USP7
出典: フリー百科事典『ウィキペディア(Wikipedia)』 (2021/04/30 15:43 UTC 版)
関連文献
- “Deubiquitinating enzymes: a new class of biological regulators”. Critical Reviews in Biochemistry and Molecular Biology 33 (5): 337–52. (1999). doi:10.1080/10409239891204251. PMID 9827704.
- “HAUSP/USP7 as an Epstein-Barr virus target”. Biochemical Society Transactions 32 (Pt 5): 731–2. (Nov 2004). doi:10.1042/BST0320731. PMID 15494000.
- “A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein”. The EMBO Journal 16 (3): 566–77. (Feb 1997). doi:10.1093/emboj/16.3.566. PMC: 1169660. PMID 9034339 .
- “A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein”. The EMBO Journal 16 (7): 1519–30. (Apr 1997). doi:10.1093/emboj/16.7.1519. PMC: 1169756. PMID 9130697 .
- “A diverse family of proteins containing tumor necrosis factor receptor-associated factor domains”. The Journal of Biological Chemistry 276 (26): 24242–52. (Jun 2001). doi:10.1074/jbc.M100354200. PMID 11279055.
- “Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization”. Nature 416 (6881): 648–53. (Apr 2002). doi:10.1038/nature737. PMID 11923872.
- “USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product”. Molecular and Cellular Neurosciences 20 (2): 298–306. (Jun 2002). doi:10.1006/mcne.2002.1103. PMID 12093161.
- “Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde”. Cell 111 (7): 1041–54. (Dec 2002). doi:10.1016/S0092-8674(02)01199-6. PMID 12507430.
- “Protein interaction domains of the ubiquitin-specific protease, USP7/HAUSP”. The Journal of Biological Chemistry 278 (48): 47753–61. (Nov 2003). doi:10.1074/jbc.M307200200. PMID 14506283.
- “Comprehensive proteomic analysis of human Par protein complexes reveals an interconnected protein network”. The Journal of Biological Chemistry 279 (13): 12804–11. (Mar 2004). doi:10.1074/jbc.M312171200. PMID 14676191.
- “A dynamic role of HAUSP in the p53-Mdm2 pathway”. Molecular Cell 13 (6): 879–86. (Mar 2004). doi:10.1016/S1097-2765(04)00157-1. PMID 15053880.
- “Tumour suppression: disruption of HAUSP gene stabilizes p53”. Nature 428 (6982): 1 p following 486. (Apr 2004). doi:10.1038/nature02501. PMID 15058298.
- “A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7”. The Journal of Biological Chemistry 279 (37): 38160–8. (Sep 2004). doi:10.1074/jbc.M402885200. PMID 15247261.
- “Large-scale characterization of HeLa cell nuclear phosphoproteins”. Proceedings of the National Academy of Sciences of the United States of America 101 (33): 12130–5. (Aug 2004). doi:10.1073/pnas.0404720101. PMC: 514446. PMID 15302935 .
- “Structure of the p53 binding domain of HAUSP/USP7 bound to Epstein-Barr nuclear antigen 1 implications for EBV-mediated immortalization”. Molecular Cell 18 (1): 25–36. (Apr 2005). doi:10.1016/j.molcel.2005.02.029. PMID 15808506.
- ^ a b c GRCh38: Ensembl release 89: ENSG00000187555 - Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000022710 - Ensembl, May 2017
- ^ Human PubMed Reference:
- ^ Mouse PubMed Reference:
- ^ “Human and mouse proteases: a comparative genomic approach”. Nature Reviews. Genetics 4 (7): 544–58. (Jul 2003). doi:10.1038/nrg1111. PMID 12838346.
- ^ “Assignment1 of herpesvirus-associated ubiquitin-specific protease gene HAUSP to human chromosome band 16p13.3 by in situ hybridization”. Cytogenetics and Cell Genetics 83 (1–2): 100. (Mar 1999). doi:10.1159/000015142. PMID 9925944.
- ^ “Entrez Gene: USP7 ubiquitin specific peptidase 7 (herpes virus-associated)”. 2021年2月14日閲覧。
- ^ “A novel ubiquitin-specific protease is dynamically associated with the PML nuclear domain and binds to a herpesvirus regulatory protein”. The EMBO Journal 16 (7): 1519–30. (Apr 1997). doi:10.1093/emboj/16.7.1519. PMC: 1169756. PMID 9130697 .
- ^ “Protein interaction domains of the ubiquitin-specific protease, USP7/HAUSP”. The Journal of Biological Chemistry 278 (48): 47753–61. (Nov 2003). doi:10.1074/jbc.M307200200. PMID 14506283.
- ^ Sherr, C. J.; Weber, J. D. (2000-02). “The ARF/p53 pathway”. Current Opinion in Genetics & Development 10 (1): 94–99. doi:10.1016/s0959-437x(99)00038-6. ISSN 0959-437X. PMID 10679383 .
- ^ Seavey, S. E.; Holubar, M.; Saucedo, L. J.; Perry, M. E. (1999-09). “The E7 oncoprotein of human papillomavirus type 16 stabilizes p53 through a mechanism independent of p19(ARF)”. Journal of Virology 73 (9): 7590–7598. doi:10.1128/JVI.73.9.7590-7598.1999. ISSN 0022-538X. PMC: PMC104286. PMID 10438849 .
- ^ Tolbert, Dawn; Lu, Xiangdong; Yin, Chaoying; Tantama, Mathew; Van Dyke, Terry (2002-01). “p19(ARF) is dispensable for oncogenic stress-induced p53-mediated apoptosis and tumor suppression in vivo”. Molecular and Cellular Biology 22 (1): 370–377. doi:10.1128/mcb.22.1.370-377.2002. ISSN 0270-7306. PMC: PMC134227. PMID 11739748 .
- ^ a b “Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization”. Nature 416 (6881): 648–53. (Apr 2002). doi:10.1038/nature737. PMID 11923872.
- ^ a b “GMP synthetase stimulates histone H2B deubiquitylation by the epigenetic silencer USP7”. Molecular Cell 17 (5): 695–707. (Mar 2005). doi:10.1016/j.molcel.2005.02.013. PMID 15749019.
- ^ “Biosynthetic enzyme GMP synthetase cooperates with ubiquitin-specific protease 7 in transcriptional regulation of ecdysteroid target genes”. Molecular and Cellular Biology 30 (3): 736–44. (Feb 2010). doi:10.1128/MCB.01121-09. PMC: 2812229. PMID 19995917 .
- ^ Meredith, M.; Orr, A.; Everett, R. (1994-05-01). “Herpes simplex virus type 1 immediate-early protein Vmw110 binds strongly and specifically to a 135-kDa cellular protein”. Virology 200 (2): 457–469. doi:10.1006/viro.1994.1209. ISSN 0042-6822. PMID 8178435 .
- ^ “HAUSP/USP7 as an Epstein-Barr virus target”. Biochemical Society Transactions 32 (Pt 5): 731–2. (Nov 2004). doi:10.1042/BST0320731. PMID 15494000.
- ^ Speck, Samuel H., ed (Oct 2009). “EBNA1-mediated recruitment of a histone H2B deubiquitylating complex to the Epstein-Barr virus latent origin of DNA replication”. PLOS Pathogens 5 (10): e1000624. doi:10.1371/journal.ppat.1000624. PMC: 2757719. PMID 19834552 .
- ^ “USP7 Acts as a Molecular Rheostat to Promote WASH-Dependent Endosomal Protein Recycling and Is Mutated in a Human Neurodevelopmental Disorder”. Mol. Cell 59 (6): 956–69. (September 2015). doi:10.1016/j.molcel.2015.07.033. PMC: 4575888. PMID 26365382 .
- ^ “USP7 Related Diseases”. National Organization for Rare Disorders (NORD). 2021年2月13日閲覧。
- ^ a b “Inhibition of USP7 activity selectively eliminates senescent cells in part via restoration of p53 activity”. Aging Cell 19 (3): e13117. (2020). doi:10.1111/acel.13117. PMC: 7059172. PMID 32064756 .
- ^ “USP7, a ubiquitin-specific protease, interacts with ataxin-1, the SCA1 gene product”. Molecular and Cellular Neurosciences 20 (2): 298–306. (Jun 2002). doi:10.1006/mcne.2002.1103. PMID 12093161.
- ^ “USP7 counteracts SCFbetaTrCP- but not APCCdh1-mediated proteolysis of Claspin”. The Journal of Cell Biology 184 (1): 13–9. (Jan 2009). doi:10.1083/jcb.200807137. PMC: 2615094. PMID 19124652 .
- ^ “Defining the human deubiquitinating enzyme interaction landscape”. Cell 138 (2): 389–403. (Jul 2009). doi:10.1016/j.cell.2009.04.042. PMC: 2716422. PMID 19615732 .
- ^ “UV-sensitive syndrome protein UVSSA recruits USP7 to regulate transcription-coupled repair”. Nature Genetics 44 (5): 598–602. (May 2012). doi:10.1038/ng.2230. PMID 22466611.
「USP7」の続きの解説一覧
- USP7のページへのリンク