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Cell Stress and Chaperones
Volumn 8, Issue 2, 2003, Pages 105-107
What is a co-chaperone?
Author keywords

[No Author keywords available]
Indexed keywords

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; CHAPERONE; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; PROTEIN KINASE C;
EID: 0043028205     PISSN: 13558145     EISSN: None     Source Type: Journal    
DOI: 10.1379/1466-1268(2003)008<0105:WIAC>2.0.CO;2     Document Type: Review
Times cited : (69)
References (8)
  • 1
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    • The tetratricopeptide repeat: A structural motif mediating protein-protein interactions
    • Blatch GL, Lassle M. 1999. The tetratricopeptide repeat: a structural motif mediating protein-protein interactions. Bioessays 21: 932-939.
    • (1999) Bioessays , vol.21 , pp. 932-939
    • Blatch, G.L.1    Lassle, M.2
  • 2
    • 0037150683 scopus 로고    scopus 로고
    • Disassembly of transcriptional regulatory complexes by molecular chaperones
    • Freeman BC, Yamamoto KR. 2002. Disassembly of transcriptional regulatory complexes by molecular chaperones. Science 296: 2232-2235.
    • (2002) Science , vol.296 , pp. 2232-2235
    • Freeman, B.C.1    Yamamoto, K.R.2
  • 3
    • 0034924812 scopus 로고    scopus 로고
    • Folding of newly translated proteins in vivo: The role of molecular chaperones
    • Frydman J. 2001. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem 70: 603-647.
    • (2001) Annu Rev Biochem , vol.70 , pp. 603-647
    • Frydman, J.1
  • 4
    • 0028842615 scopus 로고
    • Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle
    • Hohfeld J, Minami Y, Hartl FU. 1995. Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83: 589-598.
    • (1995) Cell , vol.83 , pp. 589-598
    • Hohfeld, J.1    Minami, Y.2    Hartl, F.U.3
  • 5
    • 0026596223 scopus 로고
    • Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding
    • Langer T, Lu C, Echols H, Flanagan J, Hayer MK, Hartl FU. 1992. Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding. Nature 356: 683-689.
    • (1992) Nature , vol.356 , pp. 683-689
    • Langer, T.1    Lu, C.2    Echols, H.3    Flanagan, J.4    Hayer, M.K.5    Hartl, F.U.6
  • 6
    • 0025730978 scopus 로고
    • Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK
    • Liberek K, Marszalek J, Ang D, Georgopoulos C, Zylicz M. 1991. Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK. Proc Natl Acad Sci U S A 88: 2874-2878.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 2874-2878
    • Liberek, K.1    Marszalek, J.2    Ang, D.3    Georgopoulos, C.4    Zylicz, M.5
  • 7
    • 0036911213 scopus 로고    scopus 로고
    • A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins
    • Meunier L, Usherwood YK, Chung KT, Hendershot LM. 2002. A subset of chaperones and folding enzymes form multiprotein complexes in endoplasmic reticulum to bind nascent proteins. Mol Biol Cell 13: 4456-4469.
    • (2002) Mol Biol Cell , vol.13 , pp. 4456-4469
    • Meunier, L.1    Usherwood, Y.K.2    Chung, K.T.3    Hendershot, L.M.4
  • 8
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    • Structure, function, and mechanism of the Hsp90 molecular chaperone
    • Pearl LH, Prodromou C. 2001. Structure, function, and mechanism of the Hsp90 molecular chaperone. Adv Protein Chem 59: 157-186.
    • (2001) Adv Protein Chem , vol.59 , pp. 157-186
    • Pearl, L.H.1    Prodromou, C.2

* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.