Structural characterization of the interaction of Ubp6 with the 26S proteasome. - Wikidata - awgldk - TriplyDB

Structural characterization of the interaction of Ubp6 with the 26S proteasome.

Structural characterization of the interaction of Ubp6 with the 26S proteasome.

http://www.wikidata.org/entity/Q35865605

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The life cycle of the 26S proteasome: from birth, through regulation and function, and onto its death An atomic structure of the human 26S proteasome Phosphatase UBLCP1 controls proteasome assembly Phosphorylation of the 19S regulatory particle ATPase subunit, Rpt6, modifies susceptibility to proteotoxic stress and protein aggregation.Gates, Channels, and Switches: Elements of the Proteasome Machine Rpn1 provides adjacent receptor sites for substrate binding and deubiquitination by the proteasome Ubp6 deubiquitinase controls conformational dynamics and substrate degradation of the 26S proteasome.Substrate Ubiquitination Controls the Unfolding Ability of the Proteasome.Structure of an endogenous yeast 26S proteasome reveals two major conformational states USP14 deubiquitinates proteasome-bound substrates that are ubiquitinated at multiple sites.Ubiquitin-like domains can target to the proteasome but proteolysis requires a disordered region.Characterization of Dynamic UbR-Proteasome Subcomplexes by In vivo Cross-linking (X) Assisted Bimolecular Tandem Affinity Purification (XBAP) and Label-free Quantitation.Structure of the human 26S proteasome at a resolution of 3.9 Å.Structural insights into the functional cycle of the ATPase module of the 26S proteasome.Structural disorder and its role in proteasomal degradation.Polyubiquitin-Photoactivatable Crosslinking Reagents for Mapping Ubiquitin Interactome Identify Rpn1 as a Proteasome Ubiquitin-Associating Subunit.Proteasome dynamics between proliferation and quiescence stages of Saccharomyces cerevisiae.Ubiquitin recognition by the proteasome.The Logic of the 26S Proteasome.Proteasome Structure and Assembly.Protein Degradation Systems as Antimalarial Therapeutic Targets.Rad7 E3 Ubiquitin Ligase Attenuates Polyubiquitylation of Rpn10 and Dsk2 Following DNA Damage in Saccharomyces cerevisiae.The deubiquitinating enzyme Usp14 allosterically inhibits multiple proteasomal activities and ubiquitin-independent proteolysis.Ubiquitinated proteins promote the association of proteasomes with the deubiquitinating enzyme Usp14 and the ubiquitin ligase Ube3c.Molecular Details Underlying Dynamic Structures and Regulation of the Human 26S Proteasome.Cross-Linking Mass Spectrometry: An Emerging Technology for Interactomics and Structural Biology.Meddling with Fate: The Proteasomal Deubiquitinating Enzymes.Impairment of protein degradation and proteasome function in hereditary neuropathies.In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.Structure and energetics of pairwise interactions between proteasome subunits RPN2, RPN13, and ubiquitin clarify a substrate recruitment mechanism.TRIM11 activates the proteasome and promotes overall protein degradation by regulating USP14.Conformational switching in the coiled-coil domains of a proteasomal ATPase regulates substrate processing.

P2860

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P2860

Structural characterization of the interaction of Ubp6 with the 26S proteasome.

http://www.wikidata.org/entity/Q35865605

description

2015 nî lūn-bûn

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2015年の論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年論文

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2015年论文

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2015年论文

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2015年论文

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name

Structural characterization of the interaction of Ubp6 with the 26S proteasome.

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Structural characterization of the interaction of Ubp6 with the 26S proteasome.

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type

label

Structural characterization of the interaction of Ubp6 with the 26S proteasome.

@ast

Structural characterization of the interaction of Ubp6 with the 26S proteasome.

@en

prefLabel

Structural characterization of the interaction of Ubp6 with the 26S proteasome.

@ast

Structural characterization of the interaction of Ubp6 with the 26S proteasome.

@en

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PNAS.1510449112

P1433

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

P1476

Structural characterization of the interaction of Ubp6 with the 26S proteasome.

@en

P2093

Alfred L Goldberg

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

Andreas Schweitzer

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

Antje Aufderheide

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

Eri Sakata

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

Florian Beck

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

Friedrich Förster

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Günter Pfeifer

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Michaela Hartwig

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

Wolfgang Baumeister

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P2860

Structure and mechanisms of the proteasome-associated deubiquitinating enzyme USP14

Deep classification of a large cryo-EM dataset defines the conformational landscape of the 26S proteasome

Crystal structure of the proteasomal deubiquitylation module Rpn8-Rpn11

Structure of the Rpn11-Rpn8 dimer reveals mechanisms of substrate deubiquitination during proteasomal degradation

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

Structure of 20S proteasome from yeast at 2.4 A resolution

The ubiquitin system

Proteasome subunit Rpn1 binds ubiquitin-like protein domains.

Multiple associated proteins regulate proteasome structure and function.

Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes

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8626-8631

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10.1073/PNAS.1510449112

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28

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112

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Florian Stengel

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2015-06-30T00:00:00Z

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26130806

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