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249 related items for PubMed ID: 19594134
1. Nucleotide binding and allosteric modulation of the second AAA+ domain of ClpB probed by transient kinetic studies. Werbeck ND, Kellner JN, Barends TR, Reinstein J. Biochemistry; 2009 Aug 04; 48(30):7240-50. PubMed ID: 19594134 [Abstract] [Full Text] [Related]
2. Coupling of oligomerization and nucleotide binding in the AAA+ chaperone ClpB. Werbeck ND, Zeymer C, Kellner JN, Reinstein J. Biochemistry; 2011 Feb 08; 50(5):899-909. PubMed ID: 21182296 [Abstract] [Full Text] [Related]
3. Crystal structure of E. coli Hsp100 ClpB nucleotide-binding domain 1 (NBD1) and mechanistic studies on ClpB ATPase activity. Li J, Sha B. J Mol Biol; 2002 May 10; 318(4):1127-37. PubMed ID: 12054807 [Abstract] [Full Text] [Related]
4. The chaperone function of ClpB from Thermus thermophilus depends on allosteric interactions of its two ATP-binding sites. Schlee S, Groemping Y, Herde P, Seidel R, Reinstein J. J Mol Biol; 2001 Mar 02; 306(4):889-99. PubMed ID: 11243796 [Abstract] [Full Text] [Related]
5. Coupling and dynamics of subunits in the hexameric AAA+ chaperone ClpB. Werbeck ND, Schlee S, Reinstein J. J Mol Biol; 2008 Apr 18; 378(1):178-90. PubMed ID: 18343405 [Abstract] [Full Text] [Related]
6. 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]
7. M domains couple the ClpB threading motor with the DnaK chaperone activity. Haslberger T, Weibezahn J, Zahn R, Lee S, Tsai FT, Bukau B, Mogk A. Mol Cell; 2007 Jan 26; 25(2):247-60. PubMed ID: 17244532 [Abstract] [Full Text] [Related]
8. 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]
9. The molecular mechanism of Hsp100 chaperone inhibition by the prion curing agent guanidinium chloride. Zeymer C, Werbeck ND, Schlichting I, Reinstein J. J Biol Chem; 2013 Mar 08; 288(10):7065-76. PubMed ID: 23341453 [Abstract] [Full Text] [Related]
10. Nucleotide utilization requirements that render ClpB active as a chaperone. del Castillo U, Fernández-Higuero JA, Pérez-Acebrón S, Moro F, Muga A. FEBS Lett; 2010 Mar 05; 584(5):929-34. PubMed ID: 20085762 [Abstract] [Full Text] [Related]
11. Roles of conserved arginines in ATP-binding domains of AAA+ chaperone ClpB from Thermus thermophilus. Yamasaki T, Nakazaki Y, Yoshida M, Watanabe YH. FEBS J; 2011 Jul 05; 278(13):2395-403. PubMed ID: 21554542 [Abstract] [Full Text] [Related]
12. trans-Acting arginine residues in the AAA+ chaperone ClpB allosterically regulate the activity through inter- and intradomain communication. Zeymer C, Fischer S, Reinstein J. J Biol Chem; 2014 Nov 21; 289(47):32965-76. PubMed ID: 25253689 [Abstract] [Full Text] [Related]
13. The functional cycle and regulation of the Thermus thermophilus DnaK chaperone system. Klostermeier D, Seidel R, Reinstein J. J Mol Biol; 1999 Apr 02; 287(3):511-25. PubMed ID: 10092456 [Abstract] [Full Text] [Related]
14. Interactions within the ClpB/DnaK bi-chaperone system from Escherichia coli. Kedzierska S, Chesnokova LS, Witt SN, Zolkiewski M. Arch Biochem Biophys; 2005 Dec 01; 444(1):61-5. PubMed ID: 16289019 [Abstract] [Full Text] [Related]
15. Stability of the two wings of the coiled-coil domain of ClpB chaperone is critical for its disaggregation activity. Watanabe YH, Nakazaki Y, Suno R, Yoshida M. Biochem J; 2009 Jun 12; 421(1):71-7. PubMed ID: 19351326 [Abstract] [Full Text] [Related]
16. Photophysical properties of popular fluorescent adenosine nucleotide analogs used in enzyme mechanism probing. Leskovar A, Reinstein J. Arch Biochem Biophys; 2008 May 01; 473(1):16-24. PubMed ID: 18342617 [Abstract] [Full Text] [Related]
17. Heptameric ring structure of the heat-shock protein ClpB, a protein-activated ATPase in Escherichia coli. Kim KI, Cheong GW, Park SC, Ha JS, Woo KM, Choi SJ, Chung CH. J Mol Biol; 2000 Nov 10; 303(5):655-66. PubMed ID: 11061966 [Abstract] [Full Text] [Related]
18. 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]
19. Processing of proteins by the molecular chaperone Hsp104. Schaupp A, Marcinowski M, Grimminger V, Bösl B, Walter S. J Mol Biol; 2007 Jul 20; 370(4):674-86. PubMed ID: 17543332 [Abstract] [Full Text] [Related]
20. The ClpB/Hsp104 molecular chaperone-a protein disaggregating machine. Lee S, Sowa ME, Choi JM, Tsai FT. J Struct Biol; 2004 Jul 20; 146(1-2):99-105. PubMed ID: 15037241 [Abstract] [Full Text] [Related] Page: [Next] [New Search]