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Items: 1 to 20 of 193

1.

Identification of an N-domain histidine essential for chaperone function in calreticulin.

Guo L, Groenendyk J, Papp S, Dabrowska M, Knoblach B, Kay C, Parker JM, Opas M, Michalak M.

J Biol Chem. 2003 Dec 12;278(50):50645-53. Epub 2003 Oct 1.

2.

Identification by mutational analysis of amino acid residues essential in the chaperone function of calreticulin.

Martin V, Groenendyk J, Steiner SS, Guo L, Dabrowska M, Parker JM, Müller-Esterl W, Opas M, Michalak M.

J Biol Chem. 2006 Jan 27;281(4):2338-46. Epub 2005 Nov 16.

3.

Calreticulin, a multi-process calcium-buffering chaperone of the endoplasmic reticulum.

Michalak M, Groenendyk J, Szabo E, Gold LI, Opas M.

Biochem J. 2009 Feb 1;417(3):651-66. doi: 10.1042/BJ20081847. Review.

PMID:
19133842
4.

Gentamicin binds to the lectin site of calreticulin and inhibits its chaperone activity.

Horibe T, Matsui H, Tanaka M, Nagai H, Yamaguchi Y, Kato K, Kikuchi M.

Biochem Biophys Res Commun. 2004 Oct 8;323(1):281-7.

PMID:
15351734
5.
6.
7.

The interplay between calcium and the in vitro lectin and chaperone activities of calreticulin.

Conte IL, Keith N, Gutiérrez-Gonzalez C, Parodi AJ, Caramelo JJ.

Biochemistry. 2007 Apr 17;46(15):4671-80. Epub 2007 Mar 27.

PMID:
17385894
8.

Ca2+ signaling and calcium binding chaperones of the endoplasmic reticulum.

Michalak M, Robert Parker JM, Opas M.

Cell Calcium. 2002 Nov-Dec;32(5-6):269-78. Review.

PMID:
12543089
9.

Soluble tyrosinase is an endoplasmic reticulum (ER)-associated degradation substrate retained in the ER by calreticulin and BiP/GRP78 and not calnexin.

Popescu CI, Paduraru C, Dwek RA, Petrescu SM.

J Biol Chem. 2005 Apr 8;280(14):13833-40. Epub 2005 Jan 27.

10.

Calreticulin, a Ca2+-binding chaperone of the endoplasmic reticulum.

Gelebart P, Opas M, Michalak M.

Int J Biochem Cell Biol. 2005 Feb;37(2):260-6. Review.

PMID:
15474971
11.

Functional characterization of Arabidopsis calreticulin1a: a key alleviator of endoplasmic reticulum stress.

Christensen A, Svensson K, Persson S, Jung J, Michalak M, Widell S, Sommarin M.

Plant Cell Physiol. 2008 Jun;49(6):912-24. doi: 10.1093/pcp/pcn065. Epub 2008 Apr 23.

PMID:
18436549
12.

Ca2+ regulation of interactions between endoplasmic reticulum chaperones.

Corbett EF, Oikawa K, Francois P, Tessier DC, Kay C, Bergeron JJ, Thomas DY, Krause KH, Michalak M.

J Biol Chem. 1999 Mar 5;274(10):6203-11.

13.

Functional relationship between calreticulin, calnexin, and the endoplasmic reticulum luminal domain of calnexin.

Danilczyk UG, Cohen-Doyle MF, Williams DB.

J Biol Chem. 2000 Apr 28;275(17):13089-97.

14.

Calnexin, calreticulin, and ERp57: teammates in glycoprotein folding.

Ellgaard L, Frickel EM.

Cell Biochem Biophys. 2003;39(3):223-47. Review.

PMID:
14716078
15.

The Structure of calnexin, an ER chaperone involved in quality control of protein folding.

Schrag JD, Bergeron JJ, Li Y, Borisova S, Hahn M, Thomas DY, Cygler M.

Mol Cell. 2001 Sep;8(3):633-44.

16.

ER-60 domains responsible for interaction with calnexin and calreticulin.

Urade R, Okudo H, Kato H, Moriyama T, Arakaki Y.

Biochemistry. 2004 Jul 13;43(27):8858-68.

PMID:
15236594
17.

Delineation of the lectin site of the molecular chaperone calreticulin.

Thomson SP, Williams DB.

Cell Stress Chaperones. 2005 Autumn;10(3):242-51.

18.

The metal ion binding properties of calreticulin modulate its conformational flexibility and thermal stability.

Li Z, Stafford WF, Bouvier M.

Biochemistry. 2001 Sep 18;40(37):11193-201.

PMID:
11551218
19.

Calreticulin, a multifunctional Ca2+ binding chaperone of the endoplasmic reticulum.

Michalak M, Mariani P, Opas M.

Biochem Cell Biol. 1998;76(5):779-85. Review.

PMID:
10353711
20.

Alternative chaperone machinery may compensate for calreticulin/calnexin deficiency in Caenorhabditis elegans.

Lee W, Kim KR, Singaravelu G, Park BJ, Kim DH, Ahnn J, Yoo YJ.

Proteomics. 2006 Feb;6(4):1329-39.

PMID:
16404716

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