Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates. (Q42564287)

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scientific article published on January 2011

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English	Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates.	scientific article published on January 2011

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scholarly article

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19 January 2020

Disorder targets misorder in nuclear quality control degradation: a disordered ubiquitin ligase directly recognizes its misfolded substrates (English)

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19 January 2020

quality control

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nuclear protein quality control by the ubiquitin-proteasome system

1 reference

Gene Ontology release 2020-05-02

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Richard G Gardner

11

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19 January 2020

Melissa N Locke

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19 January 2020

Lauren A Richardson

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19 January 2020

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Joel C Rosenbaum

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19 January 2020

Eric K Fredrickson

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19 January 2020

Michelle L Oeser

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19 January 2020

Carrie M Garrett-Engele

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19 January 2020

Zara W Nelson

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19 January 2020

Elizabeth D Hetrick

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19 January 2020

Thomas I Milac

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19 January 2020

Daniel E Gottschling

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19 January 2020

publication date

1 January 2011

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19 January 2020

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19 January 2020

41

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19 January 2020

1

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19 January 2020

93-106

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19 January 2020

Proteolytic processing of tau.

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28 May 2018

Ubr1 and Ubr2 function in a quality control pathway for degradation of unfolded cytosolic proteins

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Cytoplasmic protein quality control degradation mediated by parallel actions of the E3 ubiquitin ligases Ubr1 and San1

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28 May 2018

ANCHOR: web server for predicting protein binding regions in disordered proteins.

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Substrate binding site flexibility of the small heat shock protein molecular chaperones

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Misfolded membrane proteins are specifically recognized by the transmembrane domain of the Hrd1p ubiquitin ligase

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Intranuclear degradation of polyglutamine aggregates by the ubiquitin-proteasome system.

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28 May 2018

One step at a time: endoplasmic reticulum-associated degradation

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The unfoldomics decade: an update on intrinsically disordered proteins.

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28 May 2018

Degradation of a cytosolic protein requires endoplasmic reticulum-associated degradation machinery.

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28 May 2018

The Jpred 3 secondary structure prediction server

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Using circular dichroism spectra to estimate protein secondary structure

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Abnormalities of the nucleus and nuclear inclusions in neurodegenerative disease: a work in progress

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Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins

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A luminal surveillance complex that selects misfolded glycoproteins for ER-associated degradation

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28 May 2018

PML clastosomes prevent nuclear accumulation of mutant ataxin-7 and other polyglutamine proteins

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28 May 2018

The Hrd1p ligase complex forms a linchpin between ER-lumenal substrate selection and Cdc48p recruitment

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28 May 2018

Assessing protein disorder and induced folding

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28 May 2018

Nuclear aggresomes form by fusion of PML-associated aggregates.

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28 May 2018

FoldIndex: a simple tool to predict whether a given protein sequence is intrinsically unfolded

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28 May 2018

IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content

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28 May 2018

Degradation-mediated protein quality control in the nucleus

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Hsp70 chaperones: cellular functions and molecular mechanism

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The roles of proteolysis and nuclear localisation in the toxicity of the polyglutamine diseases. A review

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28 May 2018

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Intrinsically unstructured proteins

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Sequence complexity of disordered protein

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10.1016/J.MOLCEL.2010.12.004

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19 January 2020

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19 January 2020

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19 January 2020

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