A. V. Krivitskaya

Molecular modeling of ceftriaxone activation in the active sites of penicillin-binding proteins 2

A. V. Krivitskaya, M. G. Khrenova, 2022, Russian Chemical Bulletin.

The QM/MM-QTAIM approach reveals the nature of the different reactivity of cephalosporins in the active site of L1 metallo-β-lactamase

V. Tsirelson, M. Khrenova, A. V. Krivitskaya, 2019, New Journal of Chemistry.

Influence of the Active Site Flexibility on the Efficiency of Substrate Activation in the Active Sites of Bi-Zinc Metallo-β-Lactamases

M. Khrenova, A. V. Krivitskaya, 2022, Molecules.

Interplay between the Enamine and Imine Forms of the Hydrolyzed Imipenem in the Active Sites of Metallo-β-lactamases and in Water Solution

M. Khrenova, A. V. Krivitskaya, 2022, J. Chem. Inf. Model..

Physicochemical characterization of ribavirin with spectroscopy and molecular modeling

R. R. Ibragimova, I. A. Belova, K. Kienskaya, 2020, PROCEEDINGS OF INTERNATIONAL CONFERENCE ON RECENT TRENDS IN MECHANICAL AND MATERIALS ENGINEERING: ICRTMME 2019.

Evolution of Ceftriaxone Resistance of Penicillin-Binding Proteins 2 Revealed by Molecular Modeling

M. Khrenova, A. V. Krivitskaya, 2022, International journal of molecular sciences.

Boronic Acids as Prospective Inhibitors of Metallo-β-Lactamases: Efficient Chemical Reaction in the Enzymatic Active Site Revealed by Molecular Modeling

M. Khrenova, A. V. Krivitskaya, 2021, Molecules.

Two Sides of Quantum-Based Modeling of Enzyme-Catalyzed Reactions: Mechanistic and Electronic Structure Aspects of the Hydrolysis by Glutamate Carboxypeptidase

A. Nemukhin, M. Khrenova, A. V. Krivitskaya, 2021, Molecules.

Full Structure Modeling of Three-Domains Monooxygenase CYP102A1 ВМ3 from Bacillus megaterium

V. Urlacher, M. Khrenova, P. D. Parshin, 2020, Moscow University Chemistry Bulletin.

Admissible sampling time to stabilize a shaft in radial active magnetic bearings

V.S. Voronkov, A.V. Krivitskaya, A. V. Krivitskaya, 2005, Proceedings. 2005 International Conference Physics and Control, 2005..