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Volumn 10, Issue 4, 2000, Pages

The U box is a modified RING finger - A common domain in ubiquitination [1]

Author keywords

[No Author keywords available]

Indexed keywords

ANIMALIA; HERPES; HUMAN HERPESVIRUS 1;

EID: 0034708216     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(00)00398-5     Document Type: Letter
Times cited : (361)

References (19)
  • 1
    • 0032535483 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: On protein death and cell life
    • Ciechanover A. The ubiquitin-proteasome pathway: on protein death and cell life. EMBO J. 17:1998;7151-7160.
    • (1998) EMBO J , vol.17 , pp. 7151-7160
    • Ciechanover, A.1
  • 4
    • 0033525589 scopus 로고    scopus 로고
    • A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly
    • Koegl M., Hoppe T., Schlenker S., Ulrich H.D., Mayer T.U., Jentsch S. A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly. Cell. 96:1999;635-644.
    • (1999) Cell , vol.96 , pp. 635-644
    • Koegl, M.1    Hoppe, T.2    Schlenker, S.3    Ulrich, H.D.4    Mayer, T.U.5    Jentsch, S.6
  • 5
    • 0027239790 scopus 로고
    • The RING finger. A novel protein sequence motif related to the zinc finger
    • Freemont P.S. The RING finger. A novel protein sequence motif related to the zinc finger. Ann NY Acad Sci. 684:1993;174-192.
    • (1993) Ann NY Acad Sci , vol.684 , pp. 174-192
    • Freemont, P.S.1
  • 8
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 9
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • Rost B., Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins. 19:1994;55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 10
    • 0031577260 scopus 로고    scopus 로고
    • Protein, fold recognition by prediction-based threading
    • Rost B., Schneider R., Sander C. Protein, fold recognition by prediction-based threading. J Mol Biol. 270:1997;471-480.
    • (1997) J Mol Biol , vol.270 , pp. 471-480
    • Rost, B.1    Schneider, R.2    Sander, C.3
  • 11
    • 0033537993 scopus 로고    scopus 로고
    • GenTHREADER: An efficient and reliable protein fold recognition method for genomic sequences
    • Jones D.T. GenTHREADER: an efficient and reliable protein fold recognition method for genomic sequences. J Mol Biol. 287:1999;797-815.
    • (1999) J Mol Biol , vol.287 , pp. 797-815
    • Jones, D.T.1
  • 12
    • 0030053370 scopus 로고    scopus 로고
    • ProMod and Swiss-MModel: Internet-based tools for automated comparative protein modelling
    • Peitsch M.C. ProMod and Swiss-MModel: Internet-based tools for automated comparative protein modelling. Biochem Soc Trans. 24:1996;274-279.
    • (1996) Biochem Soc Trans , vol.24 , pp. 274-279
    • Peitsch, M.C.1
  • 13
    • 0028181750 scopus 로고
    • Structure, of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy. A new structural class of zinc-finger
    • Barlow P.N., Luisi B., Milner A., Elliott M., Everett M. Structure, of the C3HC4 domain by 1H-nuclear magnetic resonance spectroscopy. A new structural class of zinc-finger. J Mol Biol. 237:1994;201-211.
    • (1994) J Mol Biol , vol.237 , pp. 201-211
    • Barlow, P.N.1    Luisi, B.2    Milner, A.3    Elliott, M.4    Everett, M.5
  • 14
    • 0030959658 scopus 로고    scopus 로고
    • Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster
    • Bellon S.F., Rodgers K.K., Schatz D.G., Coleman J.E., Steitz T.A. Crystal structure of the RAG1 dimerization domain reveals multiple zinc-binding motifs including a novel zinc binuclear cluster. Nat Struct Biol. 4:1997;586-591.
    • (1997) Nat Struct Biol , vol.4 , pp. 586-591
    • Bellon, S.F.1    Rodgers, K.K.2    Schatz, D.G.3    Coleman, J.E.4    Steitz, T.A.5
  • 15
    • 0033120027 scopus 로고    scopus 로고
    • ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity
    • Ohta T., Michel J.J., Schottelius A.J., Xiong Y. ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity. Mol Cell. 3:1999;535-541.
    • (1999) Mol Cell , vol.3 , pp. 535-541
    • Ohta, T.1    Michel, J.J.2    Schottelius, A.J.3    Xiong, Y.4
  • 17
    • 0033536637 scopus 로고    scopus 로고
    • The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase
    • Joazeiro C.A., Wing S.S., Huang H., Leverson J.D., Hunter T., Liu Y.C. The tyrosine kinase negative regulator c-Cbl as a RING-type, E2-dependent ubiquitin-protein ligase. Science. 286:1999;309-312.
    • (1999) Science , vol.286 , pp. 309-312
    • Joazeiro, C.A.1    Wing, S.S.2    Huang, H.3    Leverson, J.D.4    Hunter, T.5    Liu, Y.C.6
  • 19
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • Ballinger C.A., Connell P., Wu Y., Hu Z., Thompson L.J., Yin L.Y., Patterson C. Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions. Mol Cell Biol. 19:1999;4535-4545.
    • (1999) Mol Cell Biol , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.