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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 SandalovaBiochemical 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 MkrtchianJournal 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 TsaiBiochemical and Biophysical Research Communications|October 30, 2016
The role of microRNAs in liver injury at the crossroad between hepatic cell death and regenerationVolker M Lauschke, Souren Mkrtchian, Magnus Ingelman-SundbergFrontiers in Pharmacology|December 20, 2018
Computational Methods for the Pharmacogenetic Interpretation of Next Generation Sequencing DataYitian Zhou, Kohei Fujikura, Souren Mkrtchian, et al.Drug Metabolism Reviews|June 4, 2016
The CYP2W1 enzyme: regulation, properties and activation of prodrugsJia Guo, Inger Johansson, Souren Mkrtchian, 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.Pageof 6