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Immunity|September 18, 2015
Stressed-Out Endoplasmic Reticulum Inflames the MitochondriaSunny Shin, Yair ArgonAdvances in Experimental Medicine and Biology|April 29, 2015
Candidate genes that affect aging through protein homeostasisYair Argon, Tali GidalevitzImmunological Reviews|August 9, 2021
The special unfolded protein response in plasma cellsDaniela Ricci, Tali Gidalevitz, Yair ArgonBiochimica Et Biophysica Acta|March 20, 2013
Orchestration of secretory protein folding by ER chaperonesTali Gidalevitz, Fred Stevens, Yair ArgonSeminars in Cell & Developmental Biology|March 13, 2010
GRP94 in ER quality control and stress responsesDavide Eletto, Devin Dersh, Yair ArgonBiochimica Et Biophysica Acta|November 15, 2011
GRP94: An HSP90-like protein specialized for protein folding and quality control in the endoplasmic reticulumMichal Marzec, Davide Eletto, Yair ArgonMolecular Biology of the Cell|September 30, 2016
Tay-Sachs disease mutations in HEXA target the α chain of hexosaminidase A to endoplasmic reticulum-associated degradationDevin Dersh, Yuichiro Iwamoto, Yair ArgonCellular Microbiology|July 30, 2008
Escherichia coli interaction with human brain microvascular endothelial cells induces signal transducer and activator of transcription 3 association with the C-terminal domain of Ec-gp96, the outer membrane protein A receptor for invasionRavi Maruvada, Yair Argon, Nemani V PrasadaraoThe Journal of Biological Chemistry|February 12, 2005
Cysteines in CH1 underlie retention of unassembled Ig heavy chainsYechiel Elkabetz, Yair Argon, Shoshana Bar-NunMolecular Biology of the Cell|January 23, 2009
The chaperone activity of GRP94 toward insulin-like growth factor II is necessary for the stress response to serum deprivationOlga Ostrovsky, Noreen T Ahmed, Yair ArgonPageof 12