scholarly article | Q13442814 |
P2093 | author name string | D H Shin | |
A L Goldberg | |||
C H Chung | |||
M S Kang | |||
J H Seol | |||
S J Yoo | |||
Y K Shim | |||
P2860 | cites work | A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding | Q25938984 |
Endopeptidase Clp: ATP-dependent Clp protease from Escherichia coli | Q28306708 | ||
The ubiquitin-proteasome proteolytic pathway | Q29618638 | ||
Purification and characterization of the heat shock proteins HslV and HslU that form a new ATP-dependent protease in Escherichia coli | Q34384407 | ||
Sequence analysis of four new heat-shock genes constituting the hslTS/ibpAB and hslVU operons in Escherichia coli. | Q34728633 | ||
HslV-HslU: A novel ATP-dependent protease complex in Escherichia coli related to the eukaryotic proteasome | Q34733264 | ||
Six-fold rotational symmetry of ClpQ, the E. coli homolog of the 20S proteasome, and its ATP-dependent activator, ClpY. | Q34737150 | ||
ATP-dependent protease La (lon) from Escherichia coli. | Q54645667 | ||
P433 | issue | 3 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | Escherichia coli | Q25419 |
P304 | page(s) | 1143-1150 | |
P577 | publication date | 1997-08-01 | |
P1433 | published in | FEBS Journal | Q1388041 |
P1476 | title | The heat-shock protein HslVU from Escherichia coli is a protein-activated ATPase as well as an ATP-dependent proteinase | |
P478 | volume | 247 |
Q33788930 | A widespread family of serine/threonine protein phosphatases shares a common regulatory switch with proteasomal proteases. |
Q44283109 | ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation |
Q78144063 | ATP-dependent degradation of SulA, a cell division inhibitor, by the HslVU protease in Escherichia coli |
Q34418425 | Archaeal proteasomes: proteolytic nanocompartments of the cell |
Q42262524 | Asymmetric nucleotide transactions of the HslUV protease. |
Q37142807 | Binding of MG132 or deletion of the Thr active sites in HslV subunits increases the affinity of HslV protease for HslU ATPase and makes this interaction nucleotide-independent |
Q36476658 | Characterization of the HslU chaperone affinity for HslV protease |
Q44830501 | Communication between ClpX and ClpP during substrate processing and degradation |
Q27628834 | Crystal and solution structures of an HslUV protease-chaperone complex |
Q27639130 | Crystal structure of HslUV complexed with a vinyl sulfone inhibitor: corroboration of a proposed mechanism of allosteric activation of HslV by HslU |
Q54473734 | Defining the role of the Escherichia coli chaperone SecB using comparative proteomics. |
Q42460522 | Effects of the cys mutations on structure and function of the ATP-dependent HslVU protease in Escherichia coli. The Cys287 to Val mutation in HslU uncouples the ATP-dependent proteolysis by HslvU from ATP hydrolysis |
Q37446205 | HslVU ATP-dependent protease utilizes maximally six among twelve threonine active sites during proteolysis |
Q89820491 | Improvement of Thermotolerance of Zymomonas mobilis by Genes for Reactive Oxygen Species-Scavenging Enzymes and Heat Shock Proteins |
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Q27636245 | Nucleotide-dependent conformational changes in a protease-associated ATPase HsIU |
Q46453462 | Role of the GYVG pore motif of HslU ATPase in protein unfolding and translocation for degradation by HslV peptidase |
Q35904074 | Sculpting the proteome with AAA(+) proteases and disassembly machines. |
Q27678866 | Structural and Biochemical Analyses of the Eukaryotic Heat Shock Locus V (HslV) from Trypanosoma brucei |
Q27641494 | Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome |
Q27642327 | Structure of a Delivery Protein for an AAA+ Protease in Complex with a Peptide Degradation Tag |
Q39568209 | The 20S proteasome of Streptomyces coelicolor. |
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Q42554554 | The active ClpP protease from M. tuberculosis is a complex composed of a heptameric ClpP1 and a ClpP2 ring. |
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