Author

A. Chitrakar

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· 1 Cell Biology· 1 Microbiology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Assay:bulk RNA-seq· 1 Research Focus:cell signaling & trafficking· 1 Organism:Drosophila· 1 Research Focus:metabolism & bioenergetics· 1 Assay:metabolomics· 1

Frequent Co-Authors

A. Korennykh· 2 shared S. Rath· 2 shared A. Bosque· 1 shared A. M. K. Weideman· 1 shared A. R. Coffey· 1 shared A. R. Ward· 1 shared B. R. Jones· 1 shared B. T. Mann· 1 shared

Activity by Year

2018-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 29 mutual co-author links

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Curved chords = mutual co-authorship

2 shared papersBiophysics

A. Korennykh

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Aminobisphosphonates reactivate the latent reservoir in people living with HIV-1

M. Sanz, A. M. K. Weideman, A. R. Ward, M. L. Clohosey, S. Garcia-Recio, S. R. Selitsky, B. T. Mann, M. A. Iannone, C. P. Whitworth, A. Chitrakar, C. Garrido, J. Kirchherr, A. R. Coffey, Y.- H. Tsai, S. Samir, , N. Soriano-Sarabia

This study shows that aminobisphosphonates reactivate latent HIV-1 in ART-suppressed individuals and activate immune effector cells, but do not significantly reduce the viral reservoir.

bioRxiv · Feb 7, 2023 · PreprintMicrobiology

The Metabolites NADP+ and NADPH are the Targets of the Circadian Protein Nocturnin (Curled)

M. A. Estrella, J. Du, L. Chen, S. Rath, E. Prangley, A. Chitrakar, T. Aoki, P. Schedl, J. Rabinowitz, A. Korennykh

This study identifies NADP+ and NADPH as substrates of the circadian protein Nocturnin, showing its enzymatic activity in converting these metabolites and revealing structural insights into its mechanism.

bioRxiv · Jan 30, 2019Biophysics

Realtime 2-5A kinetics suggests interferons β and {lambda} evade global arrest of translation by RNase L

A. Chitrakar, S. Rath, J. Donovan, K. Demarest, Y. Li, R. Rao Sridhar, S. Weiss, S. Kotenko, N. Wingreen, A. Korennykh

The paper develops a biosensor to study 2-5A kinetics and shows that interferons β and λ evade RNase L-mediated translation arrest during the innate immune response.

bioRxiv · Nov 26, 2018Cell Biology