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Similar articles for PubMed (Select 14522955)

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.

Functional specialization of calreticulin domains.

Nakamura K, Zuppini A, Arnaudeau S, Lynch J, Ahsan I, Krause R, Papp S, De Smedt H, Parys JB, Muller-Esterl W, Lew DP, Krause KH, Demaurex N, Opas M, Michalak M.

J Cell Biol. 2001 Sep 3;154(5):961-72. Epub 2001 Aug 27. Erratum in: J Cell Biol 2001 Dec 10;155(6):1083.

5.

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
6.
7.

Folding of thyroglobulin in the calnexin/calreticulin pathway and its alteration by loss of Ca2+ from the endoplasmic reticulum.

Di Jeso B, Ulianich L, Pacifico F, Leonardi A, Vito P, Consiglio E, Formisano S, Arvan P.

Biochem J. 2003 Mar 1;370(Pt 2):449-58.

8.
9.

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
10.

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
11.
12.

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.

13.

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
14.

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
15.

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.

16.

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.

17.

Enhanced ubiquitin-proteasome activity in calreticulin deficient cells: a compensatory mechanism for cell survival.

Uvarov AV, Mesaeli N.

Biochim Biophys Acta. 2008 Jun;1783(6):1237-47. doi: 10.1016/j.bbamcr.2008.03.004. Epub 2008 Mar 20.

18.

Glycan-dependent and -independent interactions contribute to cellular substrate recruitment by calreticulin.

Wijeyesakere SJ, Rizvi SM, Raghavan M.

J Biol Chem. 2013 Dec 6;288(49):35104-16. doi: 10.1074/jbc.M113.507921. Epub 2013 Oct 7.

19.

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

Ellgaard L, Frickel EM.

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

PMID:
14716078
20.

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.

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