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Items: 1 to 20 of 108

1.

GRP94, an ER chaperone with protein and peptide binding properties.

Argon Y, Simen BB.

Semin Cell Dev Biol. 1999 Oct;10(5):495-505. Review.

PMID:
10597632
2.
3.

Structural transitions accompanying the activation of peptide binding to the endoplasmic reticulum Hsp90 chaperone GRP94.

Wearsch PA, Voglino L, Nicchitta CV.

Biochemistry. 1998 Apr 21;37(16):5709-19.

PMID:
9548957
4.

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.

5.

Structure of unliganded GRP94, the endoplasmic reticulum Hsp90. Basis for nucleotide-induced conformational change.

Dollins DE, Immormino RM, Gewirth DT.

J Biol Chem. 2005 Aug 26;280(34):30438-47. Epub 2005 Jun 11.

6.

Receptor mediated and fluid phase pathways for internalization of the ER Hsp90 chaperone GRP94 in murine macrophages.

Wassenberg JJ, Dezfulian C, Nicchitta CV.

J Cell Sci. 1999 Jul;112 ( Pt 13):2167-75.

7.

Structures of GRP94-nucleotide complexes reveal mechanistic differences between the hsp90 chaperones.

Dollins DE, Warren JJ, Immormino RM, Gewirth DT.

Mol Cell. 2007 Oct 12;28(1):41-56.

8.

The glucose-regulated proteins (GRP78 and GRP94): functions, gene regulation, and applications.

Little E, Ramakrishnan M, Roy B, Gazit G, Lee AS.

Crit Rev Eukaryot Gene Expr. 1994;4(1):1-18. Review.

PMID:
7987045
9.

Adenosine nucleotides and the regulation of GRP94-client protein interactions.

Rosser MF, Trotta BM, Marshall MR, Berwin B, Nicchitta CV.

Biochemistry. 2004 Jul 13;43(27):8835-45.

PMID:
15236592
10.

Structure of the N-terminal domain of GRP94. Basis for ligand specificity and regulation.

Soldano KL, Jivan A, Nicchitta CV, Gewirth DT.

J Biol Chem. 2003 Nov 28;278(48):48330-8. Epub 2003 Sep 11.

11.

The immunological properties of endoplasmic reticulum chaperones: a conflict of interest?

Nicchitta CV, Reed RC.

Essays Biochem. 2000;36:15-25. Review.

PMID:
12471899
12.
13.

A Grp on the Hsp90 mechanism.

Richter K, Reinstein J, Buchner J.

Mol Cell. 2007 Oct 26;28(2):177-9. Review.

14.

GRP94 in ER quality control and stress responses.

Eletto D, Dersh D, Argon Y.

Semin Cell Dev Biol. 2010 Jul;21(5):479-85. doi: 10.1016/j.semcdb.2010.03.004. Epub 2010 Mar 16. Review.

15.

Ligand-induced conformational shift in the N-terminal domain of GRP94, an Hsp90 chaperone.

Immormino RM, Dollins DE, Shaffer PL, Soldano KL, Walker MA, Gewirth DT.

J Biol Chem. 2004 Oct 29;279(44):46162-71. Epub 2004 Aug 2.

16.

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
18.

Radicicol-sensitive peptide binding to the N-terminal portion of GRP94.

Vogen S, Gidalevitz T, Biswas C, Simen BB, Stein E, Gulmen F, Argon Y.

J Biol Chem. 2002 Oct 25;277(43):40742-50. Epub 2002 Aug 19.

19.

Hop: more than an Hsp70/Hsp90 adaptor protein.

Odunuga OO, Longshaw VM, Blatch GL.

Bioessays. 2004 Oct;26(10):1058-68. Review.

PMID:
15382137
20.

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