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The mammalian endoplasmic reticulum-associated degradation system

Cold Spring Harbor perspectives in biology, 2013-09, Vol.5 (9), p.a013185-a013185

2013

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Impairment of the Ubiquitin-Proteasome System by Protein Aggregation

Science (American Association for the Advancement of Science), 2001-05, Vol.292 (5521), p.1552-1555

2001

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Aggresomes, inclusion bodies and protein aggregation

Trends in Cell Biology, 2000-12, Vol.10 (12), p.524-530

Kopito, Ron R

2000

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Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover

Proceedings of the National Academy of Sciences - PNAS, 2013-01, Vol.110 (4), p.1345-1350

2013

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Global Impairment of the Ubiquitin-Proteasome System by Nuclear or Cytoplasmic Protein Aggregates Precedes Inclusion Body Formation

Molecular cell, 2005-02, Vol.17 (3), p.351-365

2005

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Ribosomal protein RPL26 is the principal target of UFMylation

Proceedings of the National Academy of Sciences - PNAS, 2019-01, Vol.116 (4), p.1299-1308

2019

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Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain

Nature communications, 2015-04, Vol.6 (1), p.6768-6768, Article 6768

2015

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RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum

Proceedings of the National Academy of Sciences - PNAS, 2023-04, Vol.120 (16), p.e2220340120

2023

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Subversion of cellular autophagosomal machinery by RNA viruses

PLoS biology, 2005-05, Vol.3 (5), p.e156-e156

2005

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HDAC6 and Microtubules Are Required for Autophagic Degradation of Aggregated Huntingtin

The Journal of biological chemistry, 2005-12, Vol.280 (48), p.40282-40292

2005

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Simultaneous measurement of amyloid fibril formation by dynamic light scattering and fluorescence reveals complex aggregation kinetics

PloS one, 2013-01, Vol.8 (1), p.e54541-e54541

2013

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Defining human ERAD networks through an integrative mapping strategy

Nature cell biology, 2012-01, Vol.14 (1), p.93-105

2012

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Protein misfolding specifies recruitment to cytoplasmic inclusion bodies

The Journal of cell biology, 2016-04, Vol.213 (2), p.229-241

2016

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Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates

Nature cell biology, 2009-02, Vol.11 (2), p.219-225

2009

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ER Quality Control: The Cytoplasmic Connection

Cell, 1997-02, Vol.88 (4), p.427-430

Kopito, Ron R

1997

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Redundant and Antagonistic Roles of XTP3B and OS9 in Decoding Glycan and Non-glycan Degrons in ER-Associated Degradation

Molecular cell, 2018-05, Vol.70 (3), p.516-530.e6

2018

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Aggresomes: A Cellular Response to Misfolded Proteins

The Journal of cell biology, 1998-12, Vol.143 (7), p.1883-1898

1998

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Prion-Like Characteristics of Polyglutamine-Containing Proteins

Cold Spring Harbor perspectives in medicine, 2018-02, Vol.8 (2), p.a024257

2018

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Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease

The Journal of cell biology, 2012-03, Vol.196 (5), p.573-587

2012

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Formation of High Molecular Weight Complexes of Mutant Cu,Zn-Superoxide Dismutase in a Mouse Model for Familial Amyotrophic Lateral Sclerosis

Proceedings of the National Academy of Sciences - PNAS, 2000-11, Vol.97 (23), p.12571-12576

2000

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Biosynthesis and Degradation of CFTR

Physiological reviews, 1999-01, Vol.79 (1), p.167-S173

KOPITO, RON R

1999

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Global changes to the ubiquitin system in Huntington's disease

Nature, 2007-08, Vol.448 (7154), p.704-708

2007

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A Rhodopsin Mutant Linked to Autosomal Dominant Retinitis Pigmentosa Is Prone to Aggregate and Interacts with the Ubiquitin Proteasome System

The Journal of biological chemistry, 2002-09, Vol.277 (37), p.34150-34160

2002

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Ubiquitin Accumulation on Disease Associated Protein Aggregates Is Correlated with Nuclear Ubiquitin Depletion, Histone De-Ubiquitination and Impaired DNA Damage Response

PloS one, 2017-01, Vol.12 (1), p.e0169054-e0169054

2017

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Conformational disease

Nature cell biology, 2000-11, Vol.2 (11), p.E207-E209

2000

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The mammalian endoplasmic reticulum-associated degradation system

Impairment of the Ubiquitin-Proteasome System by Protein Aggregation

Aggresomes, inclusion bodies and protein aggregation

Spatial regulation of UBXD8 and p97/VCP controls ATGL-mediated lipid droplet turnover

Global Impairment of the Ubiquitin-Proteasome System by Nuclear or Cytoplasmic Protein Aggregates Precedes Inclusion Body Formation

Ribosomal protein RPL26 is the principal target of UFMylation

Prion-like transmission of neuronal huntingtin aggregates to phagocytic glia in the Drosophila brain

RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum

Subversion of cellular autophagosomal machinery by RNA viruses

HDAC6 and Microtubules Are Required for Autophagic Degradation of Aggregated Huntingtin

Simultaneous measurement of amyloid fibril formation by dynamic light scattering and fluorescence reveals complex aggregation kinetics

Defining human ERAD networks through an integrative mapping strategy

Protein misfolding specifies recruitment to cytoplasmic inclusion bodies

Cytoplasmic penetration and persistent infection of mammalian cells by polyglutamine aggregates

ER Quality Control: The Cytoplasmic Connection

Redundant and Antagonistic Roles of XTP3B and OS9 in Decoding Glycan and Non-glycan Degrons in ER-Associated Degradation

Aggresomes: A Cellular Response to Misfolded Proteins

Prion-Like Characteristics of Polyglutamine-Containing Proteins

Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease

Formation of High Molecular Weight Complexes of Mutant Cu,Zn-Superoxide Dismutase in a Mouse Model for Familial Amyotrophic Lateral Sclerosis

Biosynthesis and Degradation of CFTR

Global changes to the ubiquitin system in Huntington's disease

A Rhodopsin Mutant Linked to Autosomal Dominant Retinitis Pigmentosa Is Prone to Aggregate and Interacts with the Ubiquitin Proteasome System

Ubiquitin Accumulation on Disease Associated Protein Aggregates Is Correlated with Nuclear Ubiquitin Depletion, Histone De-Ubiquitination and Impaired DNA Damage Response

Conformational disease

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