Ron Kopito
Affiliations: | Stanford University, Palo Alto, CA |
Area:
BiologyGoogle:
"Ron Kopito"Mean distance: 21373.2
Children
Sign in to add traineeNeil F. Bence | grad student | 2003 | Stanford |
Rahul S. Rajan | grad student | 2003 | Stanford |
Cami K. Bruns | grad student | 2006 | Stanford |
Pei-Hsien Ren | grad student | 2007 | Stanford |
Ethan J. Greenblatt | grad student | 2007-2011 | Stanford (FlyTree) |
John C. Christianson | post-doc | ||
Kate Raley Susman | post-doc | Stanford | |
James Arthur Olzmann | post-doc | 2007-2012 |
Collaborators
Sign in to add collaboratorJayakumar Rajadas | collaborator | 2003-2005 | Stanford (Chemistry Tree) |
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Publications
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Hickey KL, Panov A, Whelan EM, et al. (2024) Temporal control of acute protein aggregate turnover by UBE3C and NRF1-dependent proteasomal pathways. Biorxiv : the Preprint Server For Biology |
DaRosa PA, Penchev I, Gumbin SC, et al. (2024) UFM1 E3 ligase promotes recycling of 60S ribosomal subunits from the ER. Nature |
Riepe C, Wąchalska M, Deol KK, et al. (2023) Small molecule correctors divert CFTR-F508del from ERAD by stabilizing sequential folding states. Molecular Biology of the Cell. mbcE23080336 |
Riepe C, Wąchalska M, Deol KK, et al. (2023) Small molecule correctors divert CFTR-F508del from ERAD by stabilizing sequential folding states. Biorxiv : the Preprint Server For Biology |
Roberts MA, Deol KK, Mathiowetz AJ, et al. (2023) Parallel CRISPR-Cas9 screens identify mechanisms of PLIN2 and lipid droplet regulation. Developmental Cell |
Scavone F, Gumbin SC, Da Rosa PA, et al. (2023) RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum. Proceedings of the National Academy of Sciences of the United States of America. 120: e2220340120 |
Scavone F, Gumbin SC, DaRosa PA, et al. (2023) RPL26/uL24 UFMylation is essential for ribosome-associated quality control at the endoplasmic reticulum. Biorxiv : the Preprint Server For Biology |
Peter JJ, Magnussen HM, DaRosa PA, et al. (2022) A non-canonical scaffold-type E3 ligase complex mediates protein UFMylation. The Embo Journal. e111015 |
Gottlieb CD, Thompson ACS, Ordureau A, et al. (2019) Acute unfolding of a single protein immediately stimulates recruitment of ubiquitin protein ligase E3C (UBE3C) to 26S proteasomes. The Journal of Biological Chemistry |
Leto DE, Kopito RR. (2019) Methods for genetic analysis of mammalian ER-associated degradation. Methods in Enzymology. 619: 97-120 |