Author

A.-H. M. Mustafa

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· 1 Cancer Biology· 1 Pharmacology & Toxicology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Assay:proteomics· 3 Research Focus:drug response / drug discovery· 2 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

O. H. Kramer· 2 shared A. G. Kansy· 1 shared A. Leydecker· 1 shared A. Nguyen· 1 shared A. Piee-Staffa· 1 shared B. F. Schmalohr· 1 shared C. Brachetti· 1 shared D. Imhof· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersCancer Biology

O. H. Kramer

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Author profile →

3 papers

Recent·Most cited

Cancer BiologybioRxivPreprintSep 3, 2023

The protein phosphatase-2A subunit PR130 is linked to cytotoxic protein aggregate formation in mesenchymal pancreatic ductal adenocarcinoma cells

O. H. Kramer, A. Nguyen, A. Leydecker…·F. Butter

This study shows that mesenchymal pancreatic ductal adenocarcinoma cells depend on the PP2A subunit PR130, and its inhibition by phendione leads to apoptosis and protein aggregate formation.

DOI 10.1101/2023.09.03.556106

humanproteomics

𝕏 PostBluesky

Pharmacology & ToxicologybioRxivMar 9, 2023

Novel hydroxamic acid derivative induces apoptosis and constrains autophagy in leukemic cells

M. A. Fischer, A.-H. M. Mustafa, K. Hausmann…·O. H. Kramer

This paper synthesizes novel HDAC inhibitors that show nanomolar activity against class I HDACs and induce apoptosis while constraining autophagy in leukemic cells.

DOI 10.1016/j.jare.2023.07.005

humanproteomics

𝕏 PostBluesky

BiochemistrybioRxivAug 13, 2020

Structural insights into the interaction of heme with protein tyrosine kinase JAK2

B. F. Schmalohr, A.-H. M. Mustafa, O. Krämer, D. Imhof

The paper shows heme induces hyperphosphorylation of JAK2 via specific motifs in its kinase domain, suggesting potential for heme-related pharmacological tools in myeloproliferative disorders.

DOI 10.1002/cbic.202000730

humanproteomics

𝕏 PostBluesky