Author

K. M. Derbyshire

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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Microbiology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Assay:proteomics· 2 Organism:bacteria (other)· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:host-pathogen & immune response· 1 Organism:mouse· 1 Assay:structural biology· 1

Frequent Co-Authors

T. A. Gray· 3 shared J. T. Wade· 2 shared A. Deep· 1 shared A. H. Dills· 1 shared A. Upadhyay· 1 shared C. A. Z. Rokicki· 1 shared C. Smith· 1 shared E. Lasek-Nesselquist· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 21 mutual co-author links

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3 shared papersMicrobiology

T. A. Gray

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Author profile →

3 papers

Recent·Most cited

BiochemistrybioRxivPreprintMar 31, 2023

The small mycobacterial ribosomal protein, bS22, modulates aminoglycoside accessibility to its 16S rRNA helix-44 binding site

S. Majumdar, A. Deep, M. R. Sharma…·R. K. Agrawal

This study shows that the mycobacterial ribosomal protein bS22 modulates aminoglycoside binding to the 16S rRNA helix-44 site, influencing antibiotic resistance.

DOI 10.1101/2023.03.31.535098

structural biologyexperimental assay

𝕏 PostBluesky

MicrobiologybioRxivFeb 17, 2021

Fluorescence Imaging-Based Discovery of Membrane Domain-Associated Proteins in Mycobacterium smegmatis

C. A. Z. Rokicki, J. R. Brenner, A. H. Dills…·Y. S. Morita

The paper uses fluorescence imaging to verify and discover new proteins associated with the intracellular membrane domain in Mycobacterium smegmatis.

DOI 10.1128/jb.00419-21

bacteria (other)proteomics

𝕏 PostBluesky

MicrobiologybioRxivMar 7, 2020

Leaderless short ORFs in mycobacteria comprise a translational regulon

J. G. Canestrari, E. Lasek-Nesselquist, A. Upadhyay…·T. A. Gray

The paper identifies leaderless short ORFs in mycobacteria as functional translational regulators that control operon expression in response to cysteine availability.

DOI 10.1111/mmi.14498

mouseproteomics

𝕏 PostBluesky