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Biochemical and Biophysical Research Communications|August 25, 2004
The physiological unfolded protein response in the thyroid epithelial cellsErnest Sargsyan, Mikhail Baryshev, Souren MkrtchianBiochemical and Biophysical Research Communications|December 29, 2005
ERp29 is an essential endoplasmic reticulum factor regulating secretion of thyroglobulinMikhail Baryshev, Ernest Sargsyan, Souren MkrtchianGene|June 1, 2002
Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29Ernest Sargsyan, Mikhail Baryshev, Maria Backlund, et al.The Journal of Biological Chemistry|March 9, 2002
Identification of ERp29, an endoplasmic reticulum lumenal protein, as a new member of the thyroglobulin folding complexErnest Sargsyan, Mikhail Baryshev, Laszlo Szekely, et al.Molecular Carcinogenesis|April 9, 2008
ERp29, an endoplasmic reticulum secretion factor is involved in the growth of breast tumor xenograftsSouren Mkrtchian, Mikhail Baryshev, Ernest Sargsyan, et al.Molecular Cell|October 26, 2005
ERp29 triggers a conformational change in polyomavirus to stimulate membrane bindingBrian Magnuson, Emily K Rainey, Thomas Benjamin, et al.Endocrine-Related Cancer|March 21, 2015
Targeting unfolded protein response in cancer and diabetesSouren MkrtchianAntioxidants & Redox Signaling|May 9, 2006
ERp29, an unusual redox-inactive member of the thioredoxin familySouren Mkrtchian, Tatyana SandalovaJournal of Virology|November 21, 2008
The C-terminal domain of ERp29 mediates polyomavirus binding, unfolding, and infectionEmily K Rainey-Barger, Souren Mkrtchian, Billy TsaiMolecular Biology of the Cell|February 3, 2007
Dimerization of ERp29, a PDI-like protein, is essential for its diverse functionsEmily K Rainey-Barger, Souren Mkrtchian, Billy TsaiPageof 10