selected publications
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article
- Comparative structural and enzymatic studies on Salmonella typhimurium diaminopropionate ammonia lyase reveal its unique features.
- Crystal structure of Escherichia coli diaminopropionate ammonia-lyase reveals mechanism of enzyme activation and catalysis
- Crystal structures of open and closed forms of d -serine deaminase from Salmonella typhimurium - Implications on substrate specificity and catalysis
- Electrospray mass spectrometric characterization of hemoglobin Q (Hb Q-India) and a double mutant hemoglobin S/D in clinical samples
- Fold type II pyridoxal 5′-phosphate dependent enzymes: Structure, substrate recognition and catalysis
- Identification of key amino acid residues in the catalytic mechanism of diaminopropionate ammonialyase from Salmonella typhimurium
- Importance of tyrosine residues of Bacillus stearothermophilus serine hydroxymethyltransferase in cofactor binding and l-allo-Thr cleavage: Crystal structure and biochemical studies
- Mechanistic Insights into the Neutralization of Cytotoxic Abrin by the Monoclonal Antibody D6F10
- Prediction of Protein-Protein Interactions Between Human Host and Two Mycobacterial Organisms.
- Real-time detection of condensin-driven DNA compaction reveals a multistep binding mechanism.
- Real-time imaging of DNA loop extrusion by condensin.
- Structural Basis for a Safety-Belt Mechanism That Anchors Condensin to Chromosomes.
- Structural and functional studies of Bacillus stearothermophilus serine hydroxymethyltransferase: The role of Asn341, Tyr60 nd Phe351 in tetrahydrofolate binding
- Structural and mutational studies on substrate specificity and catalysis of Salmonella typhimurium D-cysteine desulfhydrase
- The condensin complex is a mechanochemical motor that translocates along DNA.