Crossref
journal-article
Elsevier BV
Molecular Cell (78)
References
56
Referenced
112
10.1110/ps.03422604
/ Protein Sci. / Nucleotide-induced switch in oligomerization of the AAA+ ATPase ClpB by Akoev (2004){'key': '10.1016/j.molcel.2007.01.002_bib2', 'first-page': '905', 'article-title': 'Crystallography & NMR system: a new software suite for macromolecular structure determination', 'volume': 'D54', 'author': 'Brünger', 'year': '1998', 'journal-title': 'Acta Crystallogr.'}
/ Acta Crystallogr. / Crystallography & NMR system: a new software suite for macromolecular structure determination by Brünger (1998)10.1016/S0969-2126(03)00128-X
/ Structure / Organic solvents order the dynamic switch II in Ras crystals by Buhrman (2003)10.1016/j.cell.2006.04.014
/ Cell / Molecular chaperones and protein quality control by Bukau (2006)10.1038/nsmb898
/ Nat. Struct. Mol. Biol. / Nucleotide-dependent substrate recognition by the AAA+ HslUV protease by Burton (2005)10.1016/S1097-2765(02)00499-9
/ Mol. Cell / Defining a pathway of communication from the C-terminal peptide binding domain to the N-terminal ATPase domain in a AAA protein by Cashikar (2002)10.1038/nsb972
/ Nat. Struct. Biol. / Complete structure of p97/valosin-containing protein reveals communication between nucleotide domains by DeLaBarre (2003)10.1016/j.jmb.2005.01.060
/ J. Mol. Biol. / Nucleotide dependent motion and mechanism of action of p97/VCP by DeLaBarre (2005)10.1016/S0092-8674(00)81223-4
/ Cell / Hsp104, Hsp70, and Hsp40: a novel chaperone system that rescues previously aggregated proteins by Glover (1998)10.1073/pnas.96.24.13732
/ Proc. Natl. Acad. Sci. USA / Sequential mechanism of solubilization and refolding of stable protein aggregates by a bichaperone network by Goloubinoff (1999)10.1074/jbc.M207796200
/ J. Biol. Chem. / Crystal structure of ClpA, an HSP100 chaperone and regulator of ClpAP protease by Guo (2002)10.1038/nrm1684
/ Nat. Rev. Mol. Cell Biol. / AAA+ proteins: have engine, will work by Hanson (2005)10.1016/j.molcel.2006.11.008
/ Mol. Cell / M domains couple the ClpB threading motor with the DnaK chaperone activity by Haslberger (2007)10.1016/j.cell.2005.04.012
/ Cell / Loops in the central channel of ClpA chaperone mediate protein binding, unfolding, and translocation by Hinnerwisch (2005)10.1074/jbc.272.34.21364
/ J. Biol. Chem. / Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis by Huang (1997)10.1016/j.jsb.2003.10.007
/ J. Struct. Biol. / The crystal structure of murine p97/VCP at 3.6Å by Huyton (2003)10.1073/pnas.081543698
/ Proc. Natl. Acad. Sci. USA / Translocation pathway of protein substrates in ClpAP protease by Ishikawa (2001)10.1016/j.jsb.2003.11.018
/ J. Struct. Biol. / The N-terminal substrate-binding domain of ClpA unfoldase is highly mobile and extends axially from the distal surface of ClpAP protease by Ishikawa (2004)10.1006/jmbi.2001.4633
/ J. Mol. Biol. / Bridging the information gap: computational tools for intermediate resolution structure interpretation by Jiang (2001)10.1107/S0108767390010224
/ Acta Crystallogr. / Improved methods for binding protein models in electron density maps and the location of errors in these models by Jones (1991)10.1021/bi035573d
/ Biochem. / Structure and function of the middle domain of ClpB from Escherichia coli by Kedzierska (2003)10.1074/jbc.M107580200
/ J. Biol. Chem. / Cooperative action of Escherichia coli ClpB protein and DnaK chaperone in the activation of a replication initiation protein by Konieczny (2002){'key': '10.1016/j.molcel.2007.01.002_bib23', 'first-page': '761', 'article-title': 'Simulated-annealing real-space refinement as a tool in model building', 'volume': 'D58', 'author': 'Korostelev', 'year': '2002', 'journal-title': 'Acta Crystallogr.'}
/ Acta Crystallogr. / Simulated-annealing real-space refinement as a tool in model building by Korostelev (2002)10.1016/S0092-8674(03)00807-9
/ Cell / The structure of ClpB: a molecular chaperone that rescues proteins from an aggregated state by Lee (2003)10.1006/jsbi.1999.4174
/ J. Struct. Biol. / EMAN: semiautomated software for high-resolution single-particle reconstructions by Ludtke (1999)10.1016/j.str.2004.05.006
/ Structure / Seeing GroEL at 6 Å resolution by single-particle electron cryomicroscopy by Ludtke (2004)10.1074/jbc.M403777200
/ J. Biol. Chem. / Evidence for an unfolding/threading mechanism for protein disaggregation by Saccharomyces cerevisiae Hsp104 by Lum (2004)10.1042/bst0190719
/ Biochem. Soc. Trans. / ATP-promoted interaction between ClpA and ClpP in activation of Clp protease from Escherichia coli by Maurizi (1991)10.1016/j.str.2004.01.021
/ Structure / Protein binding and disruption by Clp/Hsp100 chaperones by Maurizi (2004)10.1093/emboj/18.24.6934
/ EMBO J. / Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB by Mogk (1999)10.1074/jbc.M209686200
/ J. Biol. Chem. / Roles of individual domains and conserved motifs of the AAA+ chaperone ClpB in oligomerization, ATP hydrolysis, and chaperone activity by Mogk (2003)10.1073/pnas.96.13.7184
/ Proc. Natl. Acad. Sci. USA / Heat-inactivated proteins are rescued by the DnaK.J-GrpE set and ClpB chaperones by Motohashi (1999)10.1101/gr.9.1.27
/ Genome Res. / AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes by Neuwald (1999)10.1046/j.1365-2443.2001.00447.x
/ Genes Cells / AAA+ superfamily ATPases: common structure-diverse function by Ogura (2001)10.1074/jbc.M411733200
/ J. Biol. Chem. / The molecular chaperone, ClpA, has a single high affinity peptide binding site per hexamer by Piszczek (2005)10.1105/tpc.12.4.479
/ Plant Cell / Heat shock protein 101 plays a crucial role in thermotolerance in Arabidopsis by Queitsch (2000)10.1126/science.2188365
/ Science / Hsp104 required for induced thermotolerance by Sanchez (1990)10.1016/j.cell.2004.09.020
/ Cell / Sculpting the proteome with AAA(+) proteases and disassembly machines by Sauer (2004)10.1016/j.febslet.2004.11.051
/ FEBS Lett. / Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides by Schlieker (2004)10.1038/nsmb787
/ Nat. Struct. Mol. Biol. / Substrate recognition by the AAA+ chaperone ClpB by Schlieker (2004)10.1126/science.1098007
/ Science / Hsp104 catalyzes formation and elimination of self-replicating Sup35 prion conformers by Shorter (2004)10.1016/j.molcel.2006.05.042
/ Mol. Cell / Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities by Shorter (2006)10.1128/jb.173.14.4254-4262.1991
/ J. Bacteriol. / ClpB is the Escherichia coli heat shock protein F84.1 by Squires (1991)10.1110/ps.4860102
/ Protein Sci. / Stability and interactions of the amino-terminal domain of ClpB from Escherichia coli by Tek (2002)10.1016/S0021-9258(17)32435-3
/ J. Biol. Chem. / Activity and specificity of Escherichia coli ClpAP protease in cleaving model peptide substrates by Thompson (1994)10.1016/j.jsb.2004.07.003
/ J. Struct. Biol. / Nucleotide-dependent domain motions within rings of the RecA/AAA(+) superfamily by Wang (2004)10.1074/jbc.M414623200
/ J. Biol. Chem. / ATP binding to nucleotide binding domain (NBD)1 of the ClpB chaperone induces motion of the long coiled-coil, stabilizes the hexamer, and activates NBD2 by Watanabe (2005)10.1074/jbc.M109349200
/ J. Biol. Chem. / Roles of the two ATP binding sites of ClpB from Thermus thermophilus by Watanabe (2002)10.1074/jbc.M303653200
/ J. Biol. Chem. / Characterization of a trap mutant of the AAA+ chaperone ClpB by Weibezahn (2003)10.1016/j.cell.2004.11.027
/ Cell / Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB by Weibezahn (2004)10.1016/j.bbabio.2004.06.003
/ Biochim. Biophys. Acta / RecA-like motor ATPases-lessons from structures by Ye (2004)10.1021/bi00626a027
/ Biochem. / Crystallographic studies of protein denaturation and renaturation. 1. Effects of denaturants on volume and X-ray pattern of cross-linked triclinic lysozyme crystals by Yonath (1977)10.1074/jbc.M402405200
/ J. Biol. Chem. / Successive and synergistic action of the Hsp70 and Hsp100 chaperones in protein disaggregation by Zietkiewicz (2004)10.1074/jbc.M507893200
/ J. Biol. Chem. / Hsp70 chaperone machine remodels protein aggregates at the initial step of Hsp70-Hsp100-dependent disaggregation by Zietkiewicz (2006)10.1074/jbc.274.40.28083
/ J. Biol. Chem. / ClpB cooperates with DnaK, DnaJ, and GrpE in suppressing protein aggregation by Zolkiewski (1999)10.1110/ps.8.9.1899
/ Protein Sci. / Nucleotide-dependent oligomerization of ClpB from Escherichia coli by Zolkiewski (1999)
Dates
Type | When |
---|---|
Created | 18 years, 7 months ago (Jan. 26, 2007, 12:45 p.m.) |
Deposited | 1 year, 3 months ago (May 11, 2024, 3:10 a.m.) |
Indexed | 1 day, 12 hours ago (Aug. 30, 2025, 1:12 p.m.) |
Issued | 18 years, 8 months ago (Jan. 1, 2007) |
Published | 18 years, 8 months ago (Jan. 1, 2007) |
Published Print | 18 years, 8 months ago (Jan. 1, 2007) |
@article{Lee_2007, title={Visualizing the ATPase Cycle in a Protein Disaggregating Machine: Structural Basis for Substrate Binding by ClpB}, volume={25}, ISSN={1097-2765}, url={http://dx.doi.org/10.1016/j.molcel.2007.01.002}, DOI={10.1016/j.molcel.2007.01.002}, number={2}, journal={Molecular Cell}, publisher={Elsevier BV}, author={Lee, Sukyeong and Choi, Jae-Mun and Tsai, Francis T.F.}, year={2007}, month=jan, pages={261–271} }