{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nCyclophilin A (PPIA) is a dynamic peptidyl‐prolyl cis–trans isomerase whose intrinsic conformational fluctuations are directly coupled to its catalytic function. Detailed NMR and crystallographic studies have demonstrated that these rapid internal motions facilitate substrate turnover by enabling transient active‐site rearrangements that are essential for optimal enzyme catalysis. This fundamental mechanistic insight underscores the importance of PPIA’s conformational dynamics in regulating its isomerase activity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "3"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of viral infections, PPIA plays multifaceted roles that are critical for the viral life cycle. It binds directly to key viral proteins—such as the HIV‐1 capsid and Vpr, hepatitis C virus (HCV) nonstructural proteins, and the SARS‐CoV nucleocapsid—acting as a chaperone that catalyzes cis–trans isomerization and modulates capsid stability, uncoating, and assembly. These interactions not only promote viral replication but also impact host–virus interplay; for example, PPIA is required for efficient HIV‐1 infectivity and HCV RNA replication, while engineered fusion inhibitors using its domains have been developed to block infection. 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"}, {"type": "b", "children": [{"type": "t", "text": "Catalysis of cis/trans isomerization in native HIV-1 capsid by human cyclophilin A."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.082100499"}], "href": "https://doi.org/10.1073/pnas.082100499"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11929983"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11929983"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Theodora Hatziioannou, David Perez-Caballero, Simone Cowan, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Regulation of the tyrosine kinase Itk by the peptidyl-prolyl isomerase cyclophilin A."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.042529199"}], "href": "https://doi.org/10.1073/pnas.042529199"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11830645"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11830645"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Qing Huai, Hwa-Young Kim, Yudong Liu, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Crystal structure of calcineurin-cyclophilin-cyclosporin shows common but distinct recognition of immunophilin-drug complexes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2002)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.192206699"}], "href": "https://doi.org/10.1073/pnas.192206699"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "12218175"}], "href": "https://pubmed.ncbi.nlm.nih.gov/12218175"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Céline Candé, Nicola Vahsen, Ilektra Kouranti, et al. "}, {"type": "b", "children": [{"type": "t", "text": "AIF and cyclophilin A cooperate in apoptosis-associated chromatinolysis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/sj.onc.1207279"}], "href": "https://doi.org/10.1038/sj.onc.1207279"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "14716299"}], "href": "https://pubmed.ncbi.nlm.nih.gov/14716299"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Zheng-Gen Jin, Andreea O Lungu, Liang Xie, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Cyclophilin A is an essential cofactor for hepatitis C virus infection and the principal mediator of cyclosporine resistance in vitro."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Virol (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1128/JVI.02614-07"}], "href": "https://doi.org/10.1128/JVI.02614-07"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18385230"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18385230"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Heng Pan, Cherry Luo, Runsheng Li, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cyclophilin A is required for CXCR4-mediated nuclear export of heterogeneous nuclear ribonucleoprotein A2, activation and nuclear translocation of ERK1/2, and chemotactic cell migration."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M704934200"}], "href": "https://doi.org/10.1074/jbc.M704934200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17991743"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17991743"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Tsai-Yu Lin, Michael Emerman "}, {"type": "b", "children": [{"type": "t", "text": "Cyclophilin A interacts with diverse lentiviral capsids."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Retrovirology (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1186/1742-4690-3-70"}], "href": "https://doi.org/10.1186/1742-4690-3-70"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17038183"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17038183"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Peter Seizer, Saskia N I V Ungern-Sternberg, Tanja Schönberger, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Extracellular cyclophilin A activates platelets via EMMPRIN (CD147) and PI3K/Akt signaling, which promotes platelet adhesion and thrombus formation in vitro and in vivo."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Arterioscler Thromb Vasc Biol (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1161/ATVBAHA.114.305112"}], "href": "https://doi.org/10.1161/ATVBAHA.114.305112"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "25550208"}], "href": "https://pubmed.ncbi.nlm.nih.gov/25550208"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Amanda M Saratsis, Sridevi Yadavilli, Suresh Magge, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Insights into pediatric diffuse intrinsic pontine glioma through proteomic analysis of cerebrospinal fluid."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Neuro Oncol (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/neuonc/nos067"}], "href": "https://doi.org/10.1093/neuonc/nos067"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22492959"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22492959"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Farman Ullah Dawar, Yang Xiong, Muhammad Nasir Khan Khattak, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Potential role of cyclophilin A in regulating cytokine secretion."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Leukoc Biol (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1189/jlb.3RU0317-090RR"}], "href": "https://doi.org/10.1189/jlb.3RU0317-090RR"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28729360"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28729360"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "Fei Song, Xin Zhang, Xiao-Bai Ren, et al. 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"}, {"type": "b", "children": [{"type": "t", "text": "Prolyl isomerase cyclophilin A regulation of Janus-activated kinase 2 and the progression of human breast cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cancer Res (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1158/0008-5472.CAN-08-0639"}], "href": "https://doi.org/10.1158/0008-5472.CAN-08-0639"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18829531"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18829531"}]}]}]}