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Crystal and solution structures of an HslUV protease-chaperone complex
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scholarly article
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title
Crystal and solution structures of an HslUV protease-chaperone complex
(English)
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main subject
molecular chaperones
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author name string
M C Sousa
series ordinal
1
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C B Trame
series ordinal
2
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H Tsuruta
series ordinal
3
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S M Wilbanks
series ordinal
4
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V S Reddy
series ordinal
5
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D B McKay
series ordinal
6
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language of work or name
English
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publication date
10 November 2000
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published in
Cell
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volume
103
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issue
4
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page(s)
633-43
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cites work
The Pfam protein families database.
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Crystal structure of heat shock locus V (HslV) from Escherichia coli
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The structures of HsIU and the ATP-dependent protease HsIU-HsIV
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Covalent modification of the active site threonine of proteasomal beta subunits and the Escherichia coli homolog HslV by a new class of inhibitors
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Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination
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Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli.
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An extensively modified version of MolScript that includes greatly enhanced coloring capabilities
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Further additions to MolScript version 1.4, including reading and contouring of electron-density maps
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The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
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Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP.
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Proteolytic activity of the ATP-dependent protease HslVU can be uncoupled from ATP hydrolysis
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A graphics model building and refinement system for macromolecules
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The ATP-dependent HslVU/ClpQY protease participates in turnover of cell division inhibitor SulA in Escherichia coli
1 reference
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Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
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Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY.
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Dynamics of substrate denaturation and translocation by the ClpXP degradation machine
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Not your average density.
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A common set of conserved motifs in a vast variety of putative nucleic acid-dependent ATPases including MCM proteins involved in the initiation of eukaryotic DNA replication
1 reference
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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
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Crystal structure of the hexamerization domain of N-ethylmaleimide-sensitive fusion protein
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Disassembly of the Mu transposase tetramer by the ClpX chaperone
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Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution
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Raster3D: photorealistic molecular graphics
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Identification and characterization of HsIV HsIU (ClpQ ClpY) proteins involved in overall proteolysis of misfolded proteins in Escherichia coli.
1 reference
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HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome
1 reference
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The ATP-dependent HslVU protease from Escherichia coli is a four-ring structure resembling the proteasome.
1 reference
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HSP100/Clp proteins: a common mechanism explains diverse functions
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Proteasome from Thermoplasma acidophilum: a threonine protease
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The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2900166-5
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inferred from DOI database lookup
ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli
1 reference
stated in
Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2900166-5
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7 January 2021
based on heuristic
inferred from DOI database lookup
Unfolding and internalization of proteins by the ATP-dependent proteases ClpXP and ClpAP.
1 reference
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Crossref
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1 reference
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Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.
1 reference
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Solution small-angle X-ray scattering study of the molecular chaperone Hsc70 and its subfragments
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Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli
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ATP binding, but not its hydrolysis, is required for assembly and proteolytic activity of the HslVU protease in Escherichia coli
1 reference
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Crossref
reference URL
https://api.crossref.org/works/10.1016%2FS0092-8674%2800%2900166-5
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Structure of the ATP-dependent oligomerization domain of N-ethylmaleimide sensitive factor complexed with ATP
1 reference
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Distantly related sequences in the alpha- and beta-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
1 reference
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Identifiers
DOI
10.1016/S0092-8674(00)00166-5
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PubMed publication ID
11106733
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ResearchGate publication ID
12220850
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