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Journal Abstract Search
829 related items for PubMed ID: 16198374
1. 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]
2. 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]
3. 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]
4. Mutational analysis of the energetics of the GrpE.DnaK binding interface: equilibrium association constants by sedimentation velocity analytical ultracentrifugation. Gelinas AD, Toth J, Bethoney KA, Stafford WF, Harrison CJ. J Mol Biol; 2004 May 28; 339(2):447-58. PubMed ID: 15136046 [Abstract] [Full Text] [Related]
5. GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Packschies L, Theyssen H, Buchberger A, Bukau B, Goody RS, Reinstein J. Biochemistry; 1997 Mar 25; 36(12):3417-22. PubMed ID: 9131990 [Abstract] [Full Text] [Related]
6. Complementation studies of the DnaK-DnaJ-GrpE chaperone machineries from Vibrio harveyi and Escherichia coli, both in vivo and in vitro. Zmijewski MA, Kwiatkowska JM, Lipińska B. Arch Microbiol; 2004 Dec 25; 182(6):436-49. PubMed ID: 15448982 [Abstract] [Full Text] [Related]
11. Structural basis of the interspecies interaction between the chaperone DnaK(Hsp70) and the co-chaperone GrpE of archaea and bacteria. Zmijewski MA, Skórko-Glonek J, Tanfani F, Banecki B, Kotlarz A, Macario AJ, Lipińska B. Acta Biochim Pol; 2007 Dec 25; 54(2):245-52. PubMed ID: 17565388 [Abstract] [Full Text] [Related]
12. The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system. Pierpaoli EV, Sandmeier E, Baici A, Schönfeld HJ, Gisler S, Christen P. J Mol Biol; 1997 Jun 27; 269(5):757-68. PubMed ID: 9223639 [Abstract] [Full Text] [Related]
13. The importance of having thermosensor control in the DnaK chaperone system. Siegenthaler RK, Christen P. J Biol Chem; 2005 Apr 15; 280(15):14395-401. PubMed ID: 15705578 [Abstract] [Full Text] [Related]
14. Thermal adaptation of the yeast mitochondrial Hsp70 system is regulated by the reversible unfolding of its nucleotide exchange factor. Moro F, Muga A. J Mol Biol; 2006 May 19; 358(5):1367-77. PubMed ID: 16600294 [Abstract] [Full Text] [Related]
15. Deletion of DnaK's lid strengthens binding to the nucleotide exchange factor, GrpE: a kinetic and thermodynamic analysis. Chesnokova LS, Slepenkov SV, Protasevich II, Sehorn MG, Brouillette CG, Witt SN. Biochemistry; 2003 Aug 05; 42(30):9028-40. PubMed ID: 12885236 [Abstract] [Full Text] [Related]
16. GrpE accelerates peptide binding and release from the high affinity state of DnaK. Mally A, Witt SN. Nat Struct Biol; 2001 Mar 05; 8(3):254-7. PubMed ID: 11224572 [Abstract] [Full Text] [Related]
17. New insights into the structure and function of the complex between the Escherichia coli Hsp70, DnaK, and its nucleotide-exchange factor, GrpE. Rossi MA, Pozhidaeva AK, Clerico EM, Petridis C, Gierasch LM. J Biol Chem; 2024 Jan 05; 300(1):105574. PubMed ID: 38110031 [Abstract] [Full Text] [Related]
18. Structural dynamics of the DnaK-peptide complex. Popp S, Packschies L, Radzwill N, Vogel KP, Steinhoff HJ, Reinstein J. J Mol Biol; 2005 Apr 15; 347(5):1039-52. PubMed ID: 15784262 [Abstract] [Full Text] [Related]
19. Modulation of the chaperone DnaK allosterism by the nucleotide exchange factor GrpE. Melero R, Moro F, Pérez-Calvo MÁ, Perales-Calvo J, Quintana-Gallardo L, Llorca O, Muga A, Valpuesta JM. J Biol Chem; 2015 Apr 17; 290(16):10083-92. PubMed ID: 25739641 [Abstract] [Full Text] [Related]
20. Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration. Diamant S, Goloubinoff P. Biochemistry; 1998 Jul 07; 37(27):9688-94. PubMed ID: 9657681 [Abstract] [Full Text] [Related] Page: [Next] [New Search]