{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Wang X"],"funding":["NIAID NIH HHS","National Institutes of Health","NIAMS NIH HHS","National Institutes of Health Center for Scientific Review"],"pagination":["110513"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12390935"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["301(9)"],"pubmed_abstract":["Genetic association data, immunohistochemistry, and functional experiments implicate protein arginine deiminase 4 (PAD4) in the pathogenesis of rheumatoid arthritis (RA). This disease is characterized by immunity against epitopes with deiminated arginine (=citrulline) originating from a multitude of intra- and extracellular proteins that are modified in this manner only in patients with RA, not in healthy individuals. However, it remains uncertain how, where, and why PAD4 citrullinates these proteins in patients with RA. To gain insights into the physical interactions of PAD4 with other cellular proteins, we identified candidate PAD4-associated proteins by mass spectrometry. PAD4 in neutrophils from patients with RA and healthy controls co-immunoprecipitated with myosin-9 and 20 other prot"],"journal":["The Journal of biological chemistry"],"pubmed_title":["Association of protein arginine deiminase 4 with the myosin-9 motor complex."],"pmcid":["PMC12390935"],"funding_grant_id":["R21 AR077266","T32 AR007108","R01 AR074939","R01 AI186337","R01 AR081654","K08 AR082939"],"pubmed_authors":["An J","Shaikh F","Le E","Wang X","Van der Bogaerde S","Najjar R","Mustelin C","Mustelin T","Moadab F"],"additional_accession":[]},"is_claimable":false,"name":"Association of protein arginine deiminase 4 with the myosin-9 motor complex.","description":"Genetic association data, immunohistochemistry, and functional experiments implicate protein arginine deiminase 4 (PAD4) in the pathogenesis of rheumatoid arthritis (RA). This disease is characterized by immunity against epitopes with deiminated arginine (=citrulline) originating from a multitude of intra- and extracellular proteins that are modified in this manner only in patients with RA, not in healthy individuals. However, it remains uncertain how, where, and why PAD4 citrullinates these proteins in patients with RA. To gain insights into the physical interactions of PAD4 with other cellular proteins, we identified candidate PAD4-associated proteins by mass spectrometry. PAD4 in neutrophils from patients with RA and healthy controls co-immunoprecipitated with myosin-9 and 20 other prot","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jul","modification":"2026-05-28T07:14:16.268Z","creation":"2026-04-08T02:24:26.651Z"},"accession":"S-EPMC12390935","cross_references":{"pubmed":["40707001"],"doi":["10.1016/j.jbc.2025.110513"]}}