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Items: 9

1.

Deuterium-Depleted Water Influence on the Isotope 2H/1H Regulation in Body and Individual Adaptation.

Basov A, Fedulova L, Baryshev M, Dzhimak S.

Nutrients. 2019 Aug 15;11(8). pii: E1903. doi: 10.3390/nu11081903. Review.

2.

Upregulation of the Chemokine Receptor CCR2B in Epstein‒Barr Virus-Positive Burkitt Lymphoma Cell Lines with the Latency III Program.

Kozireva S, Rudevica Z, Baryshev M, Leonciks A, Kashuba E, Kholodnyuk I.

Viruses. 2018 May 3;10(5). pii: E239. doi: 10.3390/v10050239.

3.

DNA methylation of the Oct4A enhancers in embryonal carcinoma cells after etoposide treatment is associated with alternative splicing and altered pluripotency in reversibly senescent cells.

Baryshev M, Inashkina I, Salmina K, Huna A, Jackson TR, Erenpreisa J.

Cell Cycle. 2018;17(3):362-366. doi: 10.1080/15384101.2018.1426412. Epub 2018 Mar 19.

4.

ERp29, an endoplasmic reticulum secretion factor is involved in the growth of breast tumor xenografts.

Mkrtchian S, Baryshev M, Sargsyan E, Chatzistamou I, Volakaki AA, Chaviaras N, Pafiti A, Triantafyllou A, Kiaris H.

Mol Carcinog. 2008 Nov;47(11):886-92. doi: 10.1002/mc.20444.

PMID:
18395818
5.

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. Epub 2005 Dec 19.

PMID:
16380091
6.

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.

7.

The physiological unfolded protein response in the thyroid epithelial cells.

Sargsyan E, Baryshev M, Mkrtchian S.

Biochem Biophys Res Commun. 2004 Sep 17;322(2):570-6.

PMID:
15325268
8.

Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29.

Sargsyan E, Baryshev M, Backlund M, Sharipo A, Mkrtchian S.

Gene. 2002 Feb 20;285(1-2):127-39.

PMID:
12039039
9.

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. Epub 2002 Mar 7.

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