Conformational Properties of Substrate Proteins Bound to a Molecular Chaperone α-Crystallin
Open Access
- 1 May 1996
- journal article
- Published by Elsevier
- Vol. 271 (18), 10449-10452
- https://doi.org/10.1074/jbc.271.18.10449
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- On the interaction of α-crystallin with unfolded proteinsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1995
- Temperature‐induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α‐crystallinFEBS Letters, 1995
- On the thermal stability of .alpha.-crystallin: z new insight from infrared spectroscopyBiochemistry, 1995
- αA‐crystallin confers cellular thermoresistanceFEBS Letters, 1994
- Residues in chaperonin GroEL required for polypeptide binding and releaseNature, 1994
- Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperonesTrends in Biochemical Sciences, 1994
- Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein foldingNature, 1992
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- αB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brainCell, 1989
- Structural Homology of lens crystallinsBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1983