Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis - Test2 - elhamkhani - TriplyDB

Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis

Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis

http://www.wikidata.org/entity/Q24682823

about

Human Fas-associated factor 1, interacting with ubiquitinated proteins and valosin-containing protein, is involved in the ubiquitin-proteasome pathway Valosin-containing protein (VCP/p97) is an activator of wild-type ataxin-3 The role of the central flexible region on the aggregation and conformational properties of human ataxin-3 Regulation of retrotranslocation by p97-associated deubiquitinating enzyme ataxin-3 Crystal structure of a Josephin-ubiquitin complex: evolutionary restraints on ataxin-3 deubiquitinating activity Ubiquitination directly enhances activity of the deubiquitinating enzyme ataxin-3 Evidence for distinct functions for human DNA repair factors hHR23A and hHR23B CDK5 protects from caspase-induced Ataxin-3 cleavage and neurodegeneration Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila Yeast Pth2 is a UBL domain-binding protein that participates in the ubiquitin-proteasome pathway.Rad23 interaction with the proteasome is regulated by phosphorylation of its ubiquitin-like (UbL) domain Ubp15p, a ubiquitin hydrolase associated with the peroxisomal export machinery.The promise and perils of HDAC inhibitors in neurodegeneration Aggresome formation and neurodegenerative diseases: therapeutic implications AAA ATPase p97/valosin-containing protein interacts with gp78, a ubiquitin ligase for endoplasmic reticulum-associated degradation Inclusion body myopathy-associated mutations in p97/VCP impair endoplasmic reticulum-associated degradation Proteotoxic stress increases nuclear localization of ataxin-3 Overexpression of the autophagic beclin-1 protein clears mutant ataxin-3 and alleviates Machado-Joseph disease Trinucleotide repeats: a structural perspective The slow Wallerian degeneration protein, WldS, binds directly to VCP/p97 and partially redistributes it within the nucleus.Neuron-specific proteotoxicity of mutant ataxin-3 in C. elegans: rescue by the DAF-16 and HSF-1 pathways Ubiquitin domain proteins in disease.Polyglutamine genes interact to modulate the severity and progression of neurodegeneration in Drosophila.Allele-specific RNA silencing of mutant ataxin-3 mediates neuroprotection in a rat model of Machado-Joseph disease.Ataxin-3 promotes genome integrity by stabilizing Chk1.Ataxin-3 plays a role in mouse myogenic differentiation through regulation of integrin subunit levels Understanding the role of the Josephin domain in the PolyUb binding and cleavage properties of ataxin-3.A Mighty "Protein Extractor" of the Cell: Structure and Function of the p97/CDC48 ATPase.Absence of ataxin-3 leads to enhanced stress response in C. elegans.The solution structure of the Josephin domain of ataxin-3: structural determinants for molecular recognition.Deubiquitinating function of ataxin-3: insights from the solution structure of the Josephin domain.The polyglutamine neurodegenerative protein ataxin 3 regulates aggresome formation.RNA interference mitigates motor and neuropathological deficits in a cerebellar mouse model of Machado-Joseph disease Activity and cellular functions of the deubiquitinating enzyme and polyglutamine disease protein ataxin-3 are regulated by ubiquitination at lysine 117.Functional interactions as a survival strategy against abnormal aggregation Dominant negative effect of polyglutamine expansion perturbs normal function of ataxin-3 in neuronal cells.Valosin-containing protein gene mutations: cellular phenotypes relevant to neurodegeneration.The toxicity of tau in Alzheimer disease: turnover, targets and potential therapeutics Balancing act: deubiquitinating enzymes in the nervous system.Proteostasis regulation at the endoplasmic reticulum: a new perturbation site for targeted cancer therapy.

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P2860

Ataxin-3 interactions with rad23 and valosin-containing protein and its associations with ubiquitin chains and the proteasome are consistent with a role in ubiquitin-mediated proteolysis

http://www.wikidata.org/entity/Q24682823

description

2003 nî lūn-bûn

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2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված

@hy

2003年の論文

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2003年論文

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2003年論文

@zh-hant

2003年論文

@zh-hk

2003年論文

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2003年論文

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2003年论文

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name

Ataxin-3 interactions with rad ...... ubiquitin-mediated proteolysis

@ast

Ataxin-3 interactions with rad ...... ubiquitin-mediated proteolysis

@en

Ataxin-3 interactions with rad ...... ubiquitin-mediated proteolysis

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type

label

Ataxin-3 interactions with rad ...... ubiquitin-mediated proteolysis

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Ataxin-3 interactions with rad ...... ubiquitin-mediated proteolysis

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Ataxin-3 interactions with rad ...... ubiquitin-mediated proteolysis

@nl

prefLabel

Ataxin-3 interactions with rad ...... ubiquitin-mediated proteolysis

@ast

Ataxin-3 interactions with rad ...... ubiquitin-mediated proteolysis

@en

Ataxin-3 interactions with rad ...... ubiquitin-mediated proteolysis

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P356

MCB.23.18.6469-6483.2003

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Molecular and Cellular Biology

P1476

Ataxin-3 interactions with rad ...... ubiquitin-mediated proteolysis

@en

P2093

Edward S Stenroos

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

Ellen W Doss-Pepe

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

Kiran Madura

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

William G Johnson

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

P2860

Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome

Ataxin-3, the MJD1 gene product, interacts with the two human homologs of yeast DNA repair protein RAD23, HHR23A and HHR23B

Valosin-containing protein is a multi-ubiquitin chain-targeting factor required in ubiquitin-proteasome degradation

Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains

Involvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha

Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly.

Recognition of the polyubiquitin proteolytic signal

Direct binding of ubiquitin conjugates by the mammalian p97 adaptor complexes, p47 and Ufd1-Npl4.

The ubiquitin system

The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover.

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6469-83

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10.1128/MCB.23.18.6469-6483.2003

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2003-09-01T00:00:00Z

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10593465

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12944474

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ubiquitin-proteasome system

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193705

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