Author

A. K. Saini

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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Pharmacology & Toxicology· 2 Biochemistry· 1 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:drug response / drug discovery· 2 Organism:rat· 2 Research Focus:cell signaling & trafficking· 1 Assay:cryo-EM· 1 Research Focus:host-pathogen & immune response· 1 Assay:metabolomics· 1 Organism:mouse· 1

Frequent Co-Authors

D. Sharma· 2 shared J. Kumar· 2 shared P. Tyagi· 2 shared R. Kumar· 2 shared V. Kumar· 2 shared A. G. Hinnebusch· 1 shared F. Ahmed· 1 shared J. D. Nanda· 1 shared

Activity by Year

2018-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersPharmacology & Toxicology

D. Sharma

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4 papers

Recent·Most cited

Analytical Method Development for Evaluation of Pharmacokinetics and Tissue Distribution of Thiourea-Based Antivirals through nLC/MS-MS

J. Kumar, P. Tyagi, A. K. Saini, D. Sharma, V. Kumar

The paper develops a sensitive nLC-MS/MS method to quantify thiourea derivatives in plasma and tissues of rats, showing good linearity and precision.

bioRxiv · Jun 28, 2023 · PreprintPharmacology & Toxicology

Safety Assessment and Evaluation of Novel Thiourea Derivatives as Antivirals

J. Kumar, P. Tyagi, a. k. saini, D. Sharma, V. Kumar

This paper evaluates the safety of three thiourea derivatives (DSA-00, DSA-02, DSA-09) as antivirals, finding they are non-cytotoxic, non-mutagenic, and have moderate acute toxicity.

bioRxiv · Jun 25, 2023 · PreprintPharmacology & Toxicology

Identification of radiation responsive proteins from Spleen and Intestine tissue of mice using Mass Spectrometry approach.

M. S. Hussain, F. Ahmed, R. Kumar, A. K. Saini, S. Shubham, S. M. Shasthry, M. T. Salman

The paper identifies radiation-responsive proteins in mouse spleen and intestine using mass spectrometry and assesses Podophyllotoxin's protective effect against radiation injury.

bioRxiv · Feb 24, 2020 · PreprintBiochemistry

Translational initiation factor eIF5 replaces eIF1 on the 40S ribosomal subunit to promote start-codon recognition

J. L. Llacer, T. Hussain, A. K. Saini, J. D. Nanda, S. Kaur, Y. Gordiyenko, R. Kumar, A. G. Hinnebusch, J. R. Lorsch, V. Ramakrishnan

The paper presents a cryo-EM structure of a 48S pre-initiation complex showing eIF5's role in promoting start-codon recognition by stabilizing the Met-tRNAi-codon interaction.

bioRxiv · Jul 10, 2018Biophysics