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Overview

Andrey Kovalevsky is a researcher affiliated with Oak Ridge National Laboratory in the United States. Their research contributions span biochemistry, genetics, and molecular biology, with a primary focus on molecular biology alongside significant work in computational theory and mathematics, materials chemistry, infectious diseases, and organic chemistry.

The scientist's research topics predominantly cover computational drug discovery methods, protein structure and dynamics, enzyme structure and function, and SARS-CoV-2 and COVID-19 research. Additional areas of work include RNA and protein synthesis mechanisms, biochemical and molecular research, and studies related to cholinesterase and neurodegenerative diseases.

Frequent publication venues for Kovalevsky include the following:

  • Faculty Opinions - Post-Publication Peer Review of the Biomedical Literature
  • Journal of Biological Chemistry
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Acta Crystallographica Section A Foundations and Advances
  • Methods in enzymology on CD-ROM/Methods in enzymology

Some of their recent papers are as follows:

  • Structural plasticity of SARS-CoV-2 3CL Mpro active site cavity revealed by room temperature X-ray crystallography, 2020, Nature Communications
  • Supercomputer-Based Ensemble Docking Drug Discovery Pipeline with Application to Covid-19, 2020, Journal of Chemical Information and Modeling
  • Malleability of the SARS-CoV-2 3CL Mpro Active-Site Cavity Facilitates Binding of Clinical Antivirals, 2020, Structure
  • Unusual zwitterionic catalytic site of SARS-CoV-2 main protease revealed by neutron crystallography, 2020, Journal of Biological Chemistry
  • Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease, 2022, Nature Communications

Collaborations form a significant part of Kovalevsky's research. Frequent co-authors include Daniel W. Kneller, Leighton Coates, Oksana Gerlits, Victoria N. Drago, and G.N. Phillips.

Best Publications

  • Structural plasticity of SARS-CoV-2 3CL M pro active site cavity revealed by room temperature X-ray crystallography.

    Daniel W. Kneller;Gwyndalyn Phillips;Hugh M. O’Neill;Robert Jedrzejczak

  • Photoinduced linkage isomers of transition-metal nitrosyl compounds and related complexes.

    Philip Coppens;Irina Novozhilova;Andrey Kovalevsky

  • Physical and Kinetic Analysis of the Cooperative Role of Metal Ions in Catalysis of Phosphodiester Cleavage by a Dinuclear Zn(II) Complex

    Olga Iranzo;Andrey Y. Kovalevsky;Janet R. Morrow;John P. Richard

  • Structure-based design of novel HIV-1 protease inhibitors to combat drug resistance

    Arun K. Ghosh;Perali Ramu Sridhar;Sofiya Leshchenko;Azhar K. Hussain

  • Metal ion roles and the movement of hydrogen during reaction catalyzed by D-xylose isomerase: a joint x-ray and neutron diffraction study.

    Andrey Y. Kovalevsky;Leif Hanson;S. Zoe Fisher;Marat Mustyakimov

  • Creating nanocavities of tunable sizes: Hollow helices

    Bing Gong;Huaqiang Zeng;Jin Zhu;Lihua Yuan

  • Supercomputer-Based Ensemble Docking Drug Discovery Pipeline with Application to Covid-19.

    A. Acharya;R. Agarwal;R. Agarwal;M. B. Baker;J. Baudry

  • Ultra-high Resolution Crystal Structure of HIV-1 Protease Mutant Reveals Two Binding Sites for Clinical Inhibitor TMC114.

    Andrey Y. Kovalevsky;Fengling Liu;Sofiya Leshchenko;Arun K. Ghosh

  • Covalent narlaprevir- and boceprevir-derived hybrid inhibitors of SARS-CoV-2 main protease

    Unknown

  • Effectiveness of nonpeptide clinical inhibitor TMC-114 on HIV-1 protease with highly drug resistant mutations D30N, I50V, and L90M.

    Andrey Yu. Kovalevsky;Yunfeng Tie;Fengling Liu;Peter I. Boross

  • Amprenavir complexes with HIV-1 protease and its drug-resistant mutants altering hydrophobic clusters.

    Chen-Hsiang Shen;Yuan-Fang Wang;Andrey Y. Kovalevsky;Robert W. Harrison

  • The catalytic mechanism of an aspartic proteinase explored with neutron and X-ray diffraction.

    Leighton Coates;Han-Fang Tuan;Stephen Tomanicek;Andrey Kovalevsky

  • Capturing and Analyzing the Excited-State Structure of a Cu(I) Phenanthroline Complex by Time-Resolved Diffraction and Theoretical Calculations

    Ivan I. Vorontsov;Tim Graber;Andrey Yu. Kovalevsky;Irina V. Novozhilova

  • A new crystal form of human acetylcholinesterase for exploratory room-temperature crystallography studies

    Oksana Gerlits;Kwok-Yiu Ho;Xiaolin Cheng;Donald Blumenthal

  • Effect of flap mutations on structure of HIV-1 protease and inhibition by saquinavir and darunavir.

    Fengling Liu;Andrey Y. Kovalevsky;Yunfeng Tie;Arun K. Ghosh

  • The first photocrystallographic evidence for light-induced metastable linkage isomers of ruthenium sulfur dioxide complexes

    Andrey Yu Kovalevsky;Kimberly A Bagley;Philip Coppens

  • Catalytic asymmetric benzylic C-H activation by means of carbenoid-induced C-H insertions.

    Huw M. L. Davies;Qihui Jin;Pingda Ren;Andrey Yu. Kovalevsky

  • Malleability of the SARS-CoV-2 3CL Mpro Active-Site Cavity Facilitates Binding of Clinical Antivirals

    Daniel W. Kneller;Stephanie Galanie;Gwyndalyn Phillips;Gwyndalyn Phillips;Hugh M. O'Neill;Hugh M. O'Neill

  • Neutron diffraction of acetazolamide-bound human carbonic anhydrase II reveals atomic details of drug binding.

    S.Z Fisher;M Aggarwal;A.Y Kovalevsky;D.N Silverman

  • Unusual zwitterionic catalytic site of SARS-CoV-2 main protease revealed by neutron crystallography.

    Daniel W. Kneller;Daniel W. Kneller;Gwyndalyn Phillips;Gwyndalyn Phillips;Kevin L. Weiss;Kevin L. Weiss;Swati Pant;Swati Pant

  • Atomic resolution crystal structures of HIV‐1 protease and mutants V82A and I84V with saquinavir

    Yunfeng Tie;Andrey Y. Kovalevsky;Peter Boross;Yuan Fang Wang

  • Shedding light on the structure of a photoinduced transient excimer by time-resolved diffraction.

    Ivan I. Vorontsov;Andrey Yu. Kovalevsky;Yu-Sheng Chen;Tim Graber

  • Synthesis and Structure of Multicomponent Crystals of Fullerenes and Metal Tetraarylporphyrins

    Dmitri V. Konarev;Andrey Yu. Kovalevsky;Xue Li;Ivan S. Neretin

Frequent Co-Authors

Paul Langan
Paul Langan Oak Ridge National Laboratory
Philip Coppens
Philip Coppens University at Buffalo, State University of New York
Irene T. Weber
Irene T. Weber Georgia State University
Jeremy C. Smith
Jeremy C. Smith University of Tennessee at Knoxville
David A. Keen
David A. Keen Rutherford Appleton Laboratory
Rimma N. Lyubovskaya
Rimma N. Lyubovskaya Russian Academy of Sciences
Arun K. Ghosh
Arun K. Ghosh Purdue University West Lafayette
Hugh O'Neill
Hugh O'Neill Oak Ridge National Laboratory
John M. Louis
John M. Louis National Institutes of Health
Robert McKenna
Robert McKenna University of Florida

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