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

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, A.-H. M. Mustafa, J. Murr, 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.

bioRxiv · Sep 3, 2023 · PreprintCancer Biology

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

M. A. Fischer, A.-H. M. Mustafa, K. Hausmann, R. Ashry, A. G. Kansy, M. C. Liebl, C. Brachetti, A. Piee-Staffa, M. Zessin, H. S. Ibrahim, T. G. Hofmann, M. Schutkowski, W. Sippl, 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.

bioRxiv · Mar 9, 2023Pharmacology & Toxicology

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.

bioRxiv · Aug 13, 2020Biochemistry