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473 related items for PubMed ID: 19698713
21. Crowding Modulates the Conformation, Affinity, and Activity of the Components of the Bacterial Disaggregase Machinery. Celaya G, Fernández-Higuero JA, Martin I, Rivas G, Moro F, Muga A. J Mol Biol; 2016 Jun 05; 428(11):2474-2487. PubMed ID: 27133933 [Abstract] [Full Text] [Related]
22. The N-terminal domain of Escherichia coli ClpB enhances chaperone function. Chow IT, Barnett ME, Zolkiewski M, Baneyx F. FEBS Lett; 2005 Aug 15; 579(20):4242-8. PubMed ID: 16051221 [Abstract] [Full Text] [Related]
23. E. coli transports aggregated proteins to the poles by a specific and energy-dependent process. Rokney A, Shagan M, Kessel M, Smith Y, Rosenshine I, Oppenheim AB. J Mol Biol; 2009 Sep 25; 392(3):589-601. PubMed ID: 19596340 [Abstract] [Full Text] [Related]
24. Protein disaggregation by the AAA+ chaperone ClpB involves partial threading of looped polypeptide segments. Haslberger T, Zdanowicz A, Brand I, Kirstein J, Turgay K, Mogk A, Bukau B. Nat Struct Mol Biol; 2008 Jun 25; 15(6):641-50. PubMed ID: 18488042 [Abstract] [Full Text] [Related]
25. Synergistic coordination of polyethylene glycol with ClpB/DnaKJE bichaperone for refolding of heat-denatured malate dehydrogenase. Nian R, Kim DS, Tan L, Kim CW, Choe WS. Biotechnol Prog; 2009 Jun 25; 25(4):1078-85. PubMed ID: 19551876 [Abstract] [Full Text] [Related]
26. 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]
27. Structure and energetics of an allele-specific genetic interaction between dnaJ and dnaK: correlation of nuclear magnetic resonance chemical shift perturbations in the J-domain of Hsp40/DnaJ with binding affinity for the ATPase domain of Hsp70/DnaK. Landry SJ. Biochemistry; 2003 May 06; 42(17):4926-36. PubMed ID: 12718534 [Abstract] [Full Text] [Related]
28. The J-domain of Hsp40 couples ATP hydrolysis to substrate capture in Hsp70. Wittung-Stafshede P, Guidry J, Horne BE, Landry SJ. Biochemistry; 2003 May 06; 42(17):4937-44. PubMed ID: 12718535 [Abstract] [Full Text] [Related]
29. Role of Hsp70 (DnaK-DnaJ-GrpE) and Hsp100 (ClpA and ClpB) chaperones in refolding and increased thermal stability of bacterial luciferases in Escherichia coli cells. Zavilgelsky GB, Kotova VY, Mazhul' MM, Manukhov IV. Biochemistry (Mosc); 2002 Sep 06; 67(9):986-92. PubMed ID: 12387711 [Abstract] [Full Text] [Related]
30. 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]
31. DnaJ recruits DnaK to protein aggregates. Acebrón SP, Fernández-Sáiz V, Taneva SG, Moro F, Muga A. J Biol Chem; 2008 Jan 18; 283(3):1381-1390. PubMed ID: 17984091 [Abstract] [Full Text] [Related]
32. A chaperone network for the resolubilization of protein aggregates: direct interaction of ClpB and DnaK. Schlee S, Beinker P, Akhrymuk A, Reinstein J. J Mol Biol; 2004 Feb 06; 336(1):275-85. PubMed ID: 14741222 [Abstract] [Full Text] [Related]
33. Activation of the DnaK-ClpB Complex is Regulated by the Properties of the Bound Substrate. Fernández-Higuero JA, Aguado A, Perales-Calvo J, Moro F, Muga A. Sci Rep; 2018 Apr 11; 8(1):5796. PubMed ID: 29643454 [Abstract] [Full Text] [Related]
34. Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network. Goloubinoff P, Mogk A, Zvi AP, Tomoyasu T, Bukau B. Proc Natl Acad Sci U S A; 1999 Nov 23; 96(24):13732-7. PubMed ID: 10570141 [Abstract] [Full Text] [Related]
35. Role of the DnaK-ClpB bichaperone system in DNA gyrase reactivation during a severe heat-shock response in Escherichia coli. Lara-Ortíz T, Castro-Dorantes J, Ramírez-Santos J, Gómez-Eichelmann MC. Can J Microbiol; 2012 Feb 23; 58(2):195-9. PubMed ID: 22263929 [Abstract] [Full Text] [Related]
36. 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 Feb 23; 54(2):245-52. PubMed ID: 17565388 [Abstract] [Full Text] [Related]
37. Chaperone networks in protein disaggregation and prion propagation. Winkler J, Tyedmers J, Bukau B, Mogk A. J Struct Biol; 2012 Aug 23; 179(2):152-60. PubMed ID: 22580344 [Abstract] [Full Text] [Related]
38. Sequence-specific rates of interaction of target peptides with the molecular chaperones DnaK and DnaJ. Pierpaoli EV, Gisler SM, Christen P. Biochemistry; 1998 Nov 24; 37(47):16741-8. PubMed ID: 9843444 [Abstract] [Full Text] [Related]
39. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. Rüdiger S, Schneider-Mergener J, Bukau B. EMBO J; 2001 Mar 01; 20(5):1042-50. PubMed ID: 11230128 [Abstract] [Full Text] [Related]
40. The Hsp70 chaperone machines of Escherichia coli: a paradigm for the repartition of chaperone functions. Genevaux P, Georgopoulos C, Kelley WL. Mol Microbiol; 2007 Nov 01; 66(4):840-57. PubMed ID: 17919282 [Abstract] [Full Text] [Related] Page: [Previous] [Next] [New Search]