A regulatory link between ER-associated protein degradation and the unfolded-protein response (Q27931238)

PubMed

PubMed publication ID

10878801

1 December 2016

title

A regulatory link between ER-associated protein degradation and the unfolded-protein response (English)

1 reference

PubMed

PubMed publication ID

10878801

E2 ubiquitin-conjugating protein UBC1 YDR177W

1 December 2016

main subject

1 reference

GOA release 2020-03-11

author

Ernst Jarosch

1 reference

ORCID Public Data File 2021

author name string

R Friedlander

1

0 references

E Jarosch

2

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J Urban

3

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C Volkwein

4

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T Sommer

5

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language of work or name

English

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publication date

July 2000

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1 reference

PubMed publication ID

10878801

ER quality control: the cytoplasmic connection

1 December 2016

volume

2

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issue

7

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page(s)

379-84

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cites work

1 reference

Retrograde protein translocation: ERADication of secretory proteins in health and disease

21 January 2018

1 reference

Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP.

21 January 2018

1 reference

Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation

21 January 2018

1 reference

Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure

21 January 2018

1 reference

Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction

21 January 2018

1 reference

The engagement of Sec61p in the ER dislocation process

21 January 2018

1 reference

Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein

21 January 2018

1 reference

Der3p/Hrd1p Is Required for Endoplasmic Reticulum-associated Degradation of Misfolded Lumenal and Integral Membrane Proteins

21 January 2018

1 reference

SCF and Cullin/Ring H2-based ubiquitin ligases

21 January 2018

1 reference

ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway

21 January 2018

1 reference

Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase

21 January 2018

1 reference

Role of Cue1p in Ubiquitination and Degradation at the ER Surface

21 January 2018

1 reference

Intracellular signaling from the endoplasmic reticulum to the nucleus

21 January 2018

1 reference

A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response

21 January 2018

1 reference

A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

21 January 2018

1 reference

The Transmembrane Kinase Ire1p Is a Site-Specific Endonuclease That Initiates mRNA Splicing in the Unfolded Protein Response

21 January 2018

1 reference

Endoplasmic Reticulum Stress-induced mRNA Splicing Permits Synthesis of Transcription Factor Hac1p/Ern4p That Activates the Unfolded Protein Response

21 January 2018

1 reference

A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum

21 January 2018

1 reference

Resistance to cadmium mediated by ubiquitin-dependent proteolysis

21 January 2018

1 reference

Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls

21 January 2018

1 reference

Proteasome inhibition leads to a heat-shock response, induction of endoplasmic reticulum chaperones, and thermotolerance

21 January 2018

1 reference

Ubiquitin and the control of protein fate in the secretory and endocytic pathways

21 January 2018

1 reference

inferred from DOI database lookup

7 January 2021

based on heuristic

Degradation of subunits of the Sec61p complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway.

1 reference

inferred from DOI database lookup

7 January 2021

based on heuristic

UBC1 encodes a novel member of an essential subfamily of yeast ubiquitin-conjugating enzymes involved in protein degradation.

1 reference