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Items: 1 to 20 of 111

1.

Peptide-based interactions with calnexin target misassembled membrane proteins into endoplasmic reticulum-derived multilamellar bodies.

Korkhov VM, Milan-Lobo L, Zuber B, Farhan H, Schmid JA, Freissmuth M, Sitte HH.

J Mol Biol. 2008 Apr 25;378(2):337-52. doi: 10.1016/j.jmb.2008.02.056. Epub 2008 Mar 4.

2.

Identification of novel peptide binding proteins in the endoplasmic reticulum: ERp72, calnexin, and grp170.

Spee P, Subjeck J, Neefjes J.

Biochemistry. 1999 Aug 10;38(32):10559-66.

PMID:
10441153
3.

The Lectin Chaperone Calnexin Is Involved in the Endoplasmic Reticulum Stress Response by Regulating Ca2+ Homeostasis in Aspergillus nidulans.

Zhang S, Zheng H, Chen Q, Chen Y, Wang S, Lu L, Zhang S.

Appl Environ Microbiol. 2017 Jul 17;83(15). pii: e00673-17. doi: 10.1128/AEM.00673-17. Print 2017 Aug 1.

4.

Cell surface expression of calnexin, a molecular chaperone in the endoplasmic reticulum.

Okazaki Y, Ohno H, Takase K, Ochiai T, Saito T.

J Biol Chem. 2000 Nov 17;275(46):35751-8.

5.

Concentrative export from the endoplasmic reticulum of the gamma-aminobutyric acid transporter 1 requires binding to SEC24D.

Farhan H, Reiterer V, Korkhov VM, Schmid JA, Freissmuth M, Sitte HH.

J Biol Chem. 2007 Mar 9;282(10):7679-89. Epub 2007 Jan 8.

6.

N-glycan-dependent quality control of the Na,K-ATPase beta(2) subunit.

Tokhtaeva E, Munson K, Sachs G, Vagin O.

Biochemistry. 2010 Apr 13;49(14):3116-28. doi: 10.1021/bi100115a.

7.

Involvement of endoplasmic reticulum chaperones in the folding of hepatitis C virus glycoproteins.

Choukhi A, Ung S, Wychowski C, Dubuisson J.

J Virol. 1998 May;72(5):3851-8.

8.

Molecular chaperones stimulate the functional expression of the cocaine-sensitive serotonin transporter.

Tate CG, Whiteley E, Betenbaugh MJ.

J Biol Chem. 1999 Jun 18;274(25):17551-8.

9.

Two discontinuous segments in the carboxyl terminus are required for membrane targeting of the rat gamma-aminobutyric acid transporter-1 (GAT1).

Farhan H, Korkhov VM, Paulitschke V, Dorostkar MM, Scholze P, Kudlacek O, Freissmuth M, Sitte HH.

J Biol Chem. 2004 Jul 2;279(27):28553-63. Epub 2004 Apr 8.

10.

Folding of VSV G protein: sequential interaction with BiP and calnexin.

Hammond C, Helenius A.

Science. 1994 Oct 21;266(5184):456-8.

PMID:
7939687
13.

Role of calnexin in the glycan-independent quality control of proteolipid protein.

Swanton E, High S, Woodman P.

EMBO J. 2003 Jun 16;22(12):2948-58.

14.

Protein quality control in the ER: the recognition of misfolded proteins.

Määttänen P, Gehring K, Bergeron JJ, Thomas DY.

Semin Cell Dev Biol. 2010 Jul;21(5):500-11. doi: 10.1016/j.semcdb.2010.03.006. Epub 2010 Mar 25. Review.

PMID:
20347046
15.

In vitro assays of the functions of calnexin and calreticulin, lectin chaperones of the endoplasmic reticulum.

Ireland BS, Niggemann M, Williams DB.

Methods Mol Biol. 2006;347:331-42. Review.

PMID:
17072021
16.
17.

Oligomerization of the {gamma}-aminobutyric acid transporter-1 is driven by an interplay of polar and hydrophobic interactions in transmembrane helix II.

Korkhov VM, Farhan H, Freissmuth M, Sitte HH.

J Biol Chem. 2004 Dec 31;279(53):55728-36. Epub 2004 Oct 20.

19.

[The role of chaperone proteins in the assembly of envelope proteins of hepatitis C virus].

Dubuisson J.

Bull Mem Acad R Med Belg. 1998;153(7-9):343-9; discussion 350-1. French.

PMID:
10100398
20.

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.

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