but VIM regulation is indirect (upstream lncRNA/miRNA), no direct VIM protein mechanistic study\",\n      \"pmids\": [\"33200343\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"Vimentin (VIM) is a type III intermediate filament protein that functions as a structural component regulating cell migration and EMT (interacting with partners such as BPIFB1 and FSTL1 via direct protein-protein interactions), undergoes citrullination during autophagy to form complexes with MHC class II in synovial fibroblasts (potentially driving autoimmune antigen presentation in RA), and plays an essential role in vascular remodeling of the ductus arteriosus through a mechanism involving the Notch3/Jagged1 signaling pathway, as established by genetic knockout studies in mice.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"Vimentin (VIM) is a type III intermediate filament protein that acts as a structural and signaling node in epithelial-mesenchymal transition (EMT), cell migration, and tissue remodeling, and its level is a frequent target of upstream transcriptional and post-transcriptional control [#0, #4]. In cancer cells VIM drives a mesenchymal, migratory phenotype: this program is restrained when BPIFB1 physically binds VIM to attenuate VIM-induced EMT and suppress nasopharyngeal carcinoma migration and invasion [#0], whereas FSTL1 binding to VIM promotes colorectal cancer migration, invasion, and cytoskeletal rearrangement through focal adhesion signaling [#1]. VIM abundance is controlled upstream by multiple regulators, including METTL3-mediated m6A modification that suppresses VIM in neurons downstream of EGR1, limiting hippocampal neuronal injury [#5]. Beyond its cancer/cytoskeletal roles, genetic deletion of VIM in mice causes failure of vascular remodeling and patent ductus arteriosus, placing VIM upstream of Jagged1/Notch3 signaling in ductal closure [#4]. VIM also undergoes citrullination during autophagy in synovial fibroblasts, and citrullinated VIM physically associates with MHC class II molecules, a mechanism linked to autoantigen presentation in rheumatoid arthritis [#2].\",\n  \"teleology\": [\n    {\n      \"year\": 2015,\n      \"claim\": \"Established that VIM sits within a regulated EMT program rather than acting autonomously, by showing its expression is inversely coupled to the tumor suppressor WWOX and to the epithelial marker CDH1.\",\n      \"evidence\": \"Retroviral WWOX overexpression in endometrial cancer cells with western blotting and functional adhesion/migration assays\",\n      \"pmids\": [\"25892250\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"VIM regulation inferred from expression correlation, not a direct mechanistic link to WWOX\", \"no demonstration that VIM is required for the WWOX migratory phenotype\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Identified BPIFB1 as a direct VIM-binding partner that suppresses VIM-induced EMT, defining a protein-protein interaction that restrains the pro-migratory function of VIM.\",\n      \"evidence\": \"Co-immunoprecipitation/mass spectrometry and in vitro migration/invasion assays in nasopharyngeal carcinoma cells\",\n      \"pmids\": [\"29123267\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"no reconstitution or structural mapping of the interaction interface\", \"single-lab finding without reciprocal validation in other tumor types\"]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Showed that a different partner, FSTL1, binds VIM to promote migration and cytoskeletal rearrangement, establishing VIM as a bidirectional effector whose output depends on its interacting partner.\",\n      \"evidence\": \"Co-immunoprecipitation and migration/invasion assays in colorectal cancer cells, with focal adhesion pathway readouts\",\n      \"pmids\": [\"29844309\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"interaction not validated by reconstitution\", \"molecular basis linking VIM-FSTL1 binding to focal adhesion activation not resolved\"]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"Linked a post-translational modification of VIM to immune function, demonstrating that autophagy-driven citrullination of VIM generates a form that physically associates with MHC class II, providing a mechanism for autoantigen presentation.\",\n      \"evidence\": \"Reciprocal Co-IP, proximity ligation assay, and ACPA-positive RA sera with autophagy inhibitor experiments in synovial fibroblasts\",\n      \"pmids\": [\"31486697\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"does not establish the citrullination sites or enzyme responsible\", \"MHC class II association not shown to functionally drive T-cell activation in this study\"]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Placed VIM under post-transcriptional control by a ceRNA circuit, showing LINC01503 sponges miR-133a-5p to upregulate VIM and promote EMT.\",\n      \"evidence\": \"Luciferase reporter and RNA immunoprecipitation assays with knockdown in gastric cardia adenocarcinoma cells\",\n      \"pmids\": [\"33200343\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"VIM regulation is indirect via the lncRNA/miRNA axis\", \"no direct study of VIM protein function in this context\"]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Demonstrated an in vivo developmental requirement for VIM, showing that knockout causes failed vascular remodeling and patent ductus arteriosus, and genetically placed VIM upstream of Jagged1/Notch3 signaling.\",\n      \"evidence\": \"Vimentin knockout mouse, single-cell RNA-sequencing of the ductus arteriosus, immunohistochemistry, and epistasis with Jagged1-deleted mice\",\n      \"pmids\": [\"35443793\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"molecular mechanism by which a cytoskeletal protein controls Notch3 ligand signaling is not defined\", \"cell-type-autonomous versus systemic contribution not dissected\"]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Extended upstream regulation of VIM to the nervous system, showing EGR1-induced METTL3 deposits m6A on VIM to suppress its expression and limit neuronal injury, establishing VIM as a damage-promoting effector in epilepsy.\",\n      \"evidence\": \"VIM knockdown and EGR1/METTL3/m6A pathway assays in a kainic acid epilepsy model with immunofluorescence and western blotting\",\n      \"pmids\": [\"37268752\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"specific m6A sites on VIM mRNA not mapped\", \"not independently replicated\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How VIM's cytoskeletal/filament structure mechanistically couples to its diverse partner-dependent signaling outputs (EMT regulation, Notch3 control, MHC class II presentation) remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"no structural model linking partner binding to filament dynamics in the corpus\", \"the unifying biochemical mechanism across cancer, vascular, immune, and neuronal contexts is not established\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1266738\", \"supporting_discovery_ids\": [4]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"BPIFB1\", \"FSTL1\", \"MHC class II\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":5,"faith_total":5,"faith_pct":100.0}}