Author

R. T. Oshiro

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Microbiology· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Organism:bacteria (other)· 3 Research Focus:cell type annotation· 2 Approach:experimental assay· 2 Research Focus:protein folding & dynamics· 2 Research Focus:differential expression· 1 Research Focus:gene regulatory network inference· 1 Approach:genetic perturbation / CRISPR· 1 Assay:protein structure· 1

Frequent Co-Authors

D. B. Kearns· 3 shared A. V. Yakhnin· 1 shared F. Dempwolff· 1 shared F. J. Gueiros-Filho· 1 shared M. Kashlev· 1 shared P. Babitzke· 1 shared S. C. Jacobson· 1 shared Y. Yu· 1 shared

Activity by Year

2020-2021 · peak 2/yr

Co-Author Collaboration Network

9 top collaborators · 20 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

3 shared papersMicrobiology

D. B. Kearns

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

The division defect of a Bacillus subtilis minD noc double mutant can be suppressed by Spx-dependent and Spx-independent mechanisms

Y. Yu, F. Dempwolff, r. T. oshiro, F. J. Gueiros-Filho, S. C. Jacobson, D. B. Kearns

This study identifies Spx-dependent and Spx-independent mechanisms that suppress division defects in a Bacillus subtilis minD noc double mutant at high temperature.

bioRxiv · May 5, 2021Microbiology

NusG is an intrinsic transcription termination factor that stimulates motility and coordinates global gene expression with NusA

Z. F. Mandell, R. T. Oshiro, A. V. Yakhnin, M. Kashlev, D. B. Kearns, P. Babitzke

This study identifies NusG as an intrinsic termination factor that works with NusA to facilitate termination at most intrinsic terminators and regulates gene expression and motility in Bacillus subtilis.

bioRxiv · Aug 7, 2020Microbiology

Contact with the CsrA core is required for allosteric inhibition by FliW in Bacillus subtilis

D. B. Kearns, R. T. Oshiro

This study identifies FliW residues critical for inhibiting CsrA in Bacillus subtilis and proposes a mechanism involving salt bridge formation and core domain deformation.

bioRxiv · Jul 2, 2020Microbiology