Author

M. H. Glickman

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biochemistry· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Assay:proteomics· 4 Research Focus:protein folding & dynamics· 3 Research Focus:cell signaling & trafficking· 2 Organism:human· 2

Frequent Co-Authors

I. Sahu· 2 shared N. Reis· 2 shared A. Brik· 1 shared A. Rozenberg· 1 shared A. Sinha· 1 shared A. Thakur· 1 shared B. E. Lemma· 1 shared C. Seok· 1 shared

Activity by Year

2019-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersBiochemistry

I. Sahu

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4 papers

Recent·Most cited

A role for the proteasome alpha2 subunit N-tail in substrate processing

I. Sahu, M. Bajorek, T. Xiaolin, M. Srividya, D. Krutauz, N. Reis, P. A. Osmulski, M. E. Gaczynska, M. H. Glickman

This study investigates the role of the proteasome alpha2 subunit N-tail in substrate processing by analyzing mutations and their effects on proteolysis.

bioRxiv · Jan 11, 2023 · PreprintBiochemistry

ECPAS/Ecm29-Mediated 26S Proteasome Disassembly Is an Adaptive Response to Glucose Starvation

W. H. Choi, Y. Yun, I. Byun, S. Lee, J. Sim, S. Levi, S. Kim, S. H. Park, J. Jun, K. P. Kim, Y. T. Kwon, D. Han, T. Chiba, C. Seok, M. H. Glickman, M. J. Lee

This study shows that ECPAS-mediated 26S proteasome disassembly into 20S and 19S subcomplexes occurs during glucose starvation, enhancing proteolysis and cell survival.

bioRxiv · Jun 6, 2022Biochemistry

Rub1/NEDD8, a ubiquitin-like modifier, is also a ubiquitin modifier

S. Zerath Gurevich, A. Sinha, J. Longworth, R. K. Singh, B. E. Lemma, A. Thakur, O. Popp, D. Kornitzer, N. Reis, M. Scheffner, G. Dittmar, E. Pick, D. Fushman, M. H. Glickman

This paper shows that a single amino acid swap at position 72 can switch the substrate specificity of Rub1/NEDD8 and ubiquitin, revealing their distinct roles in cellular modification pathways.

bioRxiv · Jun 18, 2020 · PreprintBiochemistry

Signature activities of 20S proteasome include degradation of the ubiquitin-tag with the protein under hypoxia

I. Sahu, S. M. Mali, P. Sulkshane, A. Rozenberg, C. Xu, R. Morag, M. P. Sahoo, S. K. Singh, Z. Ding, Y. Wang, S. Day, Y. Cong, O. Kleifeld, A. Brik, M. H. Glickman

The paper identifies the 20S proteasome's ability to degrade ubiquitin-tagged proteins under hypoxia and shows its role in improving cell survival.

bioRxiv · Dec 20, 2019 · PreprintBiochemistry