Author

P. Keshavan

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

Biochemistry· 2 Biophysics· 2

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 4 Assay:cryo-EM· 3 Research Focus:protein structure prediction· 3 Research Focus:drug response / drug discovery· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Organism:bacteria (other)· 1 Assay:structural biology· 1

Frequent Co-Authors

N. K. Banavali· 3 shared R. K. Agrawal· 3 shared R. K. Koripella· 3 shared A. Deep· 2 shared E. K. Agrawal· 2 shared M. R. Sharma· 2 shared S. Majumdar· 2 shared A. L. Marcinkiewicz· 1 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 40 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 papersBiochemistry

N. K. Banavali

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

The structure of a hibernating ribosome in a Lyme disease pathogen

M. R. Sharma, S. R. Manjari, E. K. Agrawal, P. Keshavan, R. K. Koripella, S. Majumdar, A. L. Marcinkiewicz, Y.-P. Lin, R. K. Agrawal, N. K. Banavali

This study determines the structure of the hibernating ribosome in Borrelia burgdorferi using cryo-EM, revealing new structural features and insights into antibiotic binding.

bioRxiv · Apr 16, 2023Biochemistry

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

S. Majumdar, A. Deep, M. R. Sharma, J. Canestrari, M. Stone, C. Smith, R. K. Koripella, P. Keshavan, N. K. Banavali, J. Wade, T. A. Gray, K. M. Derbyshire, 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.

bioRxiv · Mar 31, 2023 · PreprintBiochemistry

Structures of the human mitochondrial ribosome recycling complexes reveal distinct mechanisms of recycling and antibiotic resistance

R. K. Koripella, A. Deep, E. K. Agrawal, P. Keshavan, N. K. Banavali, R. K. Agrawal

bioRxiv · Dec 20, 2020 · PreprintBiophysics

Structural insights into unique features of the human mitochondrial ribosome recycling

R. Koripella, M. Sharma, P. Risteff, P. Keshavan, R. Agrawal

The paper presents a cryo-EM structure of the human mitoribosome-RRFmt complex, revealing unique structural features and interactions involved in mitoribosome recycling.

bioRxiv · Aug 24, 2018Biophysics