Author

T. Heidebrecht

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· 4

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Approach:statistical model· 2 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1 Assay:structural biology· 1

Frequent Co-Authors

A. Perrakis· 4 shared A. Adamopoulos· 2 shared A. Fish· 2 shared R. Joosten· 2 shared B. van Beusekom· 1 shared D. Ammerlaan· 1 shared D. Geerke· 1 shared E. Pardon· 1 shared

Activity by Year

2018-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 26 mutual co-author links

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4 shared papersBiochemistry

A. Perrakis

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4 papers

Recent·Most cited

Distant sequence regions of JBP1 contribute to J-DNA binding

I. de Vries, D. Ammerlaan, T. Heidebrecht, P. Celie, D. Geerke, R. Joosten, A. Perrakis

The paper investigates how JBP1's JDBD binds to J-DNA using crystal structures, MD simulations, and mutagenesis, revealing the role of the N-terminus in DNA binding.

bioRxiv · Jan 23, 2023Biochemistry

The domain architecture of JBP1 suggests synergy between J-base DNA binding and thymidine hydroxylase activity

A. Adamopoulos, T. Heidebrecht, J. Roosendaal, W. G. Touw, I. Phan, J. Beijnen, A. Perrakis

This paper investigates the domain architecture of JBP1, showing that the JDBD domain enhances thymidine hydroxylation activity by facilitating J-DNA recognition.

bioRxiv · Dec 20, 2018Biochemistry

Lysophosphatidic acid produced by Autotaxin acts as an allosteric modulator of its catalytic efficiency

F. Salgado-Polo, A. Fish, M.-T. Matsoukas, T. Heidebrecht, W.-J. Keune, A. Perrakis

The paper investigates how lysophosphatidic acid (LPA), produced by autotaxin (ATX), modulates its own catalytic efficiency through allosteric regulation.

bioRxiv · Jun 13, 2018Biochemistry

Characterisation and structure determination of a llama-derived nanobody targeting the J-base binding protein 1

B. van Beusekom, T. Heidebrecht, A. Adamopoulos, A. Fish, E. Pardon, J. Steyaert, R. Joosten, A. Perrakis

The paper characterizes a llama-derived nanobody targeting JBP1, showing high affinity and solving its crystal structure to 1.64 Å resolution, with insights into CDR flexibility.

bioRxiv · Jun 7, 2018Biochemistry