Author

S. D. Bruner

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 Biophysics· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Organism:E. coli· 2 Approach:statistical model· 2 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:comparative / phylogenetic analysis· 1 Approach:experimental assay· 1 Research Focus:gene regulatory network inference· 1 Research Focus:metabolism & bioenergetics· 1

Frequent Co-Authors

A. D. Hanson· 2 shared M. A. Wilson· 2 shared O. Fiehn· 2 shared A. AngerhoferiD· 1 shared A. Bar-Even· 1 shared A. F. Yakunin· 1 shared A. M. Thamm· 1 shared C. Lerma-Ortiz· 1 shared

Activity by Year

2018-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 31 mutual co-author links

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2 shared papersMicrobiology

A. D. Hanson

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Metabolite Damage and Damage-Control in a Minimal Genome

D. Haas, A. M. Thamm, J. Sun, L. Huang, L. Sun, G. A. W. Beaudoin, K. S. Wise, C. Lerma-Ortiz, S. D. Bruner, M. Breuer, Z. Luthey-Schulten, J. Lin, M. A. Wilson, G. Brown, A. F. Yakunin, , V. de Crecy-Lagard

The paper identifies and validates genes involved in metabolite damage repair and preemption in the minimized Mycoplasma JCVI-Syn3A genome and extends its metabolic map.

bioRxiv · Dec 1, 2021Microbiology

Thioproline formation as a driver of formaldehyde toxicity in Escherichia coli

J. A. Patterson, H. He, J. S. Folz, Q. Lee, M. A. Wilson, O. Fiehn, S. D. Bruner, A. Bar-Even, A. D. Hanson

This study identifies thioproline formation as a key contributor to formaldehyde toxicity in E. coli and suggests PepP as a potential damage-control enzyme.

bioRxiv · Mar 19, 2020Biochemistry

The Structure of Oxalate Decarboxylase at its Active pH

M. J. Burg, J. L. Goodsell, U. T. Twahir, S. D. Bruner, A. Angerhofer

This paper reports the crystal structure of oxalate decarboxylase at its active pH, revealing a flexible loop region and insights into substrate binding and catalysis.

bioRxiv · Sep 25, 2018 · PreprintBiophysics