Unrestrained AMPylation targets cytosolic chaperones and activates the heat shock response. - Wikidata - wikimedia - TriplyDB

Unrestrained AMPylation targets cytosolic chaperones and activates the heat shock response.

Unrestrained AMPylation targets cytosolic chaperones and activates the heat shock response.

http://www.wikidata.org/entity/Q37589999

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rAMPing Up Stress Signaling: Protein AMPylation in Metazoans.Temporal dynamics of gene expression in heat-stressed Caenorhabditis elegans.In vitro AMPylation Assays Using Purified, Recombinant Proteins.Lower temperatures reduce type I interferon activity and promote alphaviral arthritis.Fic-mediated deAMPylation is not dependent on homodimerization and rescues toxic AMPylation in flies.Enzymes Involved in AMPylation and deAMPylation.Chaperone AMPylation modulates aggregation and toxicity of neurodegenerative disease-associated polypeptides.Adaptation to constant light requires Fic-mediated AMPylation of BiP to protect against reversible photoreceptor degeneration

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Unrestrained AMPylation targets cytosolic chaperones and activates the heat shock response.

http://www.wikidata.org/entity/Q37589999

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

@tr

scientific article published on 28 December 2016

@en

vedecký článok

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vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Unrestrained AMPylation target ...... vates the heat shock response.

@en

Unrestrained AMPylation target ...... vates the heat shock response.

@nl

type

label

Unrestrained AMPylation target ...... vates the heat shock response.

@en

Unrestrained AMPylation target ...... vates the heat shock response.

@nl

prefLabel

Unrestrained AMPylation target ...... vates the heat shock response.

@en

Unrestrained AMPylation target ...... vates the heat shock response.

@nl

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PNAS.1619234114

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

P1476

Unrestrained AMPylation target ...... vates the heat shock response.

@en

P2093

David Pincus

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

Hidde L Ploegh

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Jadyn R Damon

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Joanna Krakowiak

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

Monique Grootveld

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

Xu Zheng

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P2860

Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins

AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling

The Caenorhabditis elegans Protein FIC-1 Is an AMPylase That Covalently Modifies Heat-Shock 70 Family Proteins, Translation Elongation Factors and Histones

Signal integration in the endoplasmic reticulum unfolded protein response

Cooperation of the molecular chaperone Ydj1 with specific Hsp70 homologs to suppress protein aggregation.

Defining the Essential Function of Yeast Hsf1 Reveals a Compact Transcriptional Program for Maintaining Eukaryotic Proteostasis.

Adapting proteostasis for disease intervention

Enzymatic assembly of DNA molecules up to several hundred kilobases

Differential analysis of gene regulation at transcript resolution with RNA-seq

REVIGO summarizes and visualizes long lists of gene ontology terms

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scholarly article

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10.1073/PNAS.1619234114

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2

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114

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Matthias C Truttmann

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2016-12-28T00:00:00Z

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28031489

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molecular chaperones

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5240723

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