Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly - Wikidata - awgldk - TriplyDB

Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly

Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly

http://www.wikidata.org/entity/Q27678263

about

Intracellular Dynamics of the Ubiquitin-Proteasome-System Nuclear Import of Yeast Proteasomes Reconfiguration of the proteasome during chaperone-mediated assembly 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain Molecular architecture and assembly of the eukaryotic proteasome Spg5 protein regulates the proteasome in quiescence.Hug1 is an intrinsically disordered protein that inhibits ribonucleotide reductase activity by directly binding Rnr2 subunit.Proteasome assembly Purification, crystallization and preliminary X-ray data collection of the N-terminal domain of the 26S proteasome regulatory subunit p27 and its complex with the ATPase domain of Rpt5 from Mus musculus Proteasome regulation by ADP-ribosylation Maturation of the proteasome core particle induces an affinity switch that controls regulatory particle association The ubiquitin-proteasome system of Saccharomyces cerevisiae.Conformational dynamics of the Rpt6 ATPase in proteasome assembly and Rpn14 binding.Phosphorylation of the C-terminal tail of proteasome subunit α7 is required for binding of the proteasome quality control factor Ecm29.The proteasome-associated protein Ecm29 inhibits proteasomal ATPase activity and in vivo protein degradation by the proteasome Structural insights into proteasome activation by the 19S regulatory particle.Structural biology of the proteasome.Structural disorder and its role in proteasomal degradation.A mass spectrometry-based hybrid method for structural modeling of protein complexes.Crystal structure of human proteasome assembly chaperone PAC4 involved in proteasome formation.Proteasome Structure and Assembly.Proteasome Activation is Mediated via a Functional Switch of the Rpt6 C-terminal Tail Following Chaperone-dependent Assembly.Nucleotide-dependent switch in proteasome assembly mediated by the Nas6 chaperone A multiscale coarse-grained polarizable solvent model for handling long tail bulk electrostatics.Structural insights on the dynamics of proteasome formation.A Simple Light Isotope Metabolic Labeling (SLIM-labeling) Strategy: A Powerful Tool to Address the Dynamics of Proteome Variations In Vivo.PSMD5 inactivation promotes 26S proteasome assembly during colorectal tumor progression.

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P2860

Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly

http://www.wikidata.org/entity/Q27678263

description

2012 nî lūn-bûn

@nan

2012 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի ապրիլին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Dual functions of the Hsm3 pro ...... during the proteasome assembly

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Dual functions of the Hsm3 pro ...... during the proteasome assembly

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Dual functions of the Hsm3 pro ...... during the proteasome assembly

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type

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Dual functions of the Hsm3 pro ...... during the proteasome assembly

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Dual functions of the Hsm3 pro ...... during the proteasome assembly

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Dual functions of the Hsm3 pro ...... during the proteasome assembly

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prefLabel

Dual functions of the Hsm3 pro ...... during the proteasome assembly

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Dual functions of the Hsm3 pro ...... during the proteasome assembly

@en

Dual functions of the Hsm3 pro ...... during the proteasome assembly

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PNAS.1116538109

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Proceedings of the National Academy of Sciences of the United States of America

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Dual functions of the Hsm3 pro ...... during the proteasome assembly

@en

P2093

Anne Peyroche

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

Brice Murciano

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Chloe Godard

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Erwann Rousseau

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Françoise Ochsenbein

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Marie-Bénédicte Barrault

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Marie-Hélène Le Du

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Nicolas Richet

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

Raphaël Guérois

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

P2860

Assembly pathway of the Mammalian proteasome base subcomplex is mediated by multiple specific chaperones

Chaperone-mediated pathway of proteasome regulatory particle assembly

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

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

Structure of the oncoprotein gankyrin in complex with S6 ATPase of the 26S proteasome

Structural basis for the recognition between the regulatory particles Nas6 and Rpt3 of the yeast 26S proteasome

Structure and activity of the N-terminal substrate recognition domains in proteasomal ATPases

Structural Insights into the Regulatory Particle of the Proteasome from Methanocaldococcus jannaschii

The crystal structure of apo-FtsH reveals domain movements necessary for substrate unfolding and translocation.

Structural Basis for Specific Recognition of Rpt1p, an ATPase Subunit of 26 S Proteasome, by Proteasome-dedicated Chaperone Hsm3p

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E1001-10

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scholarly article

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762085

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10.1073/PNAS.1116538109

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P433

17

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109

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Jean-Baptiste Charbonnier

Benoît Le Tallec

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2012-03-29T00:00:00Z

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223989574

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22460800

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molecular chaperones

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3340050

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