Santosh Panjikar

This study identifies how SpNanR activates sialic acid metabolism in S. pneumoniae by binding N-acetylmannosamine-6-phosphate, stabilizing its tetramer and enhancing transcription of the nan and siaA operons.

The paper introduces a method to extract directional electron-density features from diffraction data using spherical-harmonic decomposition, revealing chemically interpretable dipolar features in crystallographic maps.

This study identifies Plasmodium aspartyl-tRNA synthetase as an antimalarial target by showing how natural products inhibit protein translation through reaction hijacking.

This study solves the structure of the TRAP substrate-binding protein AaSiaP in different conformations, revealing how it binds N-acetylneuraminate and stabilizes a closed state.

This study elucidates how NanR represses sialic acid metabolism in E. coli by showing its cooperative DNA binding and allosteric regulation by N-acetylneuraminate.