FICD acts bifunctionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP. - Wikidata - wikimedia - TriplyDB

FICD acts bifunctionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP.

FICD acts bifunctionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP.

http://www.wikidata.org/entity/Q41029065

about

A unique deubiquitinase that deconjugates phosphoribosyl-linked protein ubiquitination.rAMPing Up Stress Signaling: Protein AMPylation in Metazoans.Legionella and Coxiella effectors: strength in diversity and activity.Functional characterization of zebrafish orthologs of the human Beta 3-Glucosyltransferase B3GLCT gene mutated in Peters Plus Syndrome.AMPylation targets the rate-limiting step of BiP's ATPase cycle for its functional inactivation.Fic-mediated deAMPylation is not dependent on homodimerization and rescues toxic AMPylation in flies.Adapting Secretory Proteostasis and Function Through the Unfolded Protein Response.Enzymes Involved in AMPylation and deAMPylation.2-Chlorohexadecanoic acid induces ER stress and mitochondrial dysfunction in brain microvascular endothelial cells.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

P2860

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P2860

FICD acts bifunctionally to AMPylate and de-AMPylate the endoplasmic reticulum chaperone BiP.

http://www.wikidata.org/entity/Q41029065

description

2016 nî lūn-bûn

@nan

2016年の論文

@ja

2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

@zh-mo

2016年論文

@zh-tw

2016年论文

@wuu

2016年论文

@zh

2016年论文

@zh-cn

name

FICD acts bifunctionally to AM ...... asmic reticulum chaperone BiP.

@en

type

label

FICD acts bifunctionally to AM ...... asmic reticulum chaperone BiP.

@en

prefLabel

FICD acts bifunctionally to AM ...... asmic reticulum chaperone BiP.

@en

P1433

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P356

P1433

Nature Structural & Molecular Biology

P1476

FICD acts bifunctionally to AM ...... asmic reticulum chaperone BiP.

@en

P2093

Steffen Preissler

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

Vladimir Saudek

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

P2860

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

The fic domain: regulation of cell signaling by adenylylation

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

Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3

Structure of the adenylylation domain of E. coli glutamine synthetase adenylyl transferase: evidence for gene duplication and evolution of a new active site

Structural basis of Fic-mediated adenylylation

Adapting proteostasis for disease intervention

De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila

Kinetic and structural insights into the mechanism of AMPylation by VopS Fic domain

Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox

P2888

P304

23-29

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

P31

scholarly article

P356

10.1038/NSMB.3337

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P433

1

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P478

24

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2016-12-05T00:00:00Z

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1007513795

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P698

27918543

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P921

molecular chaperones

endoplasmic reticulum

P932

5221731

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