{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nCyclophilin B (PPIB) functions as a prolyl cis–trans isomerase that is critical for proper viral protein conformational dynamics. In hepatitis C virus, for example, PPIB directly interacts with the viral RNA polymerase NS5B to stimulate its RNA binding activity and thereby enhance genome replication. In addition, PPIB binds to disordered regions of viral proteins such as NS5A, serving as a substrate for its isomerization and indirectly promoting the activation of antiviral transcription factors like IRF‐3. Studies in Japanese encephalitis virus further demonstrate that the peptidyl–prolyl isomerase activity of PPIB is indispensable for efficient viral propagation, underlining its broad role as a regulatory cofactor in virus–host interactions."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the endoplasmic reticulum, PPIB is a key component of a multi‐protein collagen–modifying complex that also includes cartilage–associated protein and prolyl 3–hydroxylase 1. This ternary assembly catalyzes the 3–hydroxylation of specific prolines and drives the cis–to–trans isomerization reactions required for proper triple–helix formation in type I procollagen. Mutations in the PPIB gene disrupt the function of this complex and are associated with recessively inherited osteogenesis imperfecta, highlighting the importance of PPIB’s chaperone and isomerase activities for skeletal integrity."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "6", "end_ref": "11"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its roles in viral replication and collagen biosynthesis, PPIB exerts multifaceted functions in cellular signaling, protein homeostasis, and pathophysiological stress responses. As an endoplasmic reticulum chaperone, it cooperates with lectin chaperones (e.g., calnexin, calreticulin) to assist in the folding of glycoproteins and contributes to the maintenance of ER redox balance. Cell surface–localized and secreted pools of PPIB interact with receptors such as CD147 (and in cooperation with CD98) to modulate intracellular signaling pathways that regulate chemotaxis, adhesion, and the activation of transcription factors including Stat3—thereby influencing inflammation and tumorigenesis in breast, colon, hepatocellular, and glioblastoma contexts. PPIB has also been implicated in the regulation of calcium channel activity in epithelial cells, in the secretion of key enzymes and transporters, and in the modulation of apoptotic signaling under conditions of oxidative and ER stress. Moreover, secreted PPIB participates in intercellular communication and has shown potential as a diagnostic biomarker in pancreatic cancer and as a modulator of prolactin availability in milk. Collectively, these findings reveal that PPIB’s peptidyl–prolyl isomerase and chaperone functions span viral life cycles, extracellular matrix formation, cell adhesion, and stress adaptation, establishing it as a pivotal regulator in both normal physiology and disease."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "12", "end_ref": "33"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Yoko Obata, Kazuo Yamamoto, Masanobu Miyazaki, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Role of cyclophilin B in activation of interferon regulatory factor-3."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M501684200"}], "href": "https://doi.org/10.1074/jbc.M501684200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15764595"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15764595"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Koichi Watashi, Naoto Ishii, Makoto Hijikata, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cyclophilin B is a functional regulator of hepatitis C virus RNA polymerase."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Mol Cell (2005)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.molcel.2005.05.014"}], "href": "https://doi.org/10.1016/j.molcel.2005.05.014"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15989969"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15989969"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Xavier Hanoulle, Aurélie Badillo, Jean-Michel Wieruszeski, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Hepatitis C virus NS5A protein is a substrate for the peptidyl-prolyl cis/trans isomerase activity of cyclophilins A and B."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M809244200"}], "href": "https://doi.org/10.1074/jbc.M809244200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19297321"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19297321"}]}, {"type": "r", "ref": 4, "children": [{"type": "t", "text": "Hiroto Kambara, Hideki Tani, Yoshio Mori, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Involvement of cyclophilin B in the replication of Japanese encephalitis virus."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Virology (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.virol.2011.01.011"}], "href": "https://doi.org/10.1016/j.virol.2011.01.011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21281954"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21281954"}]}, {"type": "r", "ref": 5, "children": [{"type": "t", "text": "Kengo Morohashi, Hiroeki Sahara, Koichi Watashi, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cyclosporin A associated helicase-like protein facilitates the association of hepatitis C virus RNA polymerase with its cellular cyclophilin B."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "PLoS One (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1371/journal.pone.0018285"}], "href": "https://doi.org/10.1371/journal.pone.0018285"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21559518"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21559518"}]}, {"type": "r", "ref": 6, "children": [{"type": "t", "text": "Fleur S van Dijk, Isabel M Nesbitt, Eline H Zwikstra, et al. "}, {"type": "b", "children": [{"type": "t", "text": "PPIB mutations cause severe osteogenesis imperfecta."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Hum Genet (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.ajhg.2009.09.001"}], "href": "https://doi.org/10.1016/j.ajhg.2009.09.001"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19781681"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19781681"}]}, {"type": "r", "ref": 7, "children": [{"type": "t", "text": "Shawna M Pyott, Ulrike Schwarze, Helena E Christiansen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mutations in PPIB (cyclophilin B) delay type I procollagen chain association and result in perinatal lethal to moderate osteogenesis imperfecta phenotypes."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hum Mol Genet (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1093/hmg/ddr037"}], "href": "https://doi.org/10.1093/hmg/ddr037"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21282188"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21282188"}]}, {"type": "r", "ref": 8, "children": [{"type": "t", "text": "Yoshihiro Ishikawa, Hans Peter Bächinger "}, {"type": "b", "children": [{"type": "t", "text": "An additional function of the rough endoplasmic reticulum protein complex prolyl 3-hydroxylase 1·cartilage-associated protein·cyclophilin B: the CXXXC motif reveals disulfide isomerase activity in vitro."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2013)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M113.498063"}], "href": "https://doi.org/10.1074/jbc.M113.498063"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24043621"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24043621"}]}, {"type": "r", "ref": 9, "children": [{"type": "t", "text": "C Barbirato, M Trancozo, M G Almeida, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Mutational characterization of the P3H1/CRTAP/CypB complex in recessive osteogenesis imperfecta."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Genet Mol Res (2015)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4238/2015.December.1.36"}], "href": "https://doi.org/10.4238/2015.December.1.36"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26634552"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26634552"}]}, {"type": "r", "ref": 10, "children": [{"type": "t", "text": "Yu Jiang, Jingxin Pan, Dongwei Guo, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Two novel mutations in the PPIB gene cause a rare pedigree of osteogenesis imperfecta type IX."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Clin Chim Acta (2017)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cca.2017.02.019"}], "href": "https://doi.org/10.1016/j.cca.2017.02.019"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "28242392"}], "href": "https://pubmed.ncbi.nlm.nih.gov/28242392"}]}, {"type": "r", "ref": 11, "children": [{"type": "t", "text": "Jiawei Wu, Wenting Zhang, Li Xia, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Characterization of PPIB interaction in the P3H1 ternary complex and implications for its pathological mutations."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Mol Life Sci (2019)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s00018-019-03102-8"}], "href": "https://doi.org/10.1007/s00018-019-03102-8"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "30993352"}], "href": "https://pubmed.ncbi.nlm.nih.gov/30993352"}]}, {"type": "r", "ref": 12, "children": [{"type": "t", "text": "V Yurchenko, M O'Connor, W W Dai, et al. "}, {"type": "b", "children": [{"type": "t", "text": "CD147 is a signaling receptor for cyclophilin B."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2001)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1006/bbrc.2001.5847"}], "href": "https://doi.org/10.1006/bbrc.2001.5847"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11688976"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11688976"}]}, {"type": "r", "ref": 13, "children": [{"type": "t", "text": "Fabrice Allain, Christophe Vanpouille, Mathieu Carpentier, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Interaction with glycosaminoglycans is required for cyclophilin B to trigger integrin-mediated adhesion of peripheral blood T lymphocytes to extracellular matrix."}]}, {"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.052284899"}], "href": "https://doi.org/10.1073/pnas.052284899"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "11867726"}], "href": "https://pubmed.ncbi.nlm.nih.gov/11867726"}]}, {"type": "r", "ref": 14, "children": [{"type": "t", "text": "Christophe Vanpouille, Audrey Deligny, Maryse Delehedde, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The heparin/heparan sulfate sequence that interacts with cyclophilin B contains a 3-O-sulfated N-unsubstituted glucosamine residue."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2007)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M701835200"}], "href": "https://doi.org/10.1074/jbc.M701835200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "17588944"}], "href": "https://pubmed.ncbi.nlm.nih.gov/17588944"}]}, {"type": "r", "ref": 15, "children": [{"type": "t", "text": "Aurélie Melchior, Agnès Denys, Audrey Deligny, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cyclophilin B induces integrin-mediated cell adhesion by a mechanism involving CD98-dependent activation of protein kinase C-delta and p44/42 mitogen-activated protein kinases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Exp Cell Res (2008)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.yexcr.2007.11.007"}], "href": "https://doi.org/10.1016/j.yexcr.2007.11.007"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18054915"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18054915"}]}, {"type": "r", "ref": 16, "children": [{"type": "t", "text": "Tobias Stumpf, Qi Zhang, Daniela Hirnet, et al. "}, {"type": "b", "children": [{"type": "t", "text": "The human TRPV6 channel protein is associated with cyclophilin B in human placenta."}]}, {"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.M801821200"}], "href": "https://doi.org/10.1074/jbc.M801821200"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "18445599"}], "href": "https://pubmed.ncbi.nlm.nih.gov/18445599"}]}, {"type": "r", "ref": 17, "children": [{"type": "t", "text": "Feng Fang, Ayanna J Flegler, Pan Du, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Expression of cyclophilin B is associated with malignant progression and regulation of genes implicated in the pathogenesis of breast cancer."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Pathol (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.2353/ajpath.2009.080753"}], "href": "https://doi.org/10.2353/ajpath.2009.080753"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19056847"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19056847"}]}, {"type": "r", "ref": 18, "children": [{"type": "t", "text": "K Bauer, A K Kretzschmar, H Cvijic, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cyclophilins contribute to Stat3 signaling and survival of multiple myeloma cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncogene (2009)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1038/onc.2009.142"}], "href": "https://doi.org/10.1038/onc.2009.142"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19503092"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19503092"}]}, {"type": "r", "ref": 19, "children": [{"type": "t", "text": "Audrey Deligny, Agnès Denys, Adeline Marcant, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Synthesis of heparan sulfate with cyclophilin B-binding properties is determined by cell type-specific expression of sulfotransferases."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M109.018184"}], "href": "https://doi.org/10.1074/jbc.M109.018184"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "19940140"}], "href": "https://pubmed.ncbi.nlm.nih.gov/19940140"}]}, {"type": "r", "ref": 20, "children": [{"type": "t", "text": "Feng Fang, Jiamao Zheng, Traci L Galbaugh, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cyclophilin B as a co-regulator of prolactin-induced gene expression and function in breast cancer cells."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Mol Endocrinol (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1677/JME-09-0140"}], "href": "https://doi.org/10.1677/JME-09-0140"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20237142"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20237142"}]}, {"type": "r", "ref": 21, "children": [{"type": "t", "text": "Guennadi Kozlov, Sara Bastos-Aristizabal, Pekka Määttänen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Structural basis of cyclophilin B binding by the calnexin/calreticulin P-domain."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2010)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M110.160101"}], "href": "https://doi.org/10.1074/jbc.M110.160101"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "20801878"}], "href": "https://pubmed.ncbi.nlm.nih.gov/20801878"}]}, {"type": "r", "ref": 22, "children": [{"type": "t", "text": "Yeonghwan Kim, Miran Jang, Sangbin Lim, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Role of cyclophilin B in tumorigenesis and cisplatin resistance in hepatocellular carcinoma in humans."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Hepatology (2011)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1002/hep.24539"}], "href": "https://doi.org/10.1002/hep.24539"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "21748762"}], "href": "https://pubmed.ncbi.nlm.nih.gov/21748762"}]}, {"type": "r", "ref": 23, "children": [{"type": "t", "text": "Mary Y Lorenson, Eric K Ueda, KuanHui E Chen, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A major prolactin-binding complex on human milk fat globule membranes contains cyclophilins A and B: the complex is not the prolactin receptor."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Am J Physiol Endocrinol Metab (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1152/ajpendo.00480.2011"}], "href": "https://doi.org/10.1152/ajpendo.00480.2011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22205628"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22205628"}]}, {"type": "r", "ref": 24, "children": [{"type": "t", "text": "Birger Dieriks, Patrick Van Oostveldt "}, {"type": "b", "children": [{"type": "t", "text": "Spatiotemporal behavior of nuclear cyclophilin B indicates a role in RNA transcription."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Int J Mol Med (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.3892/ijmm.2012.937"}], "href": "https://doi.org/10.3892/ijmm.2012.937"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22426501"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22426501"}]}, {"type": "r", "ref": 25, "children": [{"type": "t", "text": "Partha Ray, Kristy L Rialon-Guevara, Emanuela Veras, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Comparing human pancreatic cell secretomes by in vitro aptamer selection identifies cyclophilin B as a candidate pancreatic cancer biomarker."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Clin Invest (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1172/JCI62385"}], "href": "https://doi.org/10.1172/JCI62385"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22484812"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22484812"}]}, {"type": "r", "ref": 26, "children": [{"type": "t", "text": "Kiyoon Kim, Hunsung Kim, Kwon Jeong, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Release of overexpressed CypB activates ERK signaling through CD147 binding for hepatoma cell resistance to oxidative stress."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Apoptosis (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1007/s10495-012-0730-5"}], "href": "https://doi.org/10.1007/s10495-012-0730-5"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22555451"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22555451"}]}, {"type": "r", "ref": 27, "children": [{"type": "t", "text": "Adeline Marcant, Agnès Denys, Aurélie Melchior, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cyclophilin B attenuates the expression of TNF-α in lipopolysaccharide-stimulated macrophages through the induction of B cell lymphoma-3."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Immunol (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.4049/jimmunol.1102803"}], "href": "https://doi.org/10.4049/jimmunol.1102803"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "22798670"}], "href": "https://pubmed.ncbi.nlm.nih.gov/22798670"}]}, {"type": "r", "ref": 28, "children": [{"type": "t", "text": "Klilah Hershko, Vijaya L Simhadri, Adam Blaisdell, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Cyclosporin A impairs the secretion and activity of ADAMTS13 (a disintegrin and metalloprotease with thrombospondin type 1 repeat)."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2012)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M112.383968"}], "href": "https://doi.org/10.1074/jbc.M112.383968"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "23144461"}], "href": "https://pubmed.ncbi.nlm.nih.gov/23144461"}]}, {"type": "r", "ref": 29, "children": [{"type": "t", "text": "Judith Nicholson, Alex Scherl, Luke Way, et al. "}, {"type": "b", "children": [{"type": "t", "text": "A systems wide mass spectrometric based linear motif screen to identify dominant in-vivo interacting proteins for the ubiquitin ligase MDM2."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Cell Signal (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.cellsig.2014.02.011"}], "href": "https://doi.org/10.1016/j.cellsig.2014.02.011"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24583282"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24583282"}]}, {"type": "r", "ref": 30, "children": [{"type": "t", "text": "Henrik Hoffmann, Cordelia Schiene-Fischer "}, {"type": "b", "children": [{"type": "t", "text": "Functional aspects of extracellular cyclophilins."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biol Chem (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1515/hsz-2014-0125"}], "href": "https://doi.org/10.1515/hsz-2014-0125"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24713575"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24713575"}]}, {"type": "r", "ref": 31, "children": [{"type": "t", "text": "Pawel Stocki, Daniel C Chapman, Lori A Beach, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Depletion of cyclophilins B and C leads to dysregulation of endoplasmic reticulum redox homeostasis."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "J Biol Chem (2014)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1074/jbc.M114.570911"}], "href": "https://doi.org/10.1074/jbc.M114.570911"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "24990953"}], "href": "https://pubmed.ncbi.nlm.nih.gov/24990953"}]}, {"type": "r", "ref": 32, "children": [{"type": "t", "text": "Jason DeBoer, Christian J Madson, Michael Belshan "}, {"type": "b", "children": [{"type": "t", "text": "Cyclophilin B enhances HIV-1 infection."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Virology (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.virol.2015.12.015"}], "href": "https://doi.org/10.1016/j.virol.2015.12.015"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "26774171"}], "href": "https://pubmed.ncbi.nlm.nih.gov/26774171"}]}, {"type": "r", "ref": 33, "children": [{"type": "t", "text": "Bin Wang, Lilu Lin, Haidong Wang, et al. "}, {"type": "b", "children": [{"type": "t", "text": "Overexpressed cyclophilin B suppresses aldosterone-induced proximal tubular cell injury both in vitro and in vivo."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Oncotarget (2016)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.18632/oncotarget.12503"}], "href": "https://doi.org/10.18632/oncotarget.12503"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "27732567"}], "href": "https://pubmed.ncbi.nlm.nih.gov/27732567"}]}]}]}