Protein quality control: chaperones culling corrupt conformations (Q40400832)

20 September 2017

title

Protein quality control: chaperones culling corrupt conformations (English)

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20 September 2017

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Amie J McClellan

1

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Judith Frydman

series ordinal

4

object named as

Judith Frydman

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20 September 2017

Stephen Tam

2

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20 September 2017

Daniel Kaganovich

series ordinal

3

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20 September 2017

publication date

1 August 2005

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20 September 2017

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20 September 2017

volume

7

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20 September 2017

issue

8

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20 September 2017

page(s)

736-741

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Folding of newly translated proteins in vivo: the role of molecular chaperones

20 September 2017

cites work

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Protein quality control: U-box-containing E3 ubiquitin ligases join the fold

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Processing of CFTR: traversing the cellular maze--how much CFTR needs to go through to avoid cystic fibrosis?

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Conformation-dependent antibodies target diseases of protein misfolding

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Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases

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Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death

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Cellular toxicity of polyglutamine expansion proteins: mechanism of transcription factor deactivation

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Hsp70 and Hsp40 attenuate formation of spherical and annular polyglutamine oligomers by partitioning monomer

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7 January 2021

Ubiquitin-dependent degradation of certain protein substrates in vitro requires the molecular chaperone Hsc70

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Involvement of the molecular chaperone Ydj1 in the ubiquitin-dependent degradation of short-lived and abnormal proteins in Saccharomyces cerevisiae

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7 January 2021

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

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7 January 2021

Distinct roles for the Hsp40 and Hsp90 molecular chaperones during cystic fibrosis transmembrane conductance regulator degradation in yeast

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Folding and quality control of the VHL tumor suppressor proceed through distinct chaperone pathways

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Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes

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7 January 2021

Cooperation of molecular chaperones with the ubiquitin/proteasome system

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7 January 2021

HSJ1 is a neuronal shuttling factor for the sorting of chaperone clients to the proteasome

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7 January 2021

Molecular chaperones and the art of recognizing a lost cause

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Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu

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A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase

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7 January 2021

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

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7 January 2021

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

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7 January 2021

Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism

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7 January 2021

Ubiquitin, proteasome and parkin

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7 January 2021

Ubiquitination of a new form of alpha-synuclein by parkin from human brain: implications for Parkinson's disease

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7 January 2021

CHIP is associated with Parkin, a gene responsible for familial Parkinson's disease, and enhances its ubiquitin ligase activity

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7 January 2021

Parkin facilitates the elimination of expanded polyglutamine proteins and leads to preservation of proteasome function.

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7 January 2021

BAG5 inhibits parkin and enhances dopaminergic neuron degeneration

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7 January 2021

CHIP activates HSF1 and confers protection against apoptosis and cellular stress

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7 January 2021

Genomic expression programs in the response of yeast cells to environmental changes

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7 January 2021

Dorfin ubiquitylates mutant SOD1 and prevents mutant SOD1-mediated neurotoxicity

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7 January 2021

Dorfin Localizes to Lewy Bodies and Ubiquitylates Synphilin-1

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7 January 2021

Sir Antagonist 1 (San1) is a ubiquitin ligase

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7 January 2021

Degradation-mediated protein quality control in the nucleus

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https://api.crossref.org/works/10.1038%2FNCB0805-736

7 January 2021

Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC.

1 reference

https://api.crossref.org/works/10.1038%2FNCB0805-736

7 January 2021

The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex

1 reference

https://api.crossref.org/works/10.1038%2FNCB0805-736

7 January 2021

The threshold for polyglutamine-expansion protein aggregation and cellular toxicity is dynamic and influenced by aging in Caenorhabditis elegans

1 reference

https://api.crossref.org/works/10.1038%2FNCB0805-736

7 January 2021

Interaction of U-box-type ubiquitin-protein ligases (E3s) with molecular chaperones

1 reference

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7 January 2021

Human Sgt1 binds HSP90 through the CHORD-Sgt1 domain and not the tetratricopeptide repeat domain

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7 January 2021

Identifiers

DOI

10.1038/NCB0805-736

1 reference

20 September 2017

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