Structural basis for dynamic regulation of the human 26S proteasome. - Wikidata - wikimedia - TriplyDB

Structural basis for dynamic regulation of the human 26S proteasome.

Structural basis for dynamic regulation of the human 26S proteasome.

http://www.wikidata.org/entity/Q37469477

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Long-range allosteric regulation of the human 26S proteasome by 20S proteasome-targeting cancer drugs.A deep convolutional neural network approach to single-particle recognition in cryo-electron microscopy Gyre and gimble in the proteasome.Structural insights into the functional cycle of the ATPase module of the 26S proteasome.Reversible phosphorylation of the 26S proteasome.Massively parallel unsupervised single-particle cryo-EM data clustering via statistical manifold learning.High-resolution cryo-EM structure of the proteasome in complex with ADP-AlFx.Monoubiquitination joins polyubiquitination as an esteemed proteasomal targeting signal.The Logic of the 26S Proteasome.Proteasome Structure and Assembly.AAA-ATPases in Protein Degradation.Mycobacterium tuberculosis proteasomal ATPase Mpa has a β-grasp domain that hinders docking with the proteasome core protease.Conformational Landscape of the p28-Bound Human Proteasome Regulatory Particle.Structure of a AAA+ unfoldase in the process of unfolding substrate.Identifying direct contacts between protein complex subunits from their conditional dependence in proteomics datasets.Electrostatic Map Of Proteasome α-Rings Encodes The Design of Allosteric Porphyrin-Based Inhibitors Able To Affect 20S Conformation By Cooperative Binding.Small Molecule Enhancement of 20S Proteasome Activity Targets Intrinsically Disordered Proteins.Meddling with Fate: The Proteasomal Deubiquitinating Enzymes.Structural characterization of the bacterial proteasome homolog BPH reveals a tetradecameric double-ring complex with unique inner cavity properties.Probing the cooperativity of Thermoplasma acidophilum proteasome core particle gating by NMR spectroscopy.In Situ Structure of Neuronal C9orf72 Poly-GA Aggregates Reveals Proteasome Recruitment.Inhibition of the proteasome activity by graphene oxide contributes to its cytotoxicity.Structural mechanism for nucleotide-driven remodeling of the AAA-ATPase unfoldase in the activated human 26S proteasome.Conformational switching in the coiled-coil domains of a proteasomal ATPase regulates substrate processing.Structure of the Cdc48 ATPase with its ubiquitin-binding cofactor Ufd1-Npl4

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Structural basis for dynamic regulation of the human 26S proteasome.

http://www.wikidata.org/entity/Q37469477

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on 21 October 2016

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Structural basis for dynamic regulation of the human 26S proteasome.

@en

Structural basis for dynamic regulation of the human 26S proteasome.

@nl

type

label

Structural basis for dynamic regulation of the human 26S proteasome.

@en

Structural basis for dynamic regulation of the human 26S proteasome.

@nl

prefLabel

Structural basis for dynamic regulation of the human 26S proteasome.

@en

Structural basis for dynamic regulation of the human 26S proteasome.

@nl

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PNAS.1614614113

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

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Structural basis for dynamic regulation of the human 26S proteasome.

@en

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Byung-Hoon Lee

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Daniel J Finley

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Jiayi Wu

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Marc W Kirschner

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Qi Ouyang

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Shuobing Chen

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Ying Lu

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Yong-Bei Ma

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Zhou Yu

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P2860

Mass spectrometric characterization of the affinity-purified human 26S proteasome complex

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

A gated channel into the proteasome core particle

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

The structure of the mammalian 20S proteasome at 2.75 A resolution

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

Structure of the S5a:K48-Linked Diubiquitin Complex and Its Interactions with Rpn13

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

Structures of asymmetric ClpX hexamers reveal nucleotide-dependent motions in a AAA+ protein-unfolding machine.

Structure of Rpn10 and Its Interactions with Polyubiquitin Chains and the Proteasome Subunit Rpn12

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12991-12996

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scholarly article

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10.1073/PNAS.1614614113

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46

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113

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2016-10-21T00:00:00Z

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5135334

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