All Stories

  1. Physicochemical and functional characterization of a biosimilar adalimumab ZRC-3197

    Article • Biosimilars, December 2014, Taylor & Francis

    Dr Sanjay Bandyopadhyay, Mr Ajit Kumar Gupta, Mukesh Mahajan, Arun Singh

  2. Reflex

    Article • December 2012, Springer Science + Business Media

    Dr Sanjay Bandyopadhyay

  3. The α 3 (βMet 222 Ser/Tyr 345 Trp) 3 γ Subcomplex of the TF 1 -ATPase Does Not Hydolyze ATP at a Significant Rate until the Substrate Binds to the Catalytic Site of the Lowest Affinity †

    Article • Biochemistry, May 2006, American Chemical Society (ACS)

    Dr Sanjay Bandyopadhyay

  4. The Characteristics of the (αV 371 C) 3 (βR 337 C) 3 γ Double Mutant Subcomplex of the TF 1 -ATPase Indicate that the Catalytic Site at the α TP −β TP Interface with Bound MgADP in Crystal Structures of MF 1 Represents a Catalytic Site Containing Inhi...

    Article • Biochemistry, February 2005, American Chemical Society (ACS)

    Dr Sanjay Bandyopadhyay

  5. γM 23 K, γM 232 K, and γL 77 K Single Substitutions in the TF 1 -ATPase Lower ATPase Activity by Disrupting a Cluster of Hydrophobic Side Chains †

    Article • Biochemistry, July 2004, American Chemical Society (ACS)

    Dr Sanjay Bandyopadhyay

  6. The Ionic Track in the F 1 -ATPase from the Thermophilic Bacillus PS3 †

    Article • Biochemistry, March 2004, American Chemical Society (ACS)

    Dr Sanjay Bandyopadhyay

  7. The βG 156 C Substitution in the F 1 -ATPase from the Thermophilic Bacillus PS3 Affects Catalytic Site Cooperativity by Destabilizing the Closed Conformation of the Catalytic Site †

    Article • Biochemistry, December 2002, American Chemical Society (ACS)

    Dr Sanjay Bandyopadhyay

  8. The (αF 357 C) 3 (βR 372 C) 3 γ Subcomplex of the F 1 -ATPase from the Thermophilic Bacillus PS3 Has Altered ATPase Activity after Cross-Linking α and β Subunits at Noncatalytic Site Interfaces †

    Article • Biochemistry, March 2002, American Chemical Society (ACS)

    Dr Sanjay Bandyopadhyay