ER-associated and proteasomemediated protein degradation: how two topologically restricted events came together (Q36914466)

17 August 2017

title

ER-associated and proteasomemediated protein degradation: how two topologically restricted events came together (English)

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17 August 2017

Brodsky JL

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17 August 2017

McCracken AA

series ordinal

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17 August 2017

publication date

1 April 1997

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17 August 2017

published in

Trends in Cell Biology

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17 August 2017

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17 August 2017

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17 August 2017

page(s)

151-156

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Ubiquitin, proteasomes, and the regulation of intracellular protein degradation

17 August 2017

cites work

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A possible role of ER-60 protease in the degradation of misfolded proteins in the endoplasmic reticulum

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Multiple proteolytic systems, including the proteasome, contribute to CFTR processing

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Degradation of CFTR by the ubiquitin-proteasome pathway

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The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol

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

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

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

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Proteasomes: multicatalytic proteinase complexes

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

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Conformational maturation of CFTR but not its mutant counterpart (delta F508) occurs in the endoplasmic reticulum and requires ATP

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Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituent of the ER quality control apparatus.

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Lumenal proteins of the mammalian endoplasmic reticulum are required to complete protein translocation

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Targeting of the hepatitis B virus precore protein to the endoplasmic reticulum membrane: after signal peptide cleavage translocation can be aborted and the product released into the cytoplasm

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In vivo iodination of a misfolded proinsulin reveals co-localized signals for Bip binding and for degradation in the ER.

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Degradation of 3-hydroxy-3-methylglutaryl-CoA reductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis.

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7 January 2021

Reversal of fortune for nascent proteins

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The human immunodeficiency virus type 1 Vpu protein specifically binds to the cytoplasmic domain of CD4: implications for the mechanism of degradation

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Oligomeric Rings of the Sec61p Complex Induced by Ligands Required for Protein Translocation

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7 January 2021

10.1016/S0962-8924(97)01020-9

Identifiers

DOI

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17 August 2017

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