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Volumn 23, Issue 2, 2015, Pages 418-424

Crystal structure of the human 20S proteasome in complex with carfilzomib

Author keywords

[No Author keywords available]

Indexed keywords

20S PROTEASOME; CARFILZOMIB; CHYMOTRYPSIN; PROTEASOME; UNCLASSIFIED DRUG; OLIGOPEPTIDE;

EID: 84930188528     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2014.11.017     Document Type: Article
Times cited : (135)

References (21)
  • 5
    • 0031973736 scopus 로고    scopus 로고
    • Immunoproteasome assembly: Cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits
    • T.A. Griffin, D. Nandi, M. Cruz, H.J. Fehling, L.V. Kaer, J.J. Monaco, and R.A. Colbert Immunoproteasome assembly: cooperative incorporation of interferon gamma (IFN-gamma)-inducible subunits J. Exp. Med. 187 1998 97 104
    • (1998) J. Exp. Med. , vol.187 , pp. 97-104
    • Griffin, T.A.1    Nandi, D.2    Cruz, M.3    Fehling, H.J.4    Kaer, L.V.5    Monaco, J.J.6    Colbert, R.A.7
  • 6
    • 72949103056 scopus 로고    scopus 로고
    • Proteasomes in immune cells: More than peptide producers?
    • M. Groettrup, C.J. Kirk, and M. Basler Proteasomes in immune cells: more than peptide producers? Nat. Rev. Immunol. 10 2010 73 78
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 73-78
    • Groettrup, M.1    Kirk, C.J.2    Basler, M.3
  • 9
    • 0343262654 scopus 로고    scopus 로고
    • Crystal structure of epoxomicin: 20S proteasome reveals a molecular basis for selectivity of alpha ',beta '-epoxyketone proteasome inhibitors
    • M. Groll, K.B. Kim, N. Kairies, R. Huber, and C.M. Crews Crystal structure of epoxomicin: 20S proteasome reveals a molecular basis for selectivity of alpha ',beta '-epoxyketone proteasome inhibitors J. Am. Chem. Soc. 122 2000 1237 1238
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 1237-1238
    • Groll, M.1    Kim, K.B.2    Kairies, N.3    Huber, R.4    Crews, C.M.5
  • 10
    • 33646137808 scopus 로고    scopus 로고
    • Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding
    • M. Groll, R. Huber, and B.C. Potts Crystal structures of Salinosporamide A (NPI-0052) and B (NPI-0047) in complex with the 20S proteasome reveal important consequences of beta-lactone ring opening and a mechanism for irreversible binding J. Am. Chem. Soc. 128 2006 5136 5141
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 5136-5141
    • Groll, M.1    Huber, R.2    Potts, B.C.3
  • 11
    • 84857313367 scopus 로고    scopus 로고
    • Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity
    • E.M. Huber, M. Basler, R. Schwab, W. Heinemeyer, C.J. Kirk, M. Groettrup, and M. Groll Immuno- and constitutive proteasome crystal structures reveal differences in substrate and inhibitor specificity Cell 148 2012 727 738
    • (2012) Cell , vol.148 , pp. 727-738
    • Huber, E.M.1    Basler, M.2    Schwab, R.3    Heinemeyer, W.4    Kirk, C.J.5    Groettrup, M.6    Groll, M.7
  • 12
    • 33646407310 scopus 로고    scopus 로고
    • MG132 induced apoptosis is associated with p53-independent induction of pro-apoptotic Noxa and transcriptional activity of beta-catenin
    • M. Jullig, W.V. Zhang, A. Ferreira, and N.S. Stott MG132 induced apoptosis is associated with p53-independent induction of pro-apoptotic Noxa and transcriptional activity of beta-catenin Apoptosis 11 2006 627 641
    • (2006) Apoptosis , vol.11 , pp. 627-641
    • Jullig, M.1    Zhang, W.V.2    Ferreira, A.3    Stott, N.S.4
  • 13
    • 0033197542 scopus 로고    scopus 로고
    • Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown
    • A.F. Kisselev, T.N. Akopian, V. Castillo, and A.L. Goldberg Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown Mol. Cell 4 1999 395 402
    • (1999) Mol. Cell , vol.4 , pp. 395-402
    • Kisselev, A.F.1    Akopian, T.N.2    Castillo, V.3    Goldberg, A.L.4
  • 14
    • 0032568514 scopus 로고    scopus 로고
    • Kinetic studies of the branched chain amino acid preferring peptidase activity of the 20S proteasome: Development of a continuous assay and inhibition by tripeptide aldehydes and clasto-lactacystin beta-lactone
    • T.A. McCormack, A.A. Cruikshank, L. Grenier, F.D. Melandri, S.L. Nunes, L. Plamondon, R.L. Stein, and L.R. Dick Kinetic studies of the branched chain amino acid preferring peptidase activity of the 20S proteasome: development of a continuous assay and inhibition by tripeptide aldehydes and clasto-lactacystin beta-lactone Biochemistry 37 1998 7792 7800
    • (1998) Biochemistry , vol.37 , pp. 7792-7800
    • McCormack, T.A.1    Cruikshank, A.A.2    Grenier, L.3    Melandri, F.D.4    Nunes, S.L.5    Plamondon, L.6    Stein, R.L.7    Dick, L.R.8
  • 19
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • D. Voges, P. Zwickl, and W. Baumeister The 26S proteasome: a molecular machine designed for controlled proteolysis Annu. Rev. Biochem. 68 1999 1015 1068
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.