Author

M. H. Tatham

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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Cell Biology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Organism:human· 3 Assay:proteomics· 3 Research Focus:cell signaling & trafficking· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

R. T. Hay· 2 shared A. F. Ibrahim· 1 shared A. Rojas-Fernandez· 1 shared B. Mojsa· 1 shared C. Kampmeyer· 1 shared E. Branigan· 1 shared E. G. Jaffray· 1 shared G. Ball· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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2 shared papersCell Biology

R. T. Hay

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Author profile →

3 papers

Recent·Most cited

Cell BiologybioRxivJan 15, 2023

PML mutants resistant to arsenic induced degradation fail to generate the appropriate SUMO and ubiquitin signals required for RNF4 and p97 recruitment

R. T. Hay, E. G. Jaffray, M. H. Tatham…·A. F. Ibrahim

The paper investigates arsenic resistance in PML mutants by analyzing SUMO and ubiquitin signaling and their impact on RNF4 and p97 recruitment.

DOI 10.1083/jcb.202407133

humanproteomics

𝕏 PostBluesky

BiochemistrybioRxivDec 8, 2022

Lysine deserts prevent adventitious ubiquitylation of ubiquitin-proteasome components

C. Kampmeyer, M. Gronbaek-Thygesen, N. Oelerich…·R. Hartmann-Petersen

The paper identifies lysine deserts in UPS proteins and shows that introducing lysines increases ubiquitylation, with functional consequences for protein stability and function.

DOI 10.1007/s00018-023-04782-z

humanproteomics

𝕏 PostBluesky

Cell BiologybioRxivDec 22, 2020

Identification of SUMO targets required to maintain human stem cells in the pluripotent state.

B. Mojsa, M. H. Tatham, L. Davidson…·R. T. Hay

This study identifies SUMO targets critical for maintaining human pluripotency by using a SUMO inhibitor and SUMOylation site mapping in hiPSCs.

DOI 10.1016/j.mcpro.2021.100164

humanproteomics

𝕏 PostBluesky