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Items: 1 to 20 of 37

1.
2.

ER protein quality control and proteasome-mediated protein degradation.

Brodsky JL, McCracken AA.

Semin Cell Dev Biol. 1999 Oct;10(5):507-13. Review.

PMID:
10597633
3.

Proteasome inhibitors: valuable new tools for cell biologists.

Lee DH, Goldberg AL.

Trends Cell Biol. 1998 Oct;8(10):397-403. Review.

PMID:
9789328
4.

Endoplasmic reticulum associated protein degradation: a chaperone assisted journey to hell.

Stolz A, Wolf DH.

Biochim Biophys Acta. 2010 Jun;1803(6):694-705. doi: 10.1016/j.bbamcr.2010.02.005. Epub 2010 Feb 25. Review.

5.

[Endoplasmic Reticulum Chaperones at the Tumor Cell Surface and in the Extracellular Space].

Brychtová V, Vojtěšek B.

Klin Onkol. Fall 2016;29 Suppl 4(Suppl 4):25-30. Review. Czech.

PMID:
27846717
6.

CHIP: a link between the chaperone and proteasome systems.

McDonough H, Patterson C.

Cell Stress Chaperones. 2003 Winter;8(4):303-8. Review.

7.

Chaperones and foldases in endoplasmic reticulum stress signaling in plants.

Gupta D, Tuteja N.

Plant Signal Behav. 2011 Feb;6(2):232-6. Epub 2011 Feb 1. Review.

8.

Molecular chaperones and proteostasis regulation during redox imbalance.

Niforou K, Cheimonidou C, Trougakos IP.

Redox Biol. 2014 Jan 30;2:323-32. doi: 10.1016/j.redox.2014.01.017. eCollection 2014. Review.

9.

BiP (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum.

Haas IG.

Experientia. 1994 Nov 30;50(11-12):1012-20. Review.

PMID:
7988659
10.
11.

Protein degradation: the ins and outs of the matter.

Cresswell P, Hughes EA.

Curr Biol. 1997 Sep 1;7(9):R552-5. Review.

12.

GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulum.

Marzec M, Eletto D, Argon Y.

Biochim Biophys Acta. 2012 Mar;1823(3):774-87. doi: 10.1016/j.bbamcr.2011.10.013. Epub 2011 Nov 3. Review.

13.

[Structure and functions of cytoplasmic peptide: N-glycanases in eukaryotic cells].

Suzuki T.

Seikagaku. 2003 Nov;75(11):1405-13. Review. Japanese. No abstract available.

PMID:
14699841
14.

[Mechanisms for sensing endoplasmic reticulum stress].

Kimata Y.

Tanpakushitsu Kakusan Koso. 2008 Jan;53(1):12-9. Review. Japanese. No abstract available.

PMID:
18186298
15.

ER chaperones in mammalian development and human diseases.

Ni M, Lee AS.

FEBS Lett. 2007 Jul 31;581(19):3641-51. Epub 2007 Apr 25. Review.

16.

Molecular chaperones in targeting misfolded proteins for ubiquitin-dependent degradation.

Kriegenburg F, Ellgaard L, Hartmann-Petersen R.

FEBS J. 2012 Feb;279(4):532-42. doi: 10.1111/j.1742-4658.2011.08456.x. Epub 2012 Jan 4. Review.

17.

The endoplasmic reticulum protein folding factory and its chaperones: new targets for drug discovery?

McLaughlin M, Vandenbroeck K.

Br J Pharmacol. 2011 Jan;162(2):328-45. doi: 10.1111/j.1476-5381.2010.01064.x. Review.

18.

Cooperation of molecular chaperones with the ubiquitin/proteasome system.

Esser C, Alberti S, Höhfeld J.

Biochim Biophys Acta. 2004 Nov 29;1695(1-3):171-88. Review.

19.

Heat shock proteins: molecular chaperones of protein biogenesis.

Craig EA, Gambill BD, Nelson RJ.

Microbiol Rev. 1993 Jun;57(2):402-14. Review.

20.

Keep your heart in shape: molecular chaperone networks for treating heart disease.

Tarone G, Brancaccio M.

Cardiovasc Res. 2014 Jun 1;102(3):346-61. doi: 10.1093/cvr/cvu049. Epub 2014 Feb 28. Review.

PMID:
24585203

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