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Items: 1 to 20 of 127


BAT3 guides misfolded glycoproteins out of the endoplasmic reticulum.

Claessen JH, Ploegh HL.

PLoS One. 2011;6(12):e28542. doi: 10.1371/journal.pone.0028542. Epub 2011 Dec 8.


Enzymatic blockade of the ubiquitin-proteasome pathway.

Ernst R, Claessen JH, Mueller B, Sanyal S, Spooner E, van der Veen AG, Kirak O, Schlieker CD, Weihofen WA, Ploegh HL.

PLoS Biol. 2011 Mar;8(3):e1000605. doi: 10.1371/journal.pbio.1000605. Epub 2011 Mar 29.


A membrane protein required for dislocation of misfolded proteins from the ER.

Lilley BN, Ploegh HL.

Nature. 2004 Jun 24;429(6994):834-40.


A viral deubiquitylating enzyme restores dislocation of substrates from the endoplasmic reticulum (ER) in semi-intact cells.

Sanyal S, Claessen JH, Ploegh HL.

J Biol Chem. 2012 Jul 6;287(28):23594-603. doi: 10.1074/jbc.M112.365312. Epub 2012 May 22.


Glycoprotein folding and the role of EDEM1, EDEM2 and EDEM3 in degradation of folding-defective glycoproteins.

Olivari S, Molinari M.

FEBS Lett. 2007 Jul 31;581(19):3658-64. Epub 2007 May 4. Review.


A ubiquitin-like domain recruits an oligomeric chaperone to a retrotranslocation complex in endoplasmic reticulum-associated degradation.

Xu Y, Liu Y, Lee JG, Ye Y.

J Biol Chem. 2013 Jun 21;288(25):18068-76. doi: 10.1074/jbc.M112.449199. Epub 2013 May 12.


Sequential assistance of molecular chaperones and transient formation of covalent complexes during protein degradation from the ER.

Molinari M, Galli C, Piccaluga V, Pieren M, Paganetti P.

J Cell Biol. 2002 Jul 22;158(2):247-57. Epub 2002 Jul 15.


The Role of Lectin-Carbohydrate Interactions in the Regulation of ER-Associated Protein Degradation.

Słomińska-Wojewódzka M, Sandvig K.

Molecules. 2015 May 27;20(6):9816-46. doi: 10.3390/molecules20069816. Review.


A novel stress-induced EDEM variant regulating endoplasmic reticulum-associated glycoprotein degradation.

Olivari S, Galli C, Alanen H, Ruddock L, Molinari M.

J Biol Chem. 2005 Jan 28;280(4):2424-8. Epub 2004 Dec 3.


Distinct machinery is required in Saccharomyces cerevisiae for the endoplasmic reticulum-associated degradation of a multispanning membrane protein and a soluble luminal protein.

Huyer G, Piluek WF, Fansler Z, Kreft SG, Hochstrasser M, Brodsky JL, Michaelis S.

J Biol Chem. 2004 Sep 10;279(37):38369-78. Epub 2004 Jul 12.


The evolution of N-glycan-dependent endoplasmic reticulum quality control factors for glycoprotein folding and degradation.

Banerjee S, Vishwanath P, Cui J, Kelleher DJ, Gilmore R, Robbins PW, Samuelson J.

Proc Natl Acad Sci U S A. 2007 Jul 10;104(28):11676-81. Epub 2007 Jul 2.


Glycoprotein folding in the endoplasmic reticulum: a tale of three chaperones?

High S, Lecomte FJ, Russell SJ, Abell BM, Oliver JD.

FEBS Lett. 2000 Jun 30;476(1-2):38-41. Review.


SEL1L, the homologue of yeast Hrd3p, is involved in protein dislocation from the mammalian ER.

Mueller B, Lilley BN, Ploegh HL.

J Cell Biol. 2006 Oct 23;175(2):261-70. Epub 2006 Oct 16.

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