Author

A. Witecka

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· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Research Focus:cell type annotation· 1 Research Focus:protein folding & dynamics· 1 Organism:rat· 1

Frequent Co-Authors

J. Drozak· 2 shared A. K. Jagielski· 1 shared H. Deng· 1 shared H. Guo· 1 shared H. Li· 1 shared H. Ma· 1 shared J. Hintzen· 1 shared J. Mecinovic· 1 shared

Activity by Year

2021-2021 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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2 shared papersBiochemistry

J. Drozak

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2 papers

Recent·Most cited

Substrate Specificity for Human Histidine Methyltransferase SETD3

J. Hintzen, H. Ma, H. Deng, A. Witecka, S. B. Andersen, J. Drozak, H. Guo, P. Qian, H. Li, J. Mecinovic

This study investigates the substrate specificity of human SETD3, showing it can methylate histidine and its mimics, with histidine being the most efficient substrate.

bioRxiv · Dec 30, 2021 · PreprintBiochemistry

The Mammalian Cytosolic Type 2 (R)-β-hydroxybutyrate Dehydrogenase (BDH2) is 4-oxo-L-proline Reductase (EC1.1.1.104)

S. P. Kwiatkowski, M. Bozko, M. Zarod, A. Witecka, A. K. Jagielski, J. Drozak

This paper identifies BDH2 as the enzyme responsible for reducing 4-oxo-L-proline to cis-4-hydroxy-L-proline, challenging the previous belief that it produces trans-4-hydroxy-L-proline.

bioRxiv · Feb 23, 2021 · PreprintBiochemistry