scispace - formally typeset
V

Valasani Koteswara Rao

Researcher at University of Kansas

Publications -  12
Citations -  413

Valasani Koteswara Rao is an academic researcher from University of Kansas. The author has contributed to research in topics: Docking (molecular) & Gene. The author has an hindex of 7, co-authored 12 publications receiving 341 citations. Previous affiliations of Valasani Koteswara Rao include Sri Venkateswara University.

Papers
More filters
Journal ArticleDOI

Mitochondrial permeability transition pore is a potential drug target for neurodegeneration

TL;DR: The CypD-dependent mPTP is directly linked to the cellular and synaptic perturbations observed in the pathogenesis of AD and designed small molecules to block this interaction would lessen the effects of Aβ neurotoxicity.
Journal ArticleDOI

Identification of substituted [3, 2-a] pyrimidines as selective antiviral agents: molecular modeling study.

TL;DR: The main objective of the present work is to carry out the QSAR studies for all the series of the compounds starting from 4a to 6j to find out their molecular descriptors and predict the biological properties, and to consider these molecules as potential antiviral drugs.
Journal ArticleDOI

Design, Synthesis and Anti Colon Cancer Activity Evaluation of Phosphorylated Derivatives of Lamivudine (3TC)

TL;DR: The novel phosphorylated derivatives of Lamivudine (5a-5l) as potential anti colon cancer agents are synthe- sized and among them 5a and 5b emerged as lead compounds with 0.003 μM and 0.0001 μM values.
Journal ArticleDOI

Cloning and characterization of l-lactate dehydrogenase gene of Staphylococcus aureus.

TL;DR: The lactate dehydrogenase (LDH) gene which catalyzes the formation of lactate was cloned, sequenced, and expressed in Escherichia coli DH5α and the LDH gene sequence "LKDIMA" was found to be conserved in all Gram positive bacteria and in all human LDH isoforms even though only 39% sequence homology was observed with all human LH isoforms.
Journal ArticleDOI

Comparison and correlation of binding mode of ATP in the kinase domains of Hexokinase family.

TL;DR: The analysis revealed that the four ATP binding domains are showing 13 identical, 7 similar and 6 dissimilar residues with similar structural conformation, which probably explains the variable phosphorylation rates among hexokinases family.