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Items: 1 to 20 of 120

1.

The endoplasmic reticulum-associated degradation pathways of budding yeast.

Thibault G, Ng DT.

Cold Spring Harb Perspect Biol. 2012 Dec 1;4(12). pii: a013193. doi: 10.1101/cshperspect.a013193. Review.

2.

The mammalian endoplasmic reticulum-associated degradation system.

Olzmann JA, Kopito RR, Christianson JC.

Cold Spring Harb Perspect Biol. 2013 Sep 1;5(9). pii: a013185. doi: 10.1101/cshperspect.a013185. Review.

3.

The evolving role of ubiquitin modification in endoplasmic reticulum-associated degradation.

Preston GM, Brodsky JL.

Biochem J. 2017 Feb 15;474(4):445-469. doi: 10.1042/BCJ20160582. Review.

PMID:
28159894
4.

Ubiquitin-specific protease 25 functions in Endoplasmic Reticulum-associated degradation.

Blount JR, Burr AA, Denuc A, Marfany G, Todi SV.

PLoS One. 2012;7(5):e36542. doi: 10.1371/journal.pone.0036542. Epub 2012 May 9.

5.

Assays to measure ER-associated degradation in yeast.

Tran JR, Brodsky JL.

Methods Mol Biol. 2012;832:505-18. doi: 10.1007/978-1-61779-474-2_36.

6.

Grp94 Protein Delivers γ-Aminobutyric Acid Type A (GABAA) Receptors to Hrd1 Protein-mediated Endoplasmic Reticulum-associated Degradation.

Di XJ, Wang YJ, Han DY, Fu YL, Duerfeldt AS, Blagg BS, Mu TW.

J Biol Chem. 2016 Apr 29;291(18):9526-39. doi: 10.1074/jbc.M115.705004. Epub 2016 Mar 4.

7.

Endoplasmic reticulum lectin XTP3-B inhibits endoplasmic reticulum-associated degradation of a misfolded α1-antitrypsin variant.

Fujimori T, Kamiya Y, Nagata K, Kato K, Hosokawa N.

FEBS J. 2013 Mar;280(6):1563-75. doi: 10.1111/febs.12157. Epub 2013 Feb 28.

8.

ERAD ubiquitin ligases: multifunctional tools for protein quality control and waste disposal in the endoplasmic reticulum.

Mehnert M, Sommer T, Jarosch E.

Bioessays. 2010 Oct;32(10):905-13. doi: 10.1002/bies.201000046. Epub 2010 Aug 30. Review.

PMID:
20806269
9.

Defining human ERAD networks through an integrative mapping strategy.

Christianson JC, Olzmann JA, Shaler TA, Sowa ME, Bennett EJ, Richter CM, Tyler RE, Greenblatt EJ, Harper JW, Kopito RR.

Nat Cell Biol. 2011 Nov 27;14(1):93-105. doi: 10.1038/ncb2383.

10.

Glycosylation-independent ERAD pathway serves as a backup system under ER stress.

Ushioda R, Hoseki J, Nagata K.

Mol Biol Cell. 2013 Oct;24(20):3155-63. doi: 10.1091/mbc.E13-03-0138. Epub 2013 Aug 21.

11.

Fusion of an intact secretory protein permits a misfolded protein to exit from the endoplasmic reticulum in yeast.

Suyama K, Hori M, Gomi K, Shintani T.

Biosci Biotechnol Biochem. 2014;78(1):49-59. doi: 10.1080/09168451.2014.877185. Epub 2014 Apr 10.

PMID:
25036483
12.

ERAD: the long road to destruction.

Meusser B, Hirsch C, Jarosch E, Sommer T.

Nat Cell Biol. 2005 Aug;7(8):766-72. Review.

PMID:
16056268
13.

Quality control: ER-associated degradation: protein quality control and beyond.

Ruggiano A, Foresti O, Carvalho P.

J Cell Biol. 2014 Mar 17;204(6):869-79. doi: 10.1083/jcb.201312042. Review.

14.

Intrinsic conformational determinants signal protein misfolding to the Hrd1/Htm1 endoplasmic reticulum-associated degradation system.

Xie W, Kanehara K, Sayeed A, Ng DT.

Mol Biol Cell. 2009 Jul;20(14):3317-29. doi: 10.1091/mbc.E09-03-0231. Epub 2009 May 20.

15.
16.

Yos9p and Hrd1p mediate ER retention of misfolded proteins for ER-associated degradation.

Izawa T, Nagai H, Endo T, Nishikawa S.

Mol Biol Cell. 2012 Apr;23(7):1283-93. doi: 10.1091/mbc.E11-08-0722. Epub 2012 Feb 1.

17.

The final moments of misfolded proteins en route to the proteasome.

Zhang T, Ye Y.

DNA Cell Biol. 2014 Aug;33(8):477-83. doi: 10.1089/dna.2014.2452. Epub 2014 May 15. Review.

18.

The delicate balance between secreted protein folding and endoplasmic reticulum-associated degradation in human physiology.

Guerriero CJ, Brodsky JL.

Physiol Rev. 2012 Apr;92(2):537-76. doi: 10.1152/physrev.00027.2011. Review.

19.

Physiological Roles of Ubiquitin Ligases Related to the Endoplasmic Reticulum.

Kaneko M.

Yakugaku Zasshi. 2016;136(6):805-9. doi: 10.1248/yakushi.15-00292-2. Review. Japanese.

20.

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.

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