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Volumn 12, Issue 4, 2011, Pages 350-357

Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21

Author keywords

cross reactivity; linkage specificity; NEDD8; SG15; ubiquitin specific protease

Indexed keywords

ALDEHYDE; INTERFERON STIMULATED GENE FACTOR 15; NEDD8 PROTEIN; POLYUBIQUITIN; TRANSCRIPTION FACTOR; UBIQUITIN; UBIQUITIN SPECIFIC PROTEASE 21; UNCLASSIFIED DRUG;

EID: 79953314427     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/embor.2011.17     Document Type: Article
Times cited : (133)

References (23)
  • 1
    • 79952301200 scopus 로고    scopus 로고
    • Molecular basis for ubiquitin and ISG15 cross-reactivity in viral OTU domains
    • Akutsu M, Ye Y, Virdee S, Chin J, Komander D (2011) Molecular basis for ubiquitin and ISG15 cross-reactivity in viral OTU domains. Proc Natl Acad Sci USA 108: 2228-2233
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 2228-2233
    • Akutsu, M.1    Ye, Y.2    Virdee, S.3    Chin, J.4    Komander, D.5
  • 3
    • 21344473677 scopus 로고    scopus 로고
    • ISG15: A ubiquitin-like enigma
    • Dao CT, Zhang DE (2005) ISG15: a ubiquitin-like enigma. Front Biosci 10: 2701-2722 (Pubitemid 40905270)
    • (2005) Frontiers in Bioscience , vol.10 , Issue.SUPPL. 2 , pp. 2701-2722
    • Dao, C.T.1    Zhang, D.-E.2
  • 4
    • 77953114765 scopus 로고    scopus 로고
    • The ISG15 conjugation system broadly targets newly synthesized proteins: Implications for the antiviral function of ISG15
    • Durfee LA, Lyon N, Seo K, Huibregtse JM (2010) The ISG15 conjugation system broadly targets newly synthesized proteins: implications for the antiviral function of ISG15. Mol Cell 38: 722-732
    • (2010) Mol Cell , vol.38 , pp. 722-732
    • Durfee, L.A.1    Lyon, N.2    Seo, K.3    Huibregtse, J.M.4
  • 5
    • 34347265174 scopus 로고    scopus 로고
    • Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins
    • DOI 10.1146/annurev.biophys.36.040306.132820
    • Dye BT, Schulman BA (2007) Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins. Annu Rev Biophys Biomol Struct 36: 131-150 (Pubitemid 46998113)
    • (2007) Annual Review of Biophysics and Biomolecular Structure , vol.36 , pp. 131-150
    • Dye, B.T.1    Schulman, B.A.2
  • 6
    • 77951639210 scopus 로고    scopus 로고
    • Structural insights into the COP9 signalosome and its common architecture with the 26S proteasome lid and eIF3
    • Enchev RI, Schreiber A, Beuron F, Morris EP (2010) Structural insights into the COP9 signalosome and its common architecture with the 26S proteasome lid and eIF3. Structure 18: 518-527
    • (2010) Structure , vol.18 , pp. 518-527
    • Enchev, R.I.1    Schreiber, A.2    Beuron, F.3    Morris, E.P.4
  • 7
    • 0034640373 scopus 로고    scopus 로고
    • Identification of a novel isopeptidase with dual specificity for ubiquitin- and NEDD8-conjugated proteins
    • DOI 10.1074/jbc.275.19.14212
    • Gong L, Kamitani T, Millas S, Yeh ET (2000) Identification of a novel isopeptidase with dual specificity for ubiquitin- and NEDD8-conjugated proteins. J Biol Chem 275: 14212-14216 (Pubitemid 30339699)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.19 , pp. 14212-14216
    • Gong, L.1    Kamitani, T.2    Millas, S.3    Yeh, E.T.H.4
  • 8
    • 63649113699 scopus 로고    scopus 로고
    • Origin and function of ubiquitin-like proteins
    • Hochstrasser M (2009) Origin and function of ubiquitin-like proteins. Nature 458: 422-429
    • (2009) Nature , vol.458 , pp. 422-429
    • Hochstrasser, M.1
  • 9
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • Komander D (2009) The emerging complexity of protein ubiquitination. Biochem Soc Trans 37: 937-953
    • (2009) Biochem Soc Trans , vol.37 , pp. 937-953
    • Komander, D.1
  • 10
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbé S (2009) Breaking the chains: structure and function of the deubiquitinases. Nat Rev Mol Cell Biol 10: 550-563
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbé, S.3
  • 13
    • 38149081168 scopus 로고    scopus 로고
    • Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation
    • Nakagawa T et al (2008) Deubiquitylation of histone H2A activates transcriptional initiation via trans-histone cross-talk with H3K4 di- and trimethylation. Genes Dev 22: 37-49
    • (2008) Genes Dev , vol.22 , pp. 37-49
    • Nakagawa, T.1
  • 15
    • 53249154203 scopus 로고    scopus 로고
    • Function and regulation of protein neddylation. 'Protein modifications: Beyond the usual suspects' review series
    • Rabut G, Peter M (2008) Function and regulation of protein neddylation. 'Protein modifications: beyond the usual suspects' review series. EMBO Rep 9: 969-976
    • (2008) EMBO Rep , vol.9 , pp. 969-976
    • Rabut, G.1    Peter, M.2
  • 17
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • Reyes-Turcu FE, Ventii KH, Wilkinson KD (2009) Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu Rev Biochem 78: 363-397
    • (2009) Annu Rev Biochem , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1    Ventii, K.H.2    Wilkinson, K.D.3
  • 18
    • 17844379780 scopus 로고    scopus 로고
    • Structural basis of NEDD8 ubiquitin discrimination by the deNEDDylating enzyme NEDP1
    • DOI 10.1038/sj.emboj.7600628
    • Shen L-n, Liu H, Dong C, Xirodimas D, Naismith JH, Hay RT (2005) Structural basis of NEDD8 ubiquitin discrimination by the deNEDDylating enzyme NEDP1. EMBO J 24: 1341-1351 (Pubitemid 40593055)
    • (2005) EMBO Journal , vol.24 , Issue.7 , pp. 1341-1351
    • Shen, L.-N.1    Liu, H.2    Dong, C.3    Xirodimas, D.4    Naismith, J.H.5    Hay, R.T.6
  • 19
    • 67649634849 scopus 로고    scopus 로고
    • Defining the human deubiquitinating enzyme interaction landscape
    • Sowa ME, Bennett EJ, Gygi SP, Harper JW (2009) Defining the human deubiquitinating enzyme interaction landscape. Cell 138: 389-403
    • (2009) Cell , vol.138 , pp. 389-403
    • Sowa, M.E.1    Bennett, E.J.2    Gygi, S.P.3    Harper, J.W.4
  • 20
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 A resolution
    • Vijay-Kumar S, Bugg CE, Cook WJ (1987) Structure of ubiquitin refined at 1.8 A resolution. J Mol Biol 194: 531-544
    • (1987) J Mol Biol , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 21
    • 28844440079 scopus 로고    scopus 로고
    • Derivitization of the C-terminus of ubiquitin and ubiquitin-like proteins using intein chemistry: Methods and uses
    • DOI 10.1016/S0076-6879(05)99001-0, PII S0076687905990034, 3, Ubiquitin and Protein Degradation, Part B
    • Wilkinson KD, Gan-Erdene T, Kolli N (2005) Derivitization of the C-terminus of ubiquitin and ubiquitin-like proteins using intein chemistry: methods and uses. Meth Enzymol 399: 37-51 (Pubitemid 41772720)
    • (2005) Methods in Enzymology , vol.399 , pp. 37-51
    • Wilkinson, K.D.1    Gan-Erdene, T.2    Kolli, N.3
  • 22
    • 74049114641 scopus 로고    scopus 로고
    • Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kB activation via binding to and deubiquitinating receptor-interacting protein 1
    • Xu G et al (2010) Ubiquitin-specific peptidase 21 inhibits tumor necrosis factor alpha-induced nuclear factor kB activation via binding to and deubiquitinating receptor-interacting protein 1. J Biol Chem 285: 969-978
    • (2010) J Biol Chem , vol.285 , pp. 969-978
    • Xu, G.1
  • 23
    • 72949102636 scopus 로고    scopus 로고
    • Dissection of USP catalytic domains reveals five common insertion points
    • Ye Y, Scheel H, Hofmann K, Komander D (2009) Dissection of USP catalytic domains reveals five common insertion points. Mol Biosyst 5: 1797-1808
    • (2009) Mol Biosyst , vol.5 , pp. 1797-1808
    • Ye, Y.1    Scheel, H.2    Hofmann, K.3    Komander, D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.