scholarly article | Q13442814 |
P819 | ADS bibcode | 2014PNAS..111.2140S |
P356 | DOI | 10.1073/PNAS.1318476111 |
P932 | PMC publication ID | 3926032 |
P698 | PubMed publication ID | 24469799 |
P50 | author | Lewis E. Kay | Q29046014 |
P2093 | author name string | Lichi Shi | |
P2860 | cites work | Structure and functions of the 20S and 26S proteasomes | Q24328777 |
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Crystal structures of the HslVU peptidase-ATPase complex reveal an ATP-dependent proteolysis mechanism | Q27630654 | ||
Structure and reactivity of an asymmetric complex between HslV and I-domain deleted HslU, a prokaryotic homolog of the eukaryotic proteasome | Q27641494 | ||
Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR | Q27649095 | ||
Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR | Q27660397 | ||
Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution | Q27730197 | ||
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The proteasome | Q33689946 | ||
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Nuclear magnetic resonance methods for quantifying microsecond-to-millisecond motions in biological macromolecules | Q34313182 | ||
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Proteasome allostery as a population shift between interchanging conformers | Q36483667 | ||
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 | Q37142807 | ||
Catalytic mechanism and assembly of the proteasome. | Q37407654 | ||
Methyl groups as probes of supra-molecular structure, dynamics and function | Q37604187 | ||
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Stereospecific isotopic labeling of methyl groups for NMR spectroscopic studies of high-molecular-weight proteins | Q43161110 | ||
Cross-correlated relaxation enhanced 1H[bond]13C NMR spectroscopy of methyl groups in very high molecular weight proteins and protein complexes | Q44554807 | ||
Stability of the proteasome can be regulated allosterically through engagement of its proteolytic active sites. | Q46891027 | ||
Probing slow dynamics in high molecular weight proteins by methyl-TROSY NMR spectroscopy: application to a 723-residue enzyme | Q47425115 | ||
Autocatalytic processing of the 20S proteasome | Q47853840 | ||
Kinetics of protein substrate degradation by HslUV. | Q47904876 | ||
An optimized relaxation-based coherence transfer NMR experiment for the measurement of side-chain order in methyl-protonated, highly deuterated proteins. | Q53400167 | ||
Quantitative dynamics and binding studies of the 20S proteasome by NMR | Q59082478 | ||
Solution NMR of supramolecular complexes: providing new insights into function | Q80972816 | ||
13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamics | Q84711439 | ||
Dissecting electrostatic interactions in Bacillus circulans xylanase through NMR-monitored pH titrations | Q84987655 | ||
Measurement of active site ionization equilibria in the 670 kDa proteasome core particle using methyl-TROSY NMR | Q87001349 | ||
P433 | issue | 6 | |
P407 | language of work or name | English | Q1860 |
P304 | page(s) | 2140-2145 | |
P577 | publication date | 2014-01-27 | |
P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
P1476 | title | Tracing an allosteric pathway regulating the activity of the HslV protease | |
P478 | volume | 111 |
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