Author

M. Moustakim

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· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:structural biology· 2 Research Focus:drug response / drug discovery· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

A. Chaikuad· 2 shared D. Heidenreich· 2 shared O. Fedorov· 2 shared S. Knapp· 2 shared B. Stauffer· 1 shared C. G. Wilson· 1 shared C. Secor· 1 shared C. Suebsuwong· 1 shared

Activity by Year

2018-2020 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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2 shared papersBiochemistry

A. Chaikuad

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3 papers

Recent·Most cited

Inhibition and Crystal Structure of the Human DHTKD1-Thiamin Diphosphate Complex

J. Leandro, S. Khamrui, H. Wang, C. Suebsuwong, N. S. Nemeria, K. Huynh, M. Moustakim, C. Secor, M. Wang, T. Dodatko, B. Stauffer, C. G. Wilson, C. Yu, M. R. Arkin, F. Jordan, , S. M. Houten

This study identifies DHTKD1 inhibitors and reports its crystal structure with thiamin diphosphate, revealing how mutations affect its function and stability.

bioRxiv · Jan 20, 2020Biochemistry

Structural insights into interaction mechanisms of alternative piperazine-urea YEATS domain binders in MLLT1

X. Ni, D. Heidenreich, T. Christott, J. Bennett, M. Moustakim, P. Brennan, O. Fedorov, S. Knapp, A. Chaikuad

The paper characterizes piperazine-urea derivatives as acetyl/acyl-lysine mimetics for MLLT1 and reveals distinct interaction mechanisms through crystal structures.

bioRxiv · Nov 9, 2019Biochemistry

A structure-based approach towards identification of inhibitory fragments for eleven-nineteen-leukemia protein (ENL) YEATS domain

D. Heidenreich, M. Moustakim, J. Schmidt, D. Merk, P. E. Brennan, O. Fedorov, A. Chaikuad, S. Knapp

The paper identifies inhibitory fragments targeting the ENL YEATS domain using crystallography, providing starting points for chemical probe development.

bioRxiv · Nov 8, 2018Biochemistry