SFX by Ex Libris Inc.

Title:	Structural analysis of substrate binding by the molecular chaperone DnaK
Source:	Science [0036-8075] Zhu, X yr:1996

Basic

Sorry, no full text available...

Please use the document delivery service (see below)

Holding information

Holdings in library search engine ALBERT

Document delivery

Request document via Library/Bibliothek

Users interested in this article also expressed an interest in the following:
description	1.	Harrison, J. "Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK." Science 276.5311 (1997): 431-435.
description	2.	Zuiderweg, E. "Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate." Proceedings of the National Academy of Sciences of the United States of America 106.21 (2009): 8471-8476.
description	3.	BECKMANN, R. "INTERACTION OF HSP-70 WITH NEWLY SYNTHESIZED PROTEINS - IMPLICATIONS FOR PROTEIN FOLDING AND ASSEMBLY." Science 248.4957 (1990): 850-854.
description	4.	Joachimiak, R. "Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain." Structure 5.3 (1997): 403-14.
description	5.	Siegers, Jason C R. "Pathways of chaperone-mediated protein folding in the cytosol." Nature reviews. Molecular cell biology 5.10: 781-791.
description	6.	Bhattacharya, A. "Allostery in Hsp70 Chaperones Is Transduced by Subdomain Rotations." Journal of molecular biology 388.3 (2009): 475-490.
description	7.	Kabani, M. "Structural and functional diversity among eukaryotic Hsp70 nucleotide exchange factors." Protein & peptide letters 16.6 (2009): 623-60.
description	8.	Wu, B. "Structure-function analysis of the Escherichia coli GrpE heat shock protein." EMBO Journal 15.18 (1996): 4806-4816.
description	9.	Sajid, M. "Conformationally Unambiguous Spin Labeling for Distance Measurements." Chemistry : a European journal 15.47 (2009): 12960-12962.
description	10.	Borges, J. "Characterization of nucleotide-induced changes on the quaternary structure of human 70 kDa heat shock protein Hsp70.1 by analytical ultracentrifugation." Biochemistry and Molecurar Biology Reports 42.3 (2009): 166-171.
description	11.	Flaherty, K. "Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein." Nature 346.6285 (1990): 623-628.
description	12.	Vogel, M. "Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker." The Journal of biological chemistry 281.50 (2006): 38705-38711.
description	13.	Johnson, M. "Probing the Phosphopantetheine Arm Conformations of Acyl Carrier Proteins Using Vibrational Spectroscopy." Journal of the American Chemical Society 136.32 (2014): 4294967295-11243.
description	14.	Fei, X. "Crystal structure of a GroEL-ADP complex in the relaxed allosteric state at 2.7 A resolution." Proceedings of the National Academy of Sciences of the United States of America 110.32 (2013): -66.
description	15.	Padfield, Andrew S. "A novel, small molecule inhibitor of Hsc70/Hsp70 potentiates Hsp90 inhibitor induced apoptosis in HCT116 colon carcinoma cells." Cancer Chemotherapy and Pharmacology 66.3 (2009): 535-545.
description	16.	Zhao, X. "Mutations in the C-terminal fragment of DnaK affecting peptide binding." Proceedings of the National Academy of Sciences of the United States of America 93.20 (1996): 10632-10637.
description	17.	Wu, X. "The second metal-binding site of 70 kDa heat-shock protein is essential for ADP binding, ATP hydrolysis and ATP synthesis." The Biochemical journal 378.Pt 3 (2004): 793-799.
description	18.	Witt, Stephan N. "The Fink blueprint for Hsp70/Hsc70 molecular chaperones." Current protein & peptide science 10.5 (2009): 424-431.
description	19.	Sander, A. "An ATPase domain common to prokaryotic cell cycle proteins, sugar kinases, actin, and hsp70 heat shock proteins." Proceedings of the National Academy of Sciences of the United States of America 89.16 (1992): 7290-4.
description	20.	FREEMAN, B C C. "IDENTIFICATION OF A REGULATORY MOTIF IN HSP70 THAT AFFECTS ATPASE ACTIVITY, SUBSTRATE-BINDING AND INTERACTION WITH HDJ-1." The EMBO journal 14.10 (1995): 2281-2292.