메뉴 건너뛰기




Volumn 787, Issue , 2011, Pages 137-143

Quantification of HSP27 and HSP70 Molecular Chaperone Activities

Author keywords

Chaperone activity; Chemical and thermal aggregation; HSP27; HSP70; Screening

Indexed keywords

HEAT SHOCK PROTEIN 27; HEAT SHOCK PROTEIN 70;

EID: 80054726322     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-61779-295-3_11     Document Type: Chapter
Times cited : (15)

References (9)
  • 2
    • 0025303147 scopus 로고
    • Interaction of Hsp 70 with newly synthesized proteins: Implications for protein folding and assembly
    • Beckmann, R.P., Mizzen, L.E., Welch, W. J. (1990) Interaction of Hsp 70 with newly synthesized proteins: implications for protein folding and assembly. Science. 248, 850–854.
    • (1990) Science , vol.248 , pp. 850-854
    • Beckmann, R.P.1    Mizzen, L.E.2    Welch, W.J.3
  • 3
    • 33646557371 scopus 로고    scopus 로고
    • Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling
    • De Los Rios, P., Ben-Zvi, A., Slutsky, O., Azem, A., Goloubinoff, P. (2006) Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling. Proc Natl Acad Sci. USA. 103, 6166–6171.
    • (2006) Proc Natl Acad Sci. USA. , vol.103 , pp. 6166-6171
    • de Los Rios, P.1    Ben-Zvi, A.2    Slutsky, O.3    Azem, A.4    Goloubinoff, P.5
  • 4
    • 0026643651 scopus 로고
    • The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate
    • Shi, Y., Thomas, J. O. (1992) The transport of proteins into the nucleus requires the 70-kilodalton heat shock protein or its cytosolic cognate. Mol Cell Biol. 12, 2186–2192.
    • (1992) Mol Cell Biol , vol.12 , pp. 2186-2192
    • Shi, Y.1    Thomas, J.O.2
  • 6
    • 0343742639 scopus 로고    scopus 로고
    • Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
    • Ehrnsperger, M., Gräber, S., Gaestel, M., Buchner, J. (1997) Binding of non-native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation. EMBO J. 16, 221–229.
    • (1997) EMBO J , vol.16 , pp. 221-229
    • Ehrnsperger, M.1    Gräber, S.2    Gaestel, M.3    Buchner, J.4
  • 7
    • 14044272992 scopus 로고    scopus 로고
    • Mechanism of chaperone function in small heat shock proteins: Dissociation of the HSP27 oligomer is required for recognition and binding of desta-bilized T4 lysozyme
    • Shashidharamurthy, R., Koteiche, H. A., Dong, J., McHaourab, H. S. (2005) Mechanism of chaperone function in small heat shock proteins: dissociation of the HSP27 oligomer is required for recognition and binding of desta-bilized T4 lysozyme. J Biol Chem. 280, 5281–5289.
    • (2005) J Biol Chem , vol.280 , pp. 5281-5289
    • Shashidharamurthy, R.1    Koteiche, H.A.2    Dong, J.3    McHaourab, H.S.4
  • 8
    • 0034609765 scopus 로고    scopus 로고
    • Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo
    • Bruey, J. M., Paul, C., Fromentin, A., Hilpert, S., Arrigo, A. P., Solary, E., Garrido, C. (2000) Differential regulation of HSP27 oligomerization in tumor cells grown in vitro and in vivo. Oncogene. 19, 4855–4863.
    • (2000) Oncogene , vol.19 , pp. 4855-4863
    • Bruey, J.M.1    Paul, C.2    Fromentin, A.3    Hilpert, S.4    Arrigo, A.P.5    Solary, E.6    Garrido, C.7
  • 9
    • 33646345849 scopus 로고    scopus 로고
    • Self-association and chaperone activity of Hsp27 are thermally activated
    • Lelj-Garolla, B., Mauk, A. G. (2006) Self-association and chaperone activity of Hsp27 are thermally activated. J Biol Chem. 281, 8169–8174.
    • (2006) J Biol Chem , vol.281 , pp. 8169-8174
    • Lelj-Garolla, B.1    Mauk, A.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.