Eric M Rubenstein
Affiliations: | Ball State University, Muncie, IN, United States |
Area:
protein quality control, cell biologyGoogle:
"Eric Rubenstein"Parents
Sign in to add mentorMartin C. Schmidt | grad student | 2003-2008 | University of Pittsburgh |
Mark W. Hochstrasser | post-doc | 2008-2012 | Yale |
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Publications
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Runnebohm AM, Indovina CJ, Turk SM, et al. (2023) Methionine Restriction Impairs Degradation of a Protein that Aberrantly Engages the Endoplasmic Reticulum Translocon. Micropublication Biology. 2023 |
Doss EM, Moore JM, Harman BH, et al. (2023) Characterization of endoplasmic reticulum-associated degradation in the human fungal pathogen . Peerj. 11: e15897 |
Turk SM, Indovina CJ, Miller JM, et al. (2023) Lipid biosynthesis perturbation impairs Endoplasmic Reticulum-Associated Degradation. The Journal of Biological Chemistry. 104939 |
Woodruff KA, Richards KA, Evans MD, et al. (2021) Inner Nuclear Membrane Asi Ubiquitin Ligase Catalytic Subunits Asi1p and Asi3p, but not Asi2p, confer resistance to aminoglycoside hygromycin B in . Micropublication Biology. 2021 |
Runnebohm AM, Evans MD, Richardson AE, et al. (2020) Loss of protein quality control gene sensitizes to the aminoglycoside hygromycin B. Fine Focus. 6: 76-83 |
Runnebohm AM, Richards KA, Irelan CB, et al. (2020) Overlapping function of Hrd1 and Ste24 in translocon quality control provides robust channel surveillance. The Journal of Biological Chemistry |
Richards KA, Runnebohm A, Dolan M, et al. (2020) Modification of the Endoplasmic Reticulum Translocon Impairs Protein Translocation The Faseb Journal. 34: 1-1 |
Broshar CL, Buchanan B, Mehrtash A, et al. (2020) The relationship between ER stress and protein quality contarol at the translocon The Faseb Journal. 34: 1-1 |
Buchanan BW, Mehrtash AB, Broshar CL, et al. (2019) Endoplasmic reticulum stress differentially inhibits endoplasmic reticulum and inner nuclear membrane protein quality control degradation pathways. The Journal of Biological Chemistry |
Engle SM, Crowder JJ, Watts SG, et al. (2017) Acetylation of N-terminus and two internal amino acids is dispensable for degradation of a protein that aberrantly engages the endoplasmic reticulum translocon. Peerj. 5: e3728 |