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Biology and Biochemistry

D-Index
61
Citations
15295
World Ranking
11242
National Ranking
863

Overview

K. Ravi Acharya is affiliated with the University of Bath in the United Kingdom. Their research spans a range of topics primarily within biochemistry, molecular biology, and medicine, with a focus on enzyme structure, function, and inhibition.

Their recent publications cover several areas related to enzyme biology and the renin-angiotensin system. Notable papers include:

  • "ACE2 and ACE: structure-based insights into mechanism, regulation and receptor recognition by SARS-CoV," published in 2020 in Clinical Science
  • "Charcot-Leyden crystal protein/galectin-10 interacts with cationic ribonucleases and is required for eosinophil granulogenesis," published in 2020 in Journal of Allergy and Clinical Immunology
  • "Angiotensin-converting enzyme open for business: structural insights into the subdomain dynamics," published in 2020 in FEBS Journal
  • "Advances in the structural basis for angiotensin-1 converting enzyme (ACE) inhibitors," published in 2024 in Bioscience Reports
  • "ACE-domain selectivity extends beyond direct interacting residues at the active site," published in 2020 in Biochemical Journal

The main research fields for Acharya include Biochemistry, Genetics and Molecular Biology with 37 publications, and Medicine with 29 publications. Subfields of particular focus are Molecular Biology, Neurology, Computational Theory and Mathematics, Cellular and Molecular Neuroscience, and Materials Chemistry.

The topics central to their work include:

  • Computational Drug Discovery Methods
  • Enzyme function and inhibition
  • Botulinum Toxin and Related Neurological Disorders
  • Enzyme Structure and Function
  • Renin-Angiotensin System Studies
  • Hereditary Neurological Disorders
  • Neurological disorders and treatments

Acharya frequently publishes in several journals with multiple contributions, including FEBS Journal, Biomolecules, Journal of Medicinal Chemistry, Toxins, and Journal of Biological Chemistry.

They have collaborated regularly with several researchers, among the most frequent co-authors are Kyle S. Gregory, Edward D. Sturrock, Gyles E. Cozier, Otsile O. Mojanaga, and Sai Liu. These collaborations suggest a research network focused on enzymology and related biochemical areas.

Best Publications

  • ANG mutations segregate with familial and 'sporadic' amyotrophic lateral sclerosis

    Matthew J Greenway;Peter M Andersen;Carsten Russ;Sean Ennis

  • Eosinophil granule proteins: form and function.

    K. Ravi Acharya;Steven J. Ackerman

  • Botulinum and tetanus neurotoxins: structure, function and therapeutic utility

    Kathryn Turton;John A Chaddock;K.Ravi Acharya

  • The CCN family of proteins: structure-function relationships.

    Kenneth P. Holbourn;K. Ravi Acharya;Bernard Perbal;Bernard Perbal

  • ACE revisited: A new target for structure-based drug design

    K. Ravi Acharya;Edward D. Sturrock;James F. Riordan;Mario R. W. Ehlers

  • Refined structure of baboon alpha-lactalbumin at 1.7 A resolution. Comparison with C-type lysozyme.

    K.R. Acharya;D.I. Stuart;N.P.C. Walker;M. Lewis

  • Crystal Structures of Apo- and Holo-bovine α-Lactalbumin at 2.2-Å Resolution Reveal an Effect of Calcium on Inter-lobe Interactions

    E D Chrysina;K Brew;K R Acharya

  • Structural Details on the Binding of Antihypertensive Drugs Captopril and Enalaprilat to Human Testicular Angiotensin I-Converting Enzyme

    Ramanathan Natesh;Sylva L. U. Schwager;Hazel R. Evans;Edward D. Sturrock

  • Crystal structure of human α-lactalbumin at 1·7 Å resolution

    K. Ravi Acharya;Jingshan Ren;David I. Stuart;David C. Phillips

  • Crystal structures of guinea-pig, goat and bovine α-lactalbumin highlight the enhanced conformational flexibility of regions that are significant for its action in lactose synthase

    Ashley C.W. Pike;Keith Brew;K. Ravi Acharya

  • Angiotensin-Converting Enzyme-2 (ACE2): Comparative Modeling of the Active Site, Specificity Requirements, and Chloride Dependence †

    Jodie L. Guy;Richard M. Jackson;K. Ravi Acharya;Edward D. Sturrock

  • Structural basis of superantigen action inferred from crystal structure of toxic-shock syndrome toxin-1.

    K R Acharya;E F Passalacqua;E Y Jones;K Harlos

  • Structural basis for the recognition of carbohydrates by human galectin-7.

    D.D. Leonidas;E.H. Vatzaki;H. Vorum;J.E. Celis

  • Crystal Structure of the N Domain of Human Somatic Angiotensin I-Converting Enzyme Provides a Structural Basis for Domain-Specific Inhibitor Design.

    Hazel R. Corradi;Sylva L.U. Schwager;Aloysius T. Nchinda;Edward D. Sturrock

  • Identification of the protein receptor binding site of botulinum neurotoxins B and G proves the double-receptor concept

    Andreas Rummel;Timo Eichner;Tanja Weil;Tino Karnath

  • Crystal structure of human Charcot-Leyden crystal protein, an eosinophil lysophospholipase, identifies it as a new member of the carbohydrate-binding family of galectins.

    Demetrios D Leonidas;Boris L Elbert;Zeqi Zhou;Hakon Leffler

  • Human angiogenin is a neuroprotective factor and amyotrophic lateral sclerosis associated angiogenin variants affect neurite extension/pathfinding and survival of motor neurons

    Vasanta Subramanian;Benedict Crabtree;K. Ravi Acharya

  • Molecular Recognition and Regulation of Human Angiotensin-I Converting Enzyme (Ace) Activity by Natural Inhibitory Peptides.

    Geoffrey Masuyer;Sylva L. U. Schwager;Edward D. Sturrock;R. Elwyn Isaac

  • The advantages and limitations of protein crystal structures

    K. Ravi Acharya;Matthew D. Lloyd

  • Crystal structure of the superantigen enterotoxin C2 from Staphylococcus aureus reveals a zinc-binding site.

    Anastassios C Papageorgiou;K.Ravi Acharya;Robert Shapiro;Edward F Passalacqua

Frequent Co-Authors

Keith Brew
Keith Brew Florida Atlantic University
Barry V. L. Potter
Barry V. L. Potter University of Oxford
Steven J. Ackerman
Steven J. Ackerman University of Illinois at Chicago
Socrates J. Tzartos
Socrates J. Tzartos Institut Pasteur
Michael J. Reed
Michael J. Reed Imperial College London
Robert Shapiro
Robert Shapiro New York University
Pierre Corvol
Pierre Corvol Collège de France
Mark H. Wilcox
Mark H. Wilcox University of Leeds
Petra C. F. Oyston
Petra C. F. Oyston Defence Science and Technology Laboratory
Gerd Döring
Gerd Döring University of Tübingen

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