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Elife|July 7, 2025
The ESCRT protein CHMP5 restricts bone formation by controlling endolysosome-mitochondrion-mediated cell senescenceFan Zhang, Yuan Wang, Luyang Zhang, et al.The Journal of Cell Biology|October 14, 2004
Translation reinitiation at alternative open reading frames regulates gene expression in an integrated stress responsePhoebe D Lu, Heather P Harding, David RonProceedings of the National Academy of Sciences of the United States of America|March 15, 2013
Membrane lipid saturation activates endoplasmic reticulum unfolded protein response transducers through their transmembrane domainsRomain Volmer, Kattria van der Ploeg, David RonActa Crystallographica. Section F, Structural Biology and Crystallization Communications|February 9, 2008
Preliminary X-ray crystallographic studies of mouse UPR responsive protein P58(IPK) TPR fragmentJiahui Tao, Yunkun Wu, David Ron, et al.Cell Reports|March 21, 2019
Entosis Controls a Developmental Cell Clearance in C. elegansYongchan Lee, Jens C Hamann, Mark Pellegrino, et al.Current Opinion in Cell Biology|June 25, 2005
The dynamic ER: experimental approaches and current questionsChristine M Federovitch, David Ron, Randolph Y HamptonJournal of Molecular Biology|February 27, 2010
Crystal structure of P58(IPK) TPR fragment reveals the mechanism for its molecular chaperone activity in UPRJiahui Tao, Kseniya Petrova, David Ron, et al.Acta Crystallographica. Section D, Biological Crystallography|May 6, 2011
The structure of the PERK kinase domain suggests the mechanism for its activationWenjun Cui, Jingzhi Li, David Ron, et al.Nature Reviews. Drug Discovery|October 27, 2021
Pharmacological targeting of endoplasmic reticulum stress in diseaseStefan J Marciniak, Joseph E Chambers, David RonThe Journal of Biological Chemistry|November 14, 2012
Uncoupling proteostasis and development in vitro with a small molecule inhibitor of the pancreatic endoplasmic reticulum kinase, PERKHeather P Harding, Alisa F Zyryanova, David RonPageof 37