Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM048742-04
Application #
2186275
Study Section
Cellular Biology and Physiology Subcommittee 1 (CBY)
Project Start
1992-12-18
Project End
1996-12-31
Budget Start
1996-01-01
Budget End
1996-12-31
Support Year
4
Fiscal Year
1996
Total Cost
Indirect Cost
Name
Sloan-Kettering Institute for Cancer Research
Department
Type
DUNS #
064931884
City
New York
State
NY
Country
United States
Zip Code
10065
Hohfeld, J; Minami, Y; Hartl, F U (1995) Hip, a novel cochaperone involved in the eukaryotic Hsc70/Hsp40 reaction cycle. Cell 83:589-98
Hohfeld, J; Hartl, F U (1994) Role of the chaperonin cofactor Hsp10 in protein folding and sorting in yeast mitochondria. J Cell Biol 126:305-15
Szabo, A; Langer, T; Schroder, H et al. (1994) The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Proc Natl Acad Sci U S A 91:10345-9
Hayer-Hartl, M K; Ewbank, J J; Creighton, T E et al. (1994) Conformational specificity of the chaperonin GroEL for the compact folding intermediates of alpha-lactalbumin. EMBO J 13:3192-202
Li, W Z; Lin, P; Frydman, J et al. (1994) Tcp20, a subunit of the eukaryotic TRiC chaperonin from humans and yeast. J Biol Chem 269:18616-22
Nimmesgern, E; Hartl, F U (1993) ATP-dependent protein refolding activity in reticulocyte lysate. Evidence for the participation of different chaperone components. FEBS Lett 331:25-30
Schroder, H; Langer, T; Hartl, F U et al. (1993) DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. EMBO J 12:4137-44
Hendrick, J P; Langer, T; Davis, T A et al. (1993) Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides. Proc Natl Acad Sci U S A 90:10216-20