Molecular and functional characterization of the only known hemiascomycete ortholog of the carboxyl terminus of Hsc70-interacting protein CHIP in the yeast Yarrowia lipolytica (Q35739990)

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scientific article published on 29 October 2011

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English	Molecular and functional characterization of the only known hemiascomycete ortholog of the carboxyl terminus of Hsc70-interacting protein CHIP in the yeast Yarrowia lipolytica	scientific article published on 29 October 2011

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scholarly article

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Europe PubMed Central

PubMed publication ID

10 August 2017

Molecular and functional characterization of the only known hemiascomycete ortholog of the carboxyl terminus of Hsc70-interacting protein CHIP in the yeast Yarrowia lipolytica (English)

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Europe PubMed Central

PubMed publication ID

10 August 2017

Yarrowia lipolytica

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inferred from title

5

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Mehdi Kabani

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Europe PubMed Central

PubMed publication ID

10 August 2017

3

object named as

Ronald Melki

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PubMed publication ID

10 August 2017

author name string

Céline N Martineau

1

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Europe PubMed Central

PubMed publication ID

10 August 2017

Marie-Thérèse Le Dall

2

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Europe PubMed Central

PubMed publication ID

10 August 2017

Jean-Marie Beckerich

4

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Europe PubMed Central

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10 August 2017

publication date

29 October 2011

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10 August 2017

number of pages

13

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Cell Stress & Chaperones

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10 August 2017

17

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10 August 2017

2

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Europe PubMed Central

PubMed publication ID

10 August 2017

229-241

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Europe PubMed Central

PubMed publication ID

10 August 2017

describes a project that uses

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11 June 2022

https://www.ebi.ac.uk/europepmc/webservices/rest/PMC3273565/fullTextXML

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Hsc70 protein interaction with soluble and fibrillar alpha-synuclein

1 reference

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The diverse members of the mammalian HSP70 machine show distinct chaperone-like activities

1 reference

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Protein quality control in the cytosol and the endoplasmic reticulum: brothers in arms.

1 reference

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Cellular strategies for controlling protein aggregation

1 reference

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Detection and analysis of alternative splicing in Yarrowia lipolytica reveal structural constraints facilitating nonsense-mediated decay of intron-retaining transcripts

1 reference

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Quality control against misfolded proteins in the cytosol: a network for cell survival

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Function of SSA subfamily of Hsp70 within and across species varies widely in complementing Saccharomyces cerevisiae cell growth and prion propagation

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Structural and functional diversity among eukaryotic Hsp70 nucleotide exchange factors.

1 reference

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Hsp104 and prion propagation

1 reference

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In vivo suppression of polyglutamine neurotoxicity by C-terminus of Hsp70-interacting protein (CHIP) supports an aggregation model of pathogenesis.

1 reference

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CHIP targets toxic alpha-Synuclein oligomers for degradation

1 reference

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CHIP deficiency decreases longevity, with accelerated aging phenotypes accompanied by altered protein quality control

1 reference

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Flo11p-independent control of "mat" formation by hsp70 molecular chaperones and nucleotide exchange factors in yeast

1 reference

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27 July 2018

Chaperone functions of the E3 ubiquitin ligase CHIP.

1 reference

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The co-chaperone CHIP is induced in various stresses and confers protection to cells.

1 reference

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1 reference

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CHIP protects from the neurotoxicity of expanded and wild-type ataxin-1 and promotes their ubiquitination and degradation

1 reference

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Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s

1 reference

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Expression of the cochaperone HspBP1 is not coordinately regulated with Hsp70 expression

1 reference

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CHIP-mediated stress recovery by sequential ubiquitination of substrates and Hsp70

1 reference

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Molecular chaperones and the assembly of the prion Sup35p, an in vitro study

1 reference

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Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex

1 reference

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The co-chaperone carboxyl terminus of Hsp70-interacting protein (CHIP) mediates alpha-synuclein degradation decisions between proteasomal and lysosomal pathways

1 reference

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Regulation of Hsp70 function by HspBP1: structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange

1 reference

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Co-chaperone CHIP associates with expanded polyglutamine protein and promotes their degradation by proteasomes.

1 reference

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Cooperation of molecular chaperones with the ubiquitin/proteasome system

1 reference

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The cochaperone HspBP1 inhibits the CHIP ubiquitin ligase and stimulates the maturation of the cystic fibrosis transmembrane conductance regulator

1 reference

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CHIP activates HSF1 and confers protection against apoptosis and cellular stress

1 reference

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For whom the bell tolls: protein quality control of the endoplasmic reticulum and the ubiquitin-proteasome connection

1 reference

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27 July 2018

U-box proteins as a new family of ubiquitin ligases

1 reference

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27 July 2018

HspBP1, a homologue of the yeast Fes1 and Sls1 proteins, is an Hsc70 nucleotide exchange factor

1 reference

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Nucleotide exchange factor for the yeast Hsp70 molecular chaperone Ssa1p

1 reference

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27 July 2018

CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein

1 reference

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Cooperation of a ubiquitin domain protein and an E3 ubiquitin ligase during chaperone/proteasome coupling

1 reference

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CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation

1 reference

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The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins

1 reference

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1 reference

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1 reference

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Conformational disease

1 reference

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Regulation of the heat-shock protein 70 reaction cycle by the mammalian DnaJ homolog, Hsp40.

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Complex interactions among members of an essential subfamily of hsp70 genes in Saccharomyces cerevisiae

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation

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CHIP suppresses polyglutamine aggregation and toxicity in vitro and in vivo.

1 reference

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1 reference

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1 reference

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1 reference

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1 reference

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

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10.1007/S12192-011-0302-6

1 reference

Europe PubMed Central

PubMed publication ID

10 August 2017

PMC publication ID

1 reference

Europe PubMed Central

PubMed publication ID

10 August 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

10 August 2017

ResearchGate publication ID

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