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Items: 1 to 20 of 73

1.

Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD.

Taxis C, Hitt R, Park SH, Deak PM, Kostova Z, Wolf DH.

J Biol Chem. 2003 Sep 19;278(38):35903-13. Epub 2003 Jul 7.

2.

Checkpoints in ER-associated degradation: excuse me, which way to the proteasome?

Ahner A, Brodsky JL.

Trends Cell Biol. 2004 Sep;14(9):474-8. Review.

PMID:
15350974
3.

Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD).

Nishikawa S, Brodsky JL, Nakatsukasa K.

J Biochem. 2005 May;137(5):551-5. Review.

PMID:
15944407
4.

Role and regulation of the ER chaperone BiP.

Gething MJ.

Semin Cell Dev Biol. 1999 Oct;10(5):465-72. Review.

PMID:
10597629
5.

Endoplasmic reticulum degradation: reverse protein flow of no return.

Sommer T, Wolf DH.

FASEB J. 1997 Dec;11(14):1227-33. Review.

PMID:
9409541
6.

Mechanism and components of endoplasmic reticulum-associated degradation.

Hoseki J, Ushioda R, Nagata K.

J Biochem. 2010 Jan;147(1):19-25. doi: 10.1093/jb/mvp194. Epub 2009 Nov 18. Review.

PMID:
19923195
7.

ER-associated degradation in protein quality control and cellular regulation.

Hampton RY.

Curr Opin Cell Biol. 2002 Aug;14(4):476-82. Review.

PMID:
12383799
8.

The role of MRH domain-containing lectins in ERAD.

Hosokawa N, Kamiya Y, Kato K.

Glycobiology. 2010 Jun;20(6):651-60. doi: 10.1093/glycob/cwq013. Epub 2010 Jan 28. Review.

PMID:
20118070
9.

Endoplasmic reticulum-associated protein degradation.

Jarosch E, Lenk U, Sommer T.

Int Rev Cytol. 2003;223:39-81. Review.

PMID:
12641210
10.

A role for Rad23 proteins in 26S proteasome-dependent protein degradation?

van Laar T, van der Eb AJ, Terleth C.

Mutat Res. 2002 Jan 29;499(1):53-61. Review.

PMID:
11804604
11.

CHIP: a quality-control E3 ligase collaborating with molecular chaperones.

Murata S, Chiba T, Tanaka K.

Int J Biochem Cell Biol. 2003 May;35(5):572-8. Review.

PMID:
12672450
12.
13.

Involvement of molecular chaperones in intracellular protein breakdown.

Sherman MY, Goldberg AL.

EXS. 1996;77:57-78. Review.

PMID:
8856969
14.

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.

15.

One step at a time: endoplasmic reticulum-associated degradation.

Vembar SS, Brodsky JL.

Nat Rev Mol Cell Biol. 2008 Dec;9(12):944-57. doi: 10.1038/nrm2546. Epub 2008 Nov 12. Review.

16.

The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum.

Nakatsukasa K, Brodsky JL.

Traffic. 2008 Jun;9(6):861-70. doi: 10.1111/j.1600-0854.2008.00729.x. Epub 2008 Feb 24. Review.

17.

Roles of ubiquitin in endoplasmic reticulum-associated protein degradation (ERAD).

Goder V.

Curr Protein Pept Sci. 2012 Aug;13(5):425-35. Review.

PMID:
22812526
18.

Lectin-like ERAD players in ER and cytosol.

Yoshida Y, Tanaka K.

Biochim Biophys Acta. 2010 Feb;1800(2):172-80. doi: 10.1016/j.bbagen.2009.07.029. Epub 2009 Aug 6. Review.

PMID:
19665047
19.
20.

Co-chaperones of the mammalian endoplasmic reticulum.

Melnyk A, Rieger H, Zimmermann R.

Subcell Biochem. 2015;78:179-200. doi: 10.1007/978-3-319-11731-7_9. Review.

PMID:
25487022

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