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Journal Abstract Search
208 related items for PubMed ID: 15351650
1. Crystal structure of the molecular chaperone HscA substrate binding domain complexed with the IscU recognition peptide ELPPVKIHC. Cupp-Vickery JR, Peterson JC, Ta DT, Vickery LE. J Mol Biol; 2004 Sep 24; 342(4):1265-78. PubMed ID: 15351650 [Abstract] [Full Text] [Related]
3. Studies on the mechanism of catalysis of iron-sulfur cluster transfer from IscU[2Fe2S] by HscA/HscB chaperones. Bonomi F, Iametti S, Morleo A, Ta D, Vickery LE. Biochemistry; 2008 Dec 02; 47(48):12795-801. PubMed ID: 18986169 [Abstract] [Full Text] [Related]
4. Sequence-dependent peptide binding orientation by the molecular chaperone DnaK. Tapley TL, Cupp-Vickery JR, Vickery LE. Biochemistry; 2005 Sep 20; 44(37):12307-15. PubMed ID: 16156644 [Abstract] [Full Text] [Related]
5. Facilitated transfer of IscU-[2Fe2S] clusters by chaperone-mediated ligand exchange. Bonomi F, Iametti S, Morleo A, Ta D, Vickery LE. Biochemistry; 2011 Nov 08; 50(44):9641-50. PubMed ID: 21977977 [Abstract] [Full Text] [Related]
6. Molecular chaperones HscA/Ssq1 and HscB/Jac1 and their roles in iron-sulfur protein maturation. Vickery LE, Cupp-Vickery JR. Crit Rev Biochem Mol Biol; 2007 Nov 08; 42(2):95-111. PubMed ID: 17453917 [Abstract] [Full Text] [Related]
7. The SufE sulfur-acceptor protein contains a conserved core structure that mediates interdomain interactions in a variety of redox protein complexes. Goldsmith-Fischman S, Kuzin A, Edstrom WC, Benach J, Shastry R, Xiao R, Acton TB, Honig B, Montelione GT, Hunt JF. J Mol Biol; 2004 Nov 19; 344(2):549-65. PubMed ID: 15522304 [Abstract] [Full Text] [Related]
8. Preferential substrate binding orientation by the molecular chaperone HscA. Tapley TL, Vickery LE. J Biol Chem; 2004 Jul 02; 279(27):28435-42. PubMed ID: 15100228 [Abstract] [Full Text] [Related]
9. 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]
10. Importance of the D and E helices of the molecular chaperone DnaK for ATP binding and substrate release. Slepenkov SV, Patchen B, Peterson KM, Witt SN. Biochemistry; 2003 May 20; 42(19):5867-76. PubMed ID: 12741845 [Abstract] [Full Text] [Related]
11. Contributions of the LPPVK motif of the iron-sulfur template protein IscU to interactions with the Hsc66-Hsc20 chaperone system. Hoff KG, Cupp-Vickery JR, Vickery LE. J Biol Chem; 2003 Sep 26; 278(39):37582-9. PubMed ID: 12871959 [Abstract] [Full Text] [Related]
12. Crystal structure of IscA, an iron-sulfur cluster assembly protein from Escherichia coli. Cupp-Vickery JR, Silberg JJ, Ta DT, Vickery LE. J Mol Biol; 2004 Apr 16; 338(1):127-37. PubMed ID: 15050828 [Abstract] [Full Text] [Related]
13. Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments. Cai S, Stevens SY, Budor AP, Zuiderweg ER. Biochemistry; 2003 Sep 30; 42(38):11100-8. PubMed ID: 14503860 [Abstract] [Full Text] [Related]
14. Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones. Kityk R, Kopp J, Sinning I, Mayer MP. Mol Cell; 2012 Dec 28; 48(6):863-74. PubMed ID: 23123194 [Abstract] [Full Text] [Related]
15. Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch. Rüdiger S, Mayer MP, Schneider-Mergener J, Bukau B. J Mol Biol; 2000 Dec 01; 304(3):245-51. PubMed ID: 11090270 [Abstract] [Full Text] [Related]
16. A novel virus-like particle based on hepatitis B core antigen and substrate-binding domain of bacterial molecular chaperone DnaK. Wang XJ, Gu K, Xiong QY, Shen L, Cao RY, Li MH, Li TM, Wu J, Liu JJ. Vaccine; 2009 Dec 09; 27(52):7377-84. PubMed ID: 19778518 [Abstract] [Full Text] [Related]
17. NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction. Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER. Biochemistry; 1998 Jun 02; 37(22):7929-40. PubMed ID: 9609686 [Abstract] [Full Text] [Related]