메뉴 건너뛰기




Volumn 15, Issue 7, 2005, Pages

SUMO modification: Wrestling with protein conformation

Author keywords

[No Author keywords available]

Indexed keywords


EID: 17144379416     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2005.03.021     Document Type: Short Survey
Times cited : (25)

References (15)
  • 1
    • 0035336677 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • R.T. Hay Protein modification by SUMO Trends Biochem. Sci. 26 2001 332 333
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 332-333
    • Hay, R.T.1
  • 2
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • E.S. Johnson Protein modification by SUMO Annu. Rev. Biochem. 73 2004 355 382
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 4
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus: Different functions, similar mechanisms?
    • G. Gill SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? Genes Dev. 18 2004 2046 2059
    • (2004) Genes Dev. , vol.18 , pp. 2046-2059
    • Gill, G.1
  • 6
    • 1942437991 scopus 로고    scopus 로고
    • SUMO: A regulator of gene expression and genome integrity
    • S. Muller, A. Ledl, and D. Schmidt SUMO: a regulator of gene expression and genome integrity Oncogene 23 2004 1998 2008
    • (2004) Oncogene , vol.23 , pp. 1998-2008
    • Muller, S.1    Ledl, A.2    Schmidt, D.3
  • 7
    • 17144410054 scopus 로고    scopus 로고
    • Functionality of human Thymine-DNA glycosylase requires SUMO regulated changes in protein conformation
    • R. Steinacher, and P. Schär Functionality of human Thymine-DNA glycosylase requires SUMO regulated changes in protein conformation this issue Curr. Biol. 2005
    • (2005) Curr. Biol.
    • Steinacher, R.1    Schär, P.2
  • 9
    • 0035111895 scopus 로고    scopus 로고
    • Recent progress in the biology, chemistry and structural biology of DNA glycosylases
    • O.D. Schärer, and J. Jiricny Recent progress in the biology, chemistry and structural biology of DNA glycosylases Bioessays 23 2001 270 281
    • (2001) Bioessays , vol.23 , pp. 270-281
    • Schärer, O.D.1    Jiricny, J.2
  • 10
    • 0025342965 scopus 로고
    • Repair of intrinsic DNA lesions
    • T. Lindahl Repair of intrinsic DNA lesions Mutat. Res. 238 1990 305 311
    • (1990) Mutat. Res. , vol.238 , pp. 305-311
    • Lindahl, T.1
  • 11
    • 0033520969 scopus 로고    scopus 로고
    • Quality control by DNA repair
    • T. Lindahl, and R.D. Wood Quality control by DNA repair Science 286 1999 1897 1905
    • (1999) Science , vol.286 , pp. 1897-1905
    • Lindahl, T.1    Wood, R.D.2
  • 12
    • 0034093291 scopus 로고    scopus 로고
    • Passing the baton in base excision repair
    • S.H. Wilson, and T.A. Kunkel Passing the baton in base excision repair Nat. Struct. Biol. 7 2000 176 178
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 176-178
    • Wilson, S.H.1    Kunkel, T.A.2
  • 13
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • U. Hardeland, R. Steinacher, J. Jiricny, and P. Schär Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover EMBO J. 21 2002 1456 1464
    • (2002) EMBO J. , vol.21 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schär, P.4
  • 14
    • 0037743666 scopus 로고    scopus 로고
    • Mismatch uracil glycosylase from Escherichia coli: A general mismatch or a specific DNA glycosylase?
    • R.J. O'Neill, O.V. Vorob'eva, H. Shahbakhti, E. Zmuda, A.S. Bhagwat, and G.S. Baldwin Mismatch uracil glycosylase from Escherichia coli: a general mismatch or a specific DNA glycosylase? J. Biol. Chem. 278 2003 20526 20532
    • (2003) J. Biol. Chem. , vol.278 , pp. 20526-20532
    • O'Neill, R.J.1    Vorob'Eva, O.V.2    Shahbakhti, H.3    Zmuda, E.4    Bhagwat, A.S.5    Baldwin, G.S.6
  • 15
    • 14044278774 scopus 로고    scopus 로고
    • Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein
    • H. Takahashi, S. Hatakeyama, H. Saitoh, and K.I. Nakayama Noncovalent SUMO-1 binding activity of thymine DNA glycosylase (TDG) is required for its SUMO-1 modification and colocalization with the promyelocytic leukemia protein J. Biol. Chem. 280 2005 5611 5621
    • (2005) J. Biol. Chem. , vol.280 , pp. 5611-5621
    • Takahashi, H.1    Hatakeyama, S.2    Saitoh, H.3    Nakayama, K.I.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.