Author

J. C. Bouwer

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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Biophysics· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Organism:E. coli· 2 Approach:experimental assay· 2 Assay:structural biology· 2 Assay:ATAC-seq· 1 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1 Assay:DNA methylation· 1

Frequent Co-Authors

A. J. Oakley· 2 shared H. Ghodke· 2 shared N. E. Dixon· 2 shared S. Jergic· 2 shared Z.-Q. Xu· 2 shared A. C. Pradhan· 1 shared A. G. Stewart· 1 shared A. M. van Oijen· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 27 mutual co-author links

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2 shared papersBiochemistry

A. J. Oakley

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Author profile →

3 papers

Recent·Most cited

Potassium dependent structural changes in the selectivity filter of HERG potassium channels

C. H. Lau, E. Flood, M. J. Hunter, B. J. Williams-Noonan, K. M. Corbett, C.-A. Ng, J. C. Bouwer, A. G. Stewart, E. Perozo, T. W. Allen, J. I. Vandenberg

The paper determines structures of conductive and non-conductive HERG selectivity filters and identifies a mechanism for rapid inactivation kinetics.

bioRxiv · Dec 14, 2023Biophysics

Structural characterisation of the complete cycle of sliding clamp loading in Escherichia coli

Z.-Q. Xu, S. Jergic, A. T. Y. Lo, A. C. Pradhan, S. H. J. Brown, J. C. Bouwer, H. Ghodke, P. J. Lewis, G. Tolun, A. J. Oakley, N. E. Dixon

This study presents six high-resolution structures of the E. coli clamp loader complex (CLC) during the clamp loading process, revealing the molecular mechanism of clamp opening and DNA binding.

bioRxiv · Jul 20, 2023 · PreprintBiochemistry

Mechanism of transcription modulation by the transcription-repair coupling factor

B. P. Paudel, Z.-Q. Xu, S. Jergic, A. J. Oakley, N. Sharma, S. H. Brown, J. C. Bouwer, P. Lewis, N. E. Dixon, A. M. van Oijen, H. Ghodke

This study investigates how the bacterial TRCF Mfd modulates transcription by converting elongation complexes into catalytically poised states and then irreversibly terminating transcription through ATP hydrolysis.

bioRxiv · Apr 2, 2021Biophysics