Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR - Wikidata - thesis-toulmin - TriplyDB

Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

http://www.wikidata.org/entity/Q27660397

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NMR Methods to Study Dynamic Allostery Solution Structure of the 128 kDa Enzyme I Dimer from Escherichia coli and Its 146 kDa Complex with HPr Using Residual Dipolar Couplings and Small- and Wide-Angle X-ray Scattering Fast methionine-based solution structure determination of calcium-calmodulin complexes Solution structure of a minor and transiently formed state of a T4 lysozyme mutant Structural Basis for Protein Antiaggregation Activity of the Trigger Factor Chaperone Facilitating unambiguous NMR assignments and enabling higher probe density through selective labeling of all methyl containing amino acids Disordered proteinaceous machines The future of the Protein Data Bank An allosteric conduit facilitates dynamic multisite substrate recognition by the SCF(Cdc4) ubiquitin ligase Signaling through dynamic linkers as revealed by PKA 13C NMR detects conformational change in the 100-kD membrane transporter ClC-ec1.NMR Backbone Assignment of Large Proteins by Using (13) Cα -Only Triple-Resonance Experiments.Understanding the mechanism of proteasome 20S core particle gating.Probing microsecond time scale dynamics in proteins by methyl (1)H Carr-Purcell-Meiboom-Gill relaxation dispersion NMR measurements. Application to activation of the signaling protein NtrC(r)Changes in conformational equilibria regulate the activity of the Dcp2 decapping enzyme.An NMR strategy for fragment-based ligand screening utilizing a paramagnetic lanthanide probe.FLAMEnGO: a fuzzy logic approach for methyl group assignment using NOESY and paramagnetic relaxation enhancement data.Structure-independent analysis of the breadth of the positional distribution of disordered groups in macromolecules from order parameters for long, variable-length vectors using NMR paramagnetic relaxation enhancement FLAMEnGO 2.0: an enhanced fuzzy logic algorithm for structure-based assignment of methyl group resonances.N-terminal domain of human Hsp90 triggers binding to the cochaperone p23.An introduction to NMR-based approaches for measuring protein dynamics.Flexible stoichiometry and asymmetry of the PIDDosome core complex by heteronuclear NMR spectroscopy and mass spectrometry.Dynamic fluctuations lubricate the circadian clock.Automated sequence- and stereo-specific assignment of methyl-labeled proteins by paramagnetic relaxation and methyl-methyl nuclear Overhauser enhancement spectroscopy.Proteasomes and protein conjugation across domains of life.Exposing the Moving Parts of Proteins with NMR Spectroscopy.The Structural Role of Antibody N-Glycosylation in Receptor Interactions CheA-receptor interaction sites in bacterial chemotaxis.Domain-domain interactions in full-length p53 and a specific DNA complex probed by methyl NMR spectroscopy.Complete determination of the Pin1 catalytic domain thermodynamic cycle by NMR lineshape analysis.The archaeal proteasome is regulated by a network of AAA ATPases Proteasome allostery as a population shift between interchanging conformers A dynamic look backward and forward.Protein-mediated antagonism between HIV reverse transcriptase ligands nevirapine and MgATP.Structural insights into proteasome activation by the 19S regulatory particle.Tracing an allosteric pathway regulating the activity of the HslV protease.Prokaryotic proteasomes: nanocompartments of degradation.Archaeal proteasomes and sampylation.A NMR experiment for simultaneous correlations of valine and leucine/isoleucine methyls with carbonyl chemical shifts in proteins.Proteasome activators.

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P2860

Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

http://www.wikidata.org/entity/Q27660397

description

2010 nî lūn-bûn

@nan

2010 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի ապրիլին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

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Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

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Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

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type

label

Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

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Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

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Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

@nl

prefLabel

Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

@ast

Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

@en

Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

@nl

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SCIENCE.1184991

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Dynamic regulation of archaeal proteasome gate opening as studied by TROSY NMR

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Remco Sprangers

http://www.w3.org/2001/XMLSchema#string

Tomasz L Religa

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P2860

Mechanism of gate opening in the 20S proteasome by the proteasomal ATPases

Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

Docking of the proteasomal ATPases' carboxyl termini in the 20S proteasome's alpha ring opens the gate for substrate entry

Structural basis for the activation of 20S proteasomes by 11S regulators

Interactions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome–ATPase interactions

Structural Basis for Signal-Sequence Recognition by the Translocase Motor SecA as Determined by NMR

Structural Models for Interactions between the 20S Proteasome and Its PAN/19S Activators

Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 A resolution

The Xplor-NIH NMR molecular structure determination package

The proteasome: paradigm of a self-compartmentalizing protease

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98-102

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scholarly article

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10.1126/SCIENCE.1184991

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5974

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328

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2010-04-02T00:00:00Z

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20360109

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