{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,8,30]],"date-time":"2026-08-30T01:42:51Z","timestamp":1788054171924,"version":"build-2784847793"},"reference-count":72,"publisher":"Impact Journals, LLC","issue":"37","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Oncotarget"],"published-print":{"date-parts":[[2016,9,13]]},"DOI":"10.18632\/oncotarget.11139","type":"journal-article","created":{"date-parts":[[2016,8,9]],"date-time":"2016-08-09T18:34:56Z","timestamp":1470767696000},"page":"60519-60534","source":"Crossref","is-referenced-by-count":29,"title":["USP9X destabilizes pVHL and promotes cell proliferation"],"prefix":"10.18632","volume":"7","author":[{"given":"Cong","family":"Zhang","sequence":"first","affiliation":[{"name":"Institute of Systems Biomedicine, State Key Laboratory of Natural and Biomimetic Drugs, Beijing Key Laboratory of Tumor Systems Biology, Department of Pathology, School of Basic Medical Sciences, Peking University Health Science Center, Peking-Tsinghua Center for Life Sciences, Beijing, 100191, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Zuohan","family":"Peng","sequence":"additional","affiliation":[{"name":"Institute of Systems Biomedicine, State Key Laboratory of Natural and Biomimetic Drugs, Beijing Key Laboratory of Tumor Systems Biology, Department of Pathology, School of Basic Medical Sciences, Peking University Health Science Center, Peking-Tsinghua Center for Life Sciences, Beijing, 100191, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Minglu","family":"Zhu","sequence":"additional","affiliation":[{"name":"Institute of Systems Biomedicine, State Key Laboratory of Natural and Biomimetic Drugs, Beijing Key Laboratory of Tumor Systems Biology, Department of Pathology, School of Basic Medical Sciences, Peking University Health Science Center, Peking-Tsinghua Center for Life Sciences, Beijing, 100191, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Penglong","family":"Wang","sequence":"additional","affiliation":[{"name":"Institute of Systems Biomedicine, State Key Laboratory of Natural and Biomimetic Drugs, Beijing Key Laboratory of Tumor Systems Biology, Department of Pathology, School of Basic Medical Sciences, Peking University Health Science Center, Peking-Tsinghua Center for Life Sciences, Beijing, 100191, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiao","family":"Du","sequence":"additional","affiliation":[{"name":"Institute of Systems Biomedicine, State Key Laboratory of Natural and Biomimetic Drugs, Beijing Key Laboratory of Tumor Systems Biology, Department of Pathology, School of Basic Medical Sciences, Peking University Health Science Center, Peking-Tsinghua Center for Life Sciences, Beijing, 100191, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiang","family":"Li","sequence":"additional","affiliation":[{"name":"Institute of Systems Biomedicine, State Key Laboratory of Natural and Biomimetic Drugs, Beijing Key Laboratory of Tumor Systems Biology, Department of Pathology, School of Basic Medical Sciences, Peking University Health Science Center, Peking-Tsinghua Center for Life Sciences, Beijing, 100191, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yu","family":"Liu","sequence":"additional","affiliation":[{"name":"Institute of Systems Biomedicine, State Key Laboratory of Natural and Biomimetic Drugs, Beijing Key Laboratory of Tumor Systems Biology, Department of Pathology, School of Basic Medical Sciences, Peking University Health Science Center, Peking-Tsinghua Center for Life Sciences, Beijing, 100191, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yan","family":"Jin","sequence":"additional","affiliation":[{"name":"Institute of Systems Biomedicine, State Key Laboratory of Natural and Biomimetic Drugs, Beijing Key Laboratory of Tumor Systems Biology, Department of Pathology, School of Basic Medical Sciences, Peking University Health Science Center, Peking-Tsinghua Center for Life Sciences, Beijing, 100191, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael A.","family":"McNutt","sequence":"additional","affiliation":[{"name":"Institute of Systems Biomedicine, State Key Laboratory of Natural and Biomimetic Drugs, Beijing Key Laboratory of Tumor Systems Biology, Department of Pathology, School of Basic Medical Sciences, Peking University Health Science Center, Peking-Tsinghua Center for Life Sciences, Beijing, 100191, China"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yuxin","family":"Yin","sequence":"additional","affiliation":[{"name":"Institute of Systems Biomedicine, State Key Laboratory of Natural and Biomimetic Drugs, Beijing Key Laboratory of Tumor Systems Biology, Department of Pathology, School of Basic Medical Sciences, Peking University Health Science Center, Peking-Tsinghua Center for Life Sciences, Beijing, 100191, China"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"7892","published-online":{"date-parts":[[2016,8,9]]},"reference":[{"key":"1","doi-asserted-by":"crossref","first-page":"1317","DOI":"10.1126\/science.8493574","article-title":"Identification of the von Hippel-Lindau disease tumor suppressor gene","volume":"260","author":"Geil","year":"1993","journal-title":"Science"},{"key":"2","doi-asserted-by":"crossref","first-page":"12436","DOI":"10.1073\/pnas.96.22.12436","article-title":"Identification of the von Hippel-lindau tumor-suppressor protein as part of an active E3 ubiquitin ligase complex","volume":"96","author":"Pause","year":"1999","journal-title":"Proceedings of the National Academy of Sciences of the United States of America"},{"key":"3","first-page":"231","article-title":"Expression pattern of the von Hippel-Lindau protein in human tissues","volume":"75","author":"Voest","year":"1996","journal-title":"Laboratory investigation"},{"key":"4","doi-asserted-by":"crossref","first-page":"2156","DOI":"10.1073\/pnas.94.6.2156","article-title":"The von Hippel-Lindau tumor-suppressor gene product forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins","volume":"94","author":"Klausner","year":"1997","journal-title":"Proc Natl Acad Sci U S A"},{"key":"5","doi-asserted-by":"crossref","first-page":"1822","DOI":"10.1101\/gad.13.14.1822","article-title":"The von Hippel-Lindau tumor suppressor protein is a component of an E3 ubiquitin-protein ligase activity","volume":"13","author":"Krek","year":"1999","journal-title":"Genes & development"},{"key":"6","doi-asserted-by":"crossref","first-page":"1444","DOI":"10.1126\/science.7660130","article-title":"Binding of the von Hippel-Lindau tumor suppressor protein to Elongin B, and C","volume":"269","author":"Kaelin","year":"1995","journal-title":"Science"},{"key":"7","doi-asserted-by":"crossref","first-page":"657","DOI":"10.1126\/science.284.5414.657","article-title":"Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase","volume":"284","author":"Conaway","year":"1999","journal-title":"Science"},{"key":"8","doi-asserted-by":"crossref","first-page":"455","DOI":"10.1126\/science.284.5413.455","article-title":"Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function","volume":"284","author":"Pavletich","year":"1999","journal-title":"Science"},{"key":"9","doi-asserted-by":"crossref","first-page":"468","DOI":"10.1126\/science.1059796","article-title":"Targeting of HIF-alpha to the von Hippel-Lindau ubiquitylation complex by O2-regulated prolyl hydroxylation","volume":"292","author":"Ratcliffe","year":"2001","journal-title":"Science"},{"key":"10","doi-asserted-by":"crossref","first-page":"858","DOI":"10.1126\/science.1068592","article-title":"Asparagine hydroxylation of the HIF transactivation domain a hypoxic switch","volume":"295","author":"Whitelaw","year":"2002","journal-title":"Science"},{"key":"11","doi-asserted-by":"crossref","first-page":"271","DOI":"10.1038\/20459","article-title":"The tumour suppressor protein VHL targets hypoxia-inducible factors for oxygen-dependent proteolysis","volume":"399","author":"Ratcliffe","year":"1999","journal-title":"Nature"},{"key":"12","doi-asserted-by":"crossref","first-page":"1886","DOI":"10.1126\/science.1073440","article-title":"Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling","volume":"296","author":"Pavletich","year":"2002","journal-title":"Science"},{"key":"13","doi-asserted-by":"crossref","first-page":"6264","DOI":"10.1158\/0008-5472.CAN-05-2519","article-title":"Role of hypoxia-inducible factor (HIF)-1alpha versus HIF-2alpha in the regulation of HIF target genes in response to hypoxia, insulin-like growth factor-I, or loss of von Hippel-Lindau function: implications for targeting the HIF pathway","volume":"66","author":"Ashcroft","year":"2006","journal-title":"Cancer research"},{"key":"14","doi-asserted-by":"crossref","first-page":"10595","DOI":"10.1073\/pnas.93.20.10595","article-title":"Negative regulation of hypoxia-inducible genes by the von Hippel-Lindau protein","volume":"93","author":"Goldberg","year":"1996","journal-title":"Proceedings of the National Academy of Sciences of the United States of America"},{"key":"15","first-page":"1358","article-title":"Up-regulation of vascular endothelial growth factor and its receptors in von Hippel-Lindau disease-associated and sporadic hemangioblastomas","volume":"55","author":"Plate","year":"1995","journal-title":"Cancer Res"},{"key":"16","doi-asserted-by":"crossref","first-page":"9630","DOI":"10.1073\/pnas.181341498","article-title":"HIF-1alpha binding to VHL is regulated by stimulus-sensitive proline hydroxylation","volume":"98","author":"Lee","year":"2001","journal-title":"Proc Natl Acad Sci U S A"},{"key":"17","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1038\/nrc3844","article-title":"VHL, the story of a tumour suppressor gene","volume":"15","author":"Maher","year":"2015","journal-title":"Nature reviews Cancer"},{"key":"18","doi-asserted-by":"crossref","first-page":"42027","DOI":"10.1074\/jbc.M111.303222","article-title":"Regulation of cellular levels of Sprouty2 protein by prolyl hydroxylase domain and von Hippel-Lindau proteins","volume":"286","author":"Patel","year":"2011","journal-title":"J Biol Chem"},{"key":"19","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1016\/j.cell.2007.01.047","article-title":"HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells","volume":"129","author":"Semenza","year":"2007","journal-title":"Cell"},{"key":"20","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/j.molcel.2011.11.031","article-title":"Regulation of KLF4 turnover reveals an unexpected tissue-specific role of pVHL in tumorigenesis","volume":"45","author":"Wan","year":"2012","journal-title":"Mol Cell"},{"key":"21","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1016\/j.ccr.2012.02.019","article-title":"VHL-regulated MiR-204 suppresses tumor growth through inhibition of LC3B-mediated autophagy in renal clear cell carcinoma","volume":"21","author":"Czyzyk-Krzeska","year":"2012","journal-title":"Cancer cell"},{"key":"22","doi-asserted-by":"crossref","first-page":"3127","DOI":"10.1038\/onc.2011.40","article-title":"von Hippel-Lindau protein promotes Skp2 destabilization on DNA damage","volume":"30","author":"Youn","year":"2011","journal-title":"Oncogene"},{"key":"23","doi-asserted-by":"crossref","first-page":"994","DOI":"10.1038\/ncb1912","article-title":"VHL loss causes spindle misorientation and chromosome instability","volume":"11","author":"Krek","year":"2009","journal-title":"Nature cell biology"},{"key":"24","first-page":"pe30","article-title":"pVHL: a multipurpose adaptor protein","volume":"1","author":"Krek","year":"2008","journal-title":"Science signaling"},{"key":"25","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1038\/ncb899","article-title":"Regulation of microtubule stability by the von Hippel-Lindau tumour suppressor protein pVHL","volume":"5","author":"Krek","year":"2003","journal-title":"Nature cell biology"},{"key":"26","doi-asserted-by":"crossref","first-page":"959","DOI":"10.1016\/S1097-2765(00)80096-9","article-title":"The von Hippel-Lindau tumor suppressor protein is required for proper assembly of an extracellular fibronectin matrix","volume":"1","author":"Iliopoulos","year":"1998","journal-title":"Mol Cell"},{"key":"27","doi-asserted-by":"crossref","first-page":"1563","DOI":"10.1038\/sj.onc.1208348","article-title":"VHL expression in renal cell carcinoma sensitizes to bortezomib (PS-341) through an NF-kappaB-dependent mechanism","volume":"24","author":"Rettig","year":"2005","journal-title":"Oncogene"},{"key":"28","doi-asserted-by":"crossref","first-page":"752","DOI":"10.1158\/0008-5472.CAN-09-2211","article-title":"NF-kappaB-dependent plasticity of the epithelial to mesenchymal transition induced by Von Hippel-Lindau inactivation in renal cell carcinomas","volume":"70","author":"Rettig","year":"2010","journal-title":"Cancer research"},{"key":"29","first-page":"7076","article-title":"The von Hippel-Lindau tumor suppressor protein sensitizes renal cell carcinoma cells to tumor necrosis factor-induced cytotoxicity by suppressing the nuclear factor-kappaB-dependent antiapoptotic pathway","volume":"63","author":"Ohh","year":"2003","journal-title":"Cancer Res"},{"key":"30","doi-asserted-by":"crossref","first-page":"15","DOI":"10.1016\/j.molcel.2007.09.010","article-title":"pVHL acts as an adaptor to promote the inhibitory phosphorylation of the NF-kappaB agonist Card9 by CK2","volume":"28","author":"Kaelin","year":"2007","journal-title":"Molecular cell"},{"key":"31","doi-asserted-by":"crossref","first-page":"3127","DOI":"10.1158\/0008-5472.CAN-13-3213","article-title":"Genetic and pharmacological strategies to refunctionalize the von Hippel Lindau R167Q mutant protein","volume":"74","author":"Jonasch","year":"2014","journal-title":"Cancer research"},{"key":"32","doi-asserted-by":"crossref","first-page":"5500","DOI":"10.1158\/0008-5472.CAN-11-0757","article-title":"VHL gene mutations and their effects on hypoxia inducible factor HIFalpha: identification of potential driver and passenger mutations","volume":"71","author":"Moch","year":"2011","journal-title":"Cancer research"},{"key":"33","doi-asserted-by":"crossref","first-page":"52","DOI":"10.1016\/j.celrep.2012.12.007","article-title":"Proteostasis modulators prolong missense VHL protein activity and halt tumor progression","volume":"3","author":"Lonser","year":"2013","journal-title":"Cell Rep"},{"key":"34","doi-asserted-by":"crossref","first-page":"208","DOI":"10.1111\/boc.201200080","article-title":"TCTP increases stability of hypoxia-inducible factor 1alpha by interaction with and degradation of the tumour suppressor VHL","volume":"105","author":"Zhou","year":"2013","journal-title":"Biology of the cell\/under the auspices of the European Cell Biology Organization"},{"key":"35","doi-asserted-by":"crossref","first-page":"809","DOI":"10.1038\/nm1440","article-title":"E2-EPF UCP targets pVHL for degradation and associates with tumor growth and metastasis","volume":"12","author":"Im","year":"2006","journal-title":"Nature medicine"},{"key":"36","doi-asserted-by":"crossref","first-page":"18168","DOI":"10.1073\/pnas.1311382110","article-title":"BC-box protein domain-related mechanism for VHL protein degradation","volume":"110","author":"Chiocca","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"37","doi-asserted-by":"crossref","first-page":"8507","DOI":"10.1073\/pnas.97.15.8507","article-title":"Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products","volume":"97","author":"Burk","year":"2000","journal-title":"Proc Natl Acad Sci U S A"},{"key":"38","doi-asserted-by":"crossref","first-page":"18666","DOI":"10.1073\/pnas.1105725108","article-title":"alpha-Synuclein fate is determined by USP9X-regulated monoubiquitination","volume":"108","author":"Engelender","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"39","doi-asserted-by":"crossref","first-page":"470","DOI":"10.1016\/j.ajhg.2014.02.004","article-title":"Mutations in USP9X are associated with X-linked intellectual disability and disrupt neuronal cell migration and growth","volume":"94","author":"Jolly","year":"2014","journal-title":"American journal of human genetics"},{"key":"40","doi-asserted-by":"crossref","first-page":"2873","DOI":"10.1038\/ncomms3873","article-title":"Mutational landscape of gingivo-buccal oral squamous cell carcinoma reveals new recurrently-mutated genes and molecular subgroups","volume":"4","author":"India Project Team of the International Cancer Genome","year":"2013","journal-title":"Nature communications"},{"key":"41","doi-asserted-by":"crossref","first-page":"2075","DOI":"10.1007\/s00018-015-1851-0","article-title":"La FAM fatale: USP9X in development and disease","volume":"72","author":"Wood","year":"2015","journal-title":"Cellular and molecular life sciences: CMLS"},{"key":"42","doi-asserted-by":"crossref","first-page":"123","DOI":"10.1016\/j.cell.2008.10.051","article-title":"FAM\/USP9x, a deubiquitinating enzyme essential for TGFbeta signaling, controls Smad4 monoubiquitination","volume":"136","author":"Piccolo","year":"2009","journal-title":"Cell"},{"key":"43","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1016\/j.molcel.2009.10.016","article-title":"Ubiquitin-like sequence in ASK1 plays critical roles in the recognition and stabilization by USP9X and oxidative stress-induced cell death","volume":"36","author":"Ichijo","year":"2009","journal-title":"Mol Cell"},{"key":"44","doi-asserted-by":"crossref","first-page":"103","DOI":"10.1038\/nature08646","article-title":"Deubiquitinase USP9X stabilizes MCL1 and promotes tumour cell survival","volume":"463","author":"Dixit","year":"2010","journal-title":"Nature"},{"key":"45","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1038\/emboj.2010.46","article-title":"USP9x-mediated deubiquitination of EFA6 regulates de novo tight junction assembly","volume":"29","author":"Luton","year":"2010","journal-title":"EMBO J"},{"key":"46","doi-asserted-by":"crossref","first-page":"1499","DOI":"10.1126\/science.1120160","article-title":"Chromosome alignment and segregation regulated by ubiquitination of survivin","volume":"310","author":"Zheng","year":"2005","journal-title":"Science"},{"key":"47","doi-asserted-by":"crossref","first-page":"2976","DOI":"10.1074\/jbc.M112.430066","article-title":"Deubiquitinase FAM\/USP9X interacts with the E3 ubiquitin ligase SMURF1 protein and protects it from ligase activity-dependent self-degradation","volume":"288","author":"Cong","year":"2013","journal-title":"The Journal of biological chemistry"},{"key":"48","doi-asserted-by":"crossref","first-page":"2305","DOI":"10.1007\/s00018-012-1170-7","article-title":"A Smurf1 tale: function and regulation of an ubiquitin ligase in multiple cellular networks","volume":"70","author":"Zhang","year":"2013","journal-title":"Cellular and molecular life sciences: CMLS"},{"key":"49","doi-asserted-by":"crossref","first-page":"1319","DOI":"10.4161\/cbt.21792","article-title":"Genetic disruption of USP9X sensitizes colorectal cancer cells to 5-fluorouracil","volume":"13","author":"Bunz","year":"2012","journal-title":"Cancer Biol Ther"},{"key":"50","doi-asserted-by":"crossref","first-page":"393","DOI":"10.1186\/1471-2407-14-393","article-title":"MicroRNA-26b inhibits epithelial-mesenchymal transition in hepatocellular carcinoma by targeting USP9X","volume":"14","author":"Jia","year":"2014","journal-title":"BMC Cancer"},{"key":"51","doi-asserted-by":"crossref","first-page":"4251","DOI":"10.1073\/pnas.1322198111","article-title":"Ablation of the oncogenic transcription factor ERG by deubiquitinase inhibition in prostate cancer","volume":"111","author":"Kittler","year":"2014","journal-title":"Proc Natl Acad Sci U S A"},{"key":"52","doi-asserted-by":"crossref","first-page":"416","DOI":"10.1016\/j.ccr.2011.02.014","article-title":"SIRT3 opposes reprogramming of cancer cell metabolism through HIF1alpha destabilization","volume":"19","author":"Haigis","year":"2011","journal-title":"Cancer cell"},{"key":"53","doi-asserted-by":"crossref","first-page":"231","DOI":"10.1007\/s10863-007-9081-2","article-title":"HIF-1 mediates the Warburg effect in clear cell renal carcinoma","volume":"39","author":"Semenza","year":"2007","journal-title":"Journal of bioenergetics and biomembranes"},{"key":"54","doi-asserted-by":"crossref","first-page":"5675","DOI":"10.1128\/MCB.25.13.5675-5686.2005","article-title":"Contrasting properties of hypoxia-inducible factor 1 (HIF-1) and HIF-2 in von Hippel-Lindau-associated renal cell carcinoma","volume":"25","author":"Ratcliffe","year":"2005","journal-title":"Molecular and cellular biology"},{"key":"55","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1096\/fj.05-4104fje","article-title":"Impact of HIF-1alpha and HIF-2alpha on proliferation and migration of human pulmonary artery fibroblasts in hypoxia","volume":"20","author":"Hanze","year":"2006","journal-title":"FASEB journal"},{"key":"56","doi-asserted-by":"crossref","first-page":"e4531","DOI":"10.1371\/journal.pone.0004531","article-title":"Differences in the tumor microenvironment between African-American and European-American breast cancer patients","volume":"4","author":"Ambs","year":"2009","journal-title":"PloS one"},{"key":"57","doi-asserted-by":"crossref","first-page":"4040","DOI":"10.1158\/0008-5472.CAN-03-3620","article-title":"Gene expression in the urinary bladder: a common carcinoma in situ gene expression signature exists disregarding histopathological classification","volume":"64","author":"Orntoft","year":"2004","journal-title":"Cancer research"},{"key":"58","doi-asserted-by":"crossref","first-page":"2590","DOI":"10.1158\/1055-9965.EPI-10-0332","article-title":"Identification of a novel biomarker, SEMA5A, for non-small cell lung carcinoma in nonsmoking women","volume":"19","author":"Chuang","year":"2010","journal-title":"Cancer epidemiology, biomarkers & prevention"},{"key":"59","doi-asserted-by":"crossref","first-page":"1324","DOI":"10.1002\/ijc.23237","article-title":"A stromal gene signature associated with inflammatory breast cancer","volume":"122","author":"Ambs","year":"2008","journal-title":"International journal of cancer"},{"key":"60","doi-asserted-by":"crossref","first-page":"2790","DOI":"10.1200\/JCO.2004.05.158","article-title":"Gene expression alterations in prostate cancer predicting tumor aggression and preceding development of malignancy","volume":"22","author":"Luo","year":"2004","journal-title":"Journal of clinical oncology"},{"key":"61","doi-asserted-by":"crossref","first-page":"760","DOI":"10.1158\/1541-7786.MCR-07-0344","article-title":"Gene expression changes in an animal melanoma model correlate with aggressiveness of human melanoma metastases","volume":"6","author":"Hynes","year":"2008","journal-title":"Molecular cancer research: MCR"},{"key":"62","doi-asserted-by":"crossref","first-page":"64","DOI":"10.1186\/1471-2407-7-64","article-title":"Gene expression profiles of prostate cancer reveal involvement of multiple molecular pathways in the metastatic process","volume":"7","author":"Monzon","year":"2007","journal-title":"BMC cancer"},{"key":"63","doi-asserted-by":"crossref","first-page":"1450","DOI":"10.1016\/j.bmc.2013.12.048","article-title":"Degrasyn-like symmetrical compounds: possible therapeutic agents for multiple myeloma (MM-I)","volume":"22","author":"Talpaz","year":"2014","journal-title":"Bioorganic & medicinal chemistry"},{"key":"64","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1158\/2159-8290.CD-12-0095","article-title":"The cBio cancer genomics portal: an open platform for exploring multidimensional cancer genomics data","volume":"2","author":"Schultz","year":"2012","journal-title":"Cancer discovery"},{"key":"65","doi-asserted-by":"crossref","first-page":"541","DOI":"10.1186\/1471-2407-12-541","article-title":"The downregulation of Mcl-1 via USP9X inhibition sensitizes solid tumors to Bcl-xl inhibition","volume":"12","author":"Cao","year":"2012","journal-title":"BMC Cancer"},{"key":"66","doi-asserted-by":"crossref","first-page":"177","DOI":"10.1186\/1746-1596-8-177","article-title":"USP9X expression correlates with tumor progression and poor prognosis in esophageal squamous cell carcinoma","volume":"8","author":"Wang","year":"2013","journal-title":"Diagnostic pathology"},{"key":"67","first-page":"672","article-title":"Elevated expression of USP9X correlates with poor prognosis in human non-small cell lung cancer","volume":"7","author":"Xie","year":"2015","journal-title":"Journal of thoracic disease"},{"key":"68","doi-asserted-by":"crossref","first-page":"266","DOI":"10.1038\/nature11114","article-title":"The deubiquitinase USP9X suppresses pancreatic ductal adenocarcinoma","volume":"486","author":"Stemple","year":"2012","journal-title":"Nature"},{"key":"69","first-page":"5830","article-title":"Overexpression of hypoxia-inducible factor 1alpha in common human cancers and their metastases","volume":"59","author":"Simons","year":"1999","journal-title":"Cancer Res"},{"key":"70","doi-asserted-by":"crossref","first-page":"836","DOI":"10.1016\/j.cmet.2014.03.023","article-title":"PTENalpha, a PTEN isoform translated through alternative initiation, regulates mitochondrial function and energy metabolism","volume":"19","author":"Yin","year":"2014","journal-title":"Cell metabolism"},{"key":"71","doi-asserted-by":"crossref","first-page":"1972","DOI":"10.1126\/science.1091362","article-title":"Mono- versus polyubiquitination: differential control of p53 fate by Mdm2","volume":"302","author":"Gu","year":"2003","journal-title":"Science"},{"key":"72","doi-asserted-by":"crossref","first-page":"e114019","DOI":"10.1371\/journal.pone.0114019","article-title":"Metabolomics analysis of metabolic effects of nicotinamide phosphoribosyltransferase (NAMPT) inhibition on human cancer cells","volume":"9","author":"Kuo","year":"2014","journal-title":"PLoS One"}],"container-title":["Oncotarget"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.oncotarget.com\/lookup\/doi\/10.18632\/oncotarget.11139","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2020,8,6]],"date-time":"2020-08-06T12:35:49Z","timestamp":1596717349000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.oncotarget.com\/lookup\/doi\/10.18632\/oncotarget.11139"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2016,8,9]]},"references-count":72,"journal-issue":{"issue":"37","published-print":{"date-parts":[[2016,9,13]]}},"alternative-id":["11139","27517496"],"URL":"https:\/\/doi.org\/10.18632\/oncotarget.11139","relation":{},"ISSN":["1949-2553"],"issn-type":[{"value":"1949-2553","type":"electronic"}],"subject":[],"published":{"date-parts":[[2016,8,9]]}}}