메뉴 건너뛰기




Volumn 20, Issue 12, 2013, Pages 1447-1455

Deubiquitinating enzyme specificity for ubiquitin chain topology profiled by di-ubiquitin activity probes

Author keywords

[No Author keywords available]

Indexed keywords

DI UBIQUITIN; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 84890859198     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.chembiol.2013.10.012     Document Type: Article
Times cited : (83)

References (42)
  • 2
    • 0035903538 scopus 로고    scopus 로고
    • A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14
    • A. Borodovsky, B.M. Kessler, R. Casagrande, H.S. Overkleeft, K.D. Wilkinson, and H.L. Ploegh A novel active site-directed probe specific for deubiquitylating enzymes reveals proteasome association of USP14 EMBO J. 20 2001 5187 5196
    • (2001) EMBO J. , vol.20 , pp. 5187-5196
    • Borodovsky, A.1    Kessler, B.M.2    Casagrande, R.3    Overkleeft, H.S.4    Wilkinson, K.D.5    Ploegh, H.L.6
  • 4
    • 77955417276 scopus 로고    scopus 로고
    • Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne
    • A. Bremm, S.M. Freund, and D. Komander Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne Nat. Struct. Mol. Biol. 17 2010 939 947
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 939-947
    • Bremm, A.1    Freund, S.M.2    Komander, D.3
  • 5
    • 80455123843 scopus 로고    scopus 로고
    • Nonenzymatic assembly of natural polyubiquitin chains of any linkage composition and isotopic labeling scheme
    • C. Castañeda, J. Liu, A. Chaturvedi, U. Nowicka, T.A. Cropp, and D. Fushman Nonenzymatic assembly of natural polyubiquitin chains of any linkage composition and isotopic labeling scheme J. Am. Chem. Soc. 133 2011 17855 17868
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 17855-17868
    • Castañeda, C.1    Liu, J.2    Chaturvedi, A.3    Nowicka, U.4    Cropp, T.A.5    Fushman, D.6
  • 7
    • 84882627336 scopus 로고    scopus 로고
    • Naturally and synthetically linked lys48 diubiquitin: A QM/MM study
    • T. Dresselhaus, N.D. Weikart, H.D. Mootz, and M.P. Waller Naturally and synthetically linked lys48 diubiquitin: a QM/MM study RSC Advances 3 2013 16122 16129
    • (2013) RSC Advances , vol.3 , pp. 16122-16129
    • Dresselhaus, T.1    Weikart, N.D.2    Mootz, H.D.3    Waller, M.P.4
  • 13
    • 0025944815 scopus 로고
    • Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors
    • B. Johnsson, S. Löfås, and G. Lindquist Immobilization of proteins to a carboxymethyldextran-modified gold surface for biospecific interaction analysis in surface plasmon resonance sensors Anal. Biochem. 198 1991 268 277
    • (1991) Anal. Biochem. , vol.198 , pp. 268-277
    • Johnsson, B.1    Löfås, S.2    Lindquist, G.3
  • 16
    • 0037039298 scopus 로고    scopus 로고
    • Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation
    • K.L. Kiick, E. Saxon, D.A. Tirrell, and C.R. Bertozzi Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation Proc. Natl. Acad. Sci. USA 99 2002 19 24
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 19-24
    • Kiick, K.L.1    Saxon, E.2    Tirrell, D.A.3    Bertozzi, C.R.4
  • 19
    • 84864222562 scopus 로고    scopus 로고
    • Atypical ubiquitylation - The unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages
    • Y. Kulathu, and D. Komander Atypical ubiquitylation - the unexplored world of polyubiquitin beyond Lys48 and Lys63 linkages Nat. Rev. Mol. Cell Biol. 13 2012 508 523
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 508-523
    • Kulathu, Y.1    Komander, D.2
  • 21
    • 34548170626 scopus 로고    scopus 로고
    • Preparation of the functionalizable methionine surrogate azidohomoalanine via copper-catalyzed diazo transfer
    • A.J. Link, M.K. Vink, and D.A. Tirrell Preparation of the functionalizable methionine surrogate azidohomoalanine via copper-catalyzed diazo transfer Nat. Protoc. 2 2007 1879 1883
    • (2007) Nat. Protoc. , vol.2 , pp. 1879-1883
    • Link, A.J.1    Vink, M.K.2    Tirrell, D.A.3
  • 22
    • 65649126339 scopus 로고    scopus 로고
    • Ubiquitin C-terminal electrophiles are activity-based probes for identification and mechanistic study of ubiquitin conjugating machinery
    • K.R. Love, R.K. Pandya, E. Spooner, and H.L. Ploegh Ubiquitin C-terminal electrophiles are activity-based probes for identification and mechanistic study of ubiquitin conjugating machinery ACS Chem. Biol. 4 2009 275 287
    • (2009) ACS Chem. Biol. , vol.4 , pp. 275-287
    • Love, K.R.1    Pandya, R.K.2    Spooner, E.3    Ploegh, H.L.4
  • 28
    • 28844462033 scopus 로고    scopus 로고
    • Controlled synthesis of polyubiquitin chains
    • C.M. Pickart, and S. Raasi Controlled synthesis of polyubiquitin chains Methods Enzymol. 399 2005 21 36
    • (2005) Methods Enzymol. , vol.399 , pp. 21-36
    • Pickart, C.M.1    Raasi, S.2
  • 29
    • 0030863993 scopus 로고    scopus 로고
    • Inhibition of the 26 S proteasome by polyubiquitin chains synthesized to have defined lengths
    • J. Piotrowski, R. Beal, L. Hoffman, K.D. Wilkinson, R.E. Cohen, and C.M. Pickart Inhibition of the 26 S proteasome by polyubiquitin chains synthesized to have defined lengths J. Biol. Chem. 272 1997 23712 23721
    • (1997) J. Biol. Chem. , vol.272 , pp. 23712-23721
    • Piotrowski, J.1    Beal, R.2    Hoffman, L.3    Wilkinson, K.D.4    Cohen, R.E.5    Pickart, C.M.6
  • 30
    • 67650620318 scopus 로고    scopus 로고
    • Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes
    • F.E. Reyes-Turcu, K.H. Ventii, and K.D. Wilkinson Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes Annu. Rev. Biochem. 78 2009 363 397
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 363-397
    • Reyes-Turcu, F.E.1    Ventii, K.H.2    Wilkinson, K.D.3
  • 31
    • 0037099395 scopus 로고    scopus 로고
    • A stepwise Huisgen cycloaddition process: Copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes
    • V.V. Rostovtsev, L.G. Green, V.V. Fokin, and K.B. Sharpless A stepwise Huisgen cycloaddition process: copper(I)-catalyzed regioselective "ligation" of azides and terminal alkynes Angew. Chem. Int. Ed. Engl. 41 2002 2596 2599
    • (2002) Angew. Chem. Int. Ed. Engl. , vol.41 , pp. 2596-2599
    • Rostovtsev, V.V.1    Green, L.G.2    Fokin, V.V.3    Sharpless, K.B.4
  • 33
    • 77956903406 scopus 로고    scopus 로고
    • Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase
    • S. Virdee, Y. Ye, D.P. Nguyen, D. Komander, and J.W. Chin Engineered diubiquitin synthesis reveals Lys29-isopeptide specificity of an OTU deubiquitinase Nat. Chem. Biol. 6 2010 750 757
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 750-757
    • Virdee, S.1    Ye, Y.2    Nguyen, D.P.3    Komander, D.4    Chin, J.W.5
  • 35
    • 38849132058 scopus 로고    scopus 로고
    • Processing of N-terminal unnatural amino acids in recombinant human interferon-beta in Escherichia coli
    • A. Wang, N. Winblade Nairn, R.S. Johnson, D.A. Tirrell, and K. Grabstein Processing of N-terminal unnatural amino acids in recombinant human interferon-beta in Escherichia coli ChemBioChem 9 2008 324 330
    • (2008) ChemBioChem , vol.9 , pp. 324-330
    • Wang, A.1    Winblade Nairn, N.2    Johnson, R.S.3    Tirrell, D.A.4    Grabstein, K.5
  • 36
    • 77950671571 scopus 로고    scopus 로고
    • Generation of site-specific and enzymatically stable conjugates of recombinant proteins with ubiquitin-like modifiers by the Cu(I)-catalyzed azide-alkyne cycloaddition
    • N.D. Weikart, and H.D. Mootz Generation of site-specific and enzymatically stable conjugates of recombinant proteins with ubiquitin-like modifiers by the Cu(I)-catalyzed azide-alkyne cycloaddition ChemBioChem 11 2010 774 777
    • (2010) ChemBioChem , vol.11 , pp. 774-777
    • Weikart, N.D.1    Mootz, H.D.2
  • 37
    • 82555193829 scopus 로고    scopus 로고
    • Click synthesis of ubiquitin dimer analogs to interrogate linkage-specific UBA domain binding
    • N.D. Weikart, S. Sommer, and H.D. Mootz Click synthesis of ubiquitin dimer analogs to interrogate linkage-specific UBA domain binding Chem. Commun. (Camb.) 48 2012 296 298
    • (2012) Chem. Commun. (Camb.) , vol.48 , pp. 296-298
    • Weikart, N.D.1    Sommer, S.2    Mootz, H.D.3
  • 40
    • 77956841522 scopus 로고    scopus 로고
    • Synthesis of K48-linked diubiquitin using dual native chemical ligation at lysine
    • R. Yang, K.K. Pasunooti, F. Li, X.W. Liu, and C.F. Liu Synthesis of K48-linked diubiquitin using dual native chemical ligation at lysine Chem. Commun. (Camb.) 46 2010 7199 7201
    • (2010) Chem. Commun. (Camb.) , vol.46 , pp. 7199-7201
    • Yang, R.1    Pasunooti, K.K.2    Li, F.3    Liu, X.W.4    Liu, C.F.5
  • 42
    • 84055178186 scopus 로고    scopus 로고
    • Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains
    • Z.R. Zhou, Y.H. Zhang, S. Liu, A.X. Song, and H.Y. Hu Length of the active-site crossover loop defines the substrate specificity of ubiquitin C-terminal hydrolases for ubiquitin chains Biochem. J. 441 2012 143 149
    • (2012) Biochem. J. , vol.441 , pp. 143-149
    • Zhou, Z.R.1    Zhang, Y.H.2    Liu, S.3    Song, A.X.4    Hu, H.Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.