메뉴 건너뛰기




Volumn 287, Issue 3, 2001, Pages 642-647

α-B- and α-A-crystallin prevent irreversible acidification-induced protein denaturation

Author keywords

Acidification; Molecular chaperone; Reactivation; Small heat shock protein; A crystallin; B crystallin; crystallin

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; HEAT SHOCK PROTEIN; LUCIFERASE;

EID: 0035964739     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1006/bbrc.2001.5636     Document Type: Article
Times cited : (14)

References (51)
  • 18
    • 0028282965 scopus 로고
    • The chaperone activity of bovine α-crystallin: Interaction with other lens crystallins in native and denatured states
    • (1994) J. Biol. Chem. , vol.269 , pp. 13601-13608
    • Wang, K.1    Spector, A.2
  • 23
    • 0033863553 scopus 로고    scopus 로고
    • Alpha-crystallin prevents irreversible protein denaturation and acts cooperatively with other HSPs to renature the stabilized partially denatured protein in an ATP dependent manner
    • (2000) Eur. J. Biochem. , vol.267 , pp. 4705-4712
    • Wang, K.1    Spector, A.2
  • 31
    • 0035819541 scopus 로고    scopus 로고
    • The lens protein alpha-B-crystallin of the blind subterranean mole-rat: High homology with sighted mammals
    • (2001) Gene , vol.264 , pp. 45-49
    • Avivi, A.1    Joel, A.2    Nevo, E.3
  • 41
    • 0029658123 scopus 로고    scopus 로고
    • α-Crystallin stabilizes actin filaments and prevents cytochalasin-induced depolymerization in a phosphorylation-dependent manner
    • (1996) Eur. J. Biochem. , vol.242 , pp. 56-66
    • Wang, K.1    Spector, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.