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144 related items for PubMed ID: 1544910
1. DnaK, hsp73, and their molten globules. Two different ways heat shock proteins respond to heat. Palleros DR, Reid KL, McCarty JS, Walker GC, Fink AL. J Biol Chem; 1992 Mar 15; 267(8):5279-85. PubMed ID: 1544910 [Abstract] [Full Text] [Related]
2. Protein conformational changes induced by 1,1'-bis(4-anilino-5-naphthalenesulfonic acid): preferential binding to the molten globule of DnaK. Shi L, Palleros DR, Fink AL. Biochemistry; 1994 Jun 21; 33(24):7536-46. PubMed ID: 8011619 [Abstract] [Full Text] [Related]
3. Physical interactions between members of the DnaK chaperone machinery: characterization of the DnaK.GrpE complex. Reid KL, Fink AL. Cell Stress Chaperones; 1996 Jun 21; 1(2):127-37. PubMed ID: 9222598 [Abstract] [Full Text] [Related]
4. Reversible thermal transition in GrpE, the nucleotide exchange factor of the DnaK heat-shock system. Grimshaw JP, Jelesarov I, Schönfeld HJ, Christen P. J Biol Chem; 2001 Mar 02; 276(9):6098-104. PubMed ID: 11084044 [Abstract] [Full Text] [Related]
5. The heat-sensitive Escherichia coli grpE280 phenotype: impaired interaction of GrpE(G122D) with DnaK. Grimshaw JP, Siegenthaler RK, Züger S, Schönfeld HJ, Z'graggen BR, Christen P. J Mol Biol; 2005 Nov 04; 353(4):888-96. PubMed ID: 16198374 [Abstract] [Full Text] [Related]
6. Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures. Grimshaw JP, Jelesarov I, Siegenthaler RK, Christen P. J Biol Chem; 2003 May 23; 278(21):19048-53. PubMed ID: 12639955 [Abstract] [Full Text] [Related]
11. Folding properties of the nucleotide exchange factor GrpE from Thermus thermophilus: GrpE is a thermosensor that mediates heat shock response. Groemping Y, Reinstein J. J Mol Biol; 2001 Nov 16; 314(1):167-78. PubMed ID: 11724541 [Abstract] [Full Text] [Related]
12. Thermodynamic and structural analysis of the folding/unfolding transitions of the Escherichia coli molecular chaperone DnaK. Montgomery D, Jordan R, McMacken R, Freire E. J Mol Biol; 1993 Jul 20; 232(2):680-92. PubMed ID: 8102181 [Abstract] [Full Text] [Related]
13. Real time kinetics of the DnaK/DnaJ/GrpE molecular chaperone machine action. Banecki B, Zylicz M. J Biol Chem; 1996 Mar 15; 271(11):6137-43. PubMed ID: 8626401 [Abstract] [Full Text] [Related]
14. Three-state denaturation of DnaK induced by guanidine hydrochloride. Evidence for an expandable intermediate. Palleros DR, Shi L, Reid KL, Fink AL. Biochemistry; 1993 Apr 27; 32(16):4314-21. PubMed ID: 8476860 [Abstract] [Full Text] [Related]
15. The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE. Szabo A, Langer T, Schröder H, Flanagan J, Bukau B, Hartl FU. Proc Natl Acad Sci U S A; 1994 Oct 25; 91(22):10345-9. PubMed ID: 7937953 [Abstract] [Full Text] [Related]
16. Regulation of ATPase and chaperone cycle of DnaK from Thermus thermophilus by the nucleotide exchange factor GrpE. Groemping Y, Klostermeier D, Herrmann C, Veit T, Seidel R, Reinstein J. J Mol Biol; 2001 Feb 02; 305(5):1173-83. PubMed ID: 11162122 [Abstract] [Full Text] [Related]
17. Kinetics of the reactions of the Escherichia coli molecular chaperone DnaK with ATP: evidence that a three-step reaction precedes ATP hydrolysis. Slepenkov SV, Witt SN. Biochemistry; 1998 Jan 27; 37(4):1015-24. PubMed ID: 9454592 [Abstract] [Full Text] [Related]
18. hsp70-protein complexes. Complex stability and conformation of bound substrate protein. Palleros DR, Shi L, Reid KL, Fink AL. J Biol Chem; 1994 May 06; 269(18):13107-14. PubMed ID: 8175736 [Abstract] [Full Text] [Related]