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Items: 1 to 20 of 100

1.

Dimerization of ERp29, a PDI-like protein, is essential for its diverse functions.

Rainey-Barger EK, Mkrtchian S, Tsai B.

Mol Biol Cell. 2007 Apr;18(4):1253-60.

2.

The C-terminal domain of ERp29 mediates polyomavirus binding, unfolding, and infection.

Rainey-Barger EK, Mkrtchian S, Tsai B.

J Virol. 2009 Feb;83(3):1483-91. doi: 10.1128/JVI.02057-08.

3.

A PDI family network acts distinctly and coordinately with ERp29 to facilitate polyomavirus infection.

Walczak CP, Tsai B.

J Virol. 2011 Mar;85(5):2386-96. doi: 10.1128/JVI.01855-10.

4.

Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complex.

Sargsyan E, Baryshev M, Szekely L, Sharipo A, Mkrtchian S.

J Biol Chem. 2002 May 10;277(19):17009-15.

5.

Unfolded protein response is involved in the pathology of human congenital hypothyroid goiter and rat non-goitrous congenital hypothyroidism.

Baryshev M, Sargsyan E, Wallin G, Lejnieks A, Furudate S, Hishinuma A, Mkrtchian S.

J Mol Endocrinol. 2004 Jun;32(3):903-20.

PMID:
15171721
6.

Overexpression of ERp29 in the thyrocytes of FRTL-5 cells.

Park S, You KH, Shong M, Goo TW, Yun EY, Kang SW, Kwon OY.

Mol Biol Rep. 2005 Mar;32(1):7-13.

PMID:
15865205
7.

ERp29 triggers a conformational change in polyomavirus to stimulate membrane binding.

Magnuson B, Rainey EK, Benjamin T, Baryshev M, Mkrtchian S, Tsai B.

Mol Cell. 2005 Oct 28;20(2):289-300.

8.

ERp29 is an essential endoplasmic reticulum factor regulating secretion of thyroglobulin.

Baryshev M, Sargsyan E, Mkrtchian S.

Biochem Biophys Res Commun. 2006 Feb 10;340(2):617-24.

PMID:
16380091
9.

Oligomerization properties of ERp29, an endoplasmic reticulum stress protein.

Mkrtchian S, Baryshev M, Matvijenko O, Sharipo A, Sandalova T, Schneider G, Ingelman-Sundberg M.

FEBS Lett. 1998 Jul 24;431(3):322-6. Erratum in: FEBS Lett 1998 Aug 21;433(3):335. Mkrtchiana S [corrected to Mkrtchian S].

10.
11.

Thioredoxin fold as homodimerization module in the putative chaperone ERp29: NMR structures of the domains and experimental model of the 51 kDa dimer.

Liepinsh E, Baryshev M, Sharipo A, Ingelman-Sundberg M, Otting G, Mkrtchian S.

Structure. 2001 Jun;9(6):457-71.

12.

Mixed-disulfide folding intermediates between thyroglobulin and endoplasmic reticulum resident oxidoreductases ERp57 and protein disulfide isomerase.

Di Jeso B, Park YN, Ulianich L, Treglia AS, Urbanas ML, High S, Arvan P.

Mol Cell Biol. 2005 Nov;25(22):9793-805.

13.

Crystal structure and functional analysis of the protein disulfide isomerase-related protein ERp29.

Barak NN, Neumann P, Sevvana M, Schutkowski M, Naumann K, Malesević M, Reichardt H, Fischer G, Stubbs MT, Ferrari DM.

J Mol Biol. 2009 Feb 6;385(5):1630-42. doi: 10.1016/j.jmb.2008.11.052.

PMID:
19084538
14.

ERp29 deficiency affects sensitivity to apoptosis via impairment of the ATF6-CHOP pathway of stress response.

Hirsch I, Weiwad M, Prell E, Ferrari DM.

Apoptosis. 2014 May;19(5):801-15. doi: 10.1007/s10495-013-0961-0.

PMID:
24370996
15.

Biophysical characterization of ERp29. Evidence for a key structural role of cysteine 125.

Hermann VM, Cutfield JF, Hubbard MJ.

J Biol Chem. 2005 Apr 8;280(14):13529-37.

16.

Endoplasmic reticulum protein (ERp) 29 binds as strongly as protein disulfide isomerase (PDI) to bisphenol A.

Miyake Y, Hashimoto S, Sasaki Y, Kudo T, Oguro A, Imaoka S.

Chem Res Toxicol. 2014 Apr 21;27(4):501-6. doi: 10.1021/tx400357q.

PMID:
24512454
17.

Purification and biochemical characterization of native ERp29 from rat liver.

Hubbard MJ, Mangum JE, McHugh NJ.

Biochem J. 2004 Nov 1;383(Pt. 3):589-97.

18.

Endoplasmic reticulum protein 29 (ERp29): An emerging role in cancer.

Zhang D, Richardson DR.

Int J Biochem Cell Biol. 2011 Jan;43(1):33-6. doi: 10.1016/j.biocel.2010.09.019. Review.

PMID:
20920593
19.

ERp29, a general endoplasmic reticulum marker, is highly expressed throughout the brain.

MacLeod JC, Sayer RJ, Lucocq JM, Hubbard MJ.

J Comp Neurol. 2004 Sep 6;477(1):29-42.

PMID:
15281078
20.

ERp29 regulates response to doxorubicin by a PERK-mediated mechanism.

Farmaki E, Mkrtchian S, Papazian I, Papavassiliou AG, Kiaris H.

Biochim Biophys Acta. 2011 Jun;1813(6):1165-71. doi: 10.1016/j.bbamcr.2011.03.003.

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