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Chemistry

D-Index
59
Citations
9832
World Ranking
10379
National Ranking
2868

Biology and Biochemistry

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60
Citations
10135
World Ranking
12182
National Ranking
5203

Overview

Ben M. Dunn is affiliated with the University of Florida in the United States. Their research primarily falls within the field of Medicine, with a strong focus on Infectious Diseases, Molecular Biology, and Virology. They have contributed to topics including HIV/AIDS drug development and treatment, HIV research and treatment, and HIV/AIDS research and interventions, as well as peptidase inhibition and analysis, glycosylation and glycoproteins research, galectins and cancer biology, and mentoring and academic development.

Ben M. Dunn has published in several academic venues with frequent contributions to:

  • Current Protein and Peptide Science
  • Protein and Peptide Letters
  • bioRxiv (Cold Spring Harbor Laboratory)
  • Biochemistry
  • Journal of AIDS & Clinical Research

Their recent papers include:

  • Preface, 2023, Current Protein and Peptide Science
  • Serine-Carboxyl Peptidases, Sedolisins: From Discovery to Evolution, 2022, Biochemistry
  • Molecular docking-based screening for novel inhibitors of the human immunodeficiency virus type 1 protease that effectively reduce the viral replication in human cells, 2020, bioRxiv (Cold Spring Harbor Laboratory)
  • Role of the Matrix-Capsid Cleavage Site Polymorphism S124V of HIV-1 Sub-subtype A2 in Gag Polyprotein Processing, 2020, bioRxiv (Cold Spring Harbor Laboratory)
  • Molecular Docking-Based Screening for Novel Inhibitors of the Human Immunodeficiency Virus Type 1 Protease that Effectively Reduce the Viral Replication in Human Cells, 2021, Journal of AIDS & Clinical Research

Frequent collaborators in the scientific community include Carla Mavian, Roxana M. Coman, Maureen M. Goodenow, Xinrui Zhang, and Steve Pomeroy. These partnerships have contributed to multiple joint publications and research efforts.

Best Publications

  • Structure and mechanism of the pepsin-like family of aspartic peptidases.

    Ben M. Dunn

  • Effective blocking of HIV-1 proteinase activity by characteristic inhibitors of aspartic proteinases.

    Anthony D. Richards;Ray Roberts;Ben M. Dunn;Mary C. Graves

  • A systematic series of synthetic chromophoric substrates for aspartic proteinases.

    B M Dunn;M Jimenez;B F Parten;M J Valler

  • Sensitive, soluble chromogenic substrates for HIV-1 proteinase.

    A D Richards;L H Phylip;W G Farmerie;P E Scarborough

  • Aspartic peptidase inhibitors: implications in drug development

    Chandravanu Dash;Aarohi Kulkarni;Ben Dunn;Mala Rao

  • Initial Cleavage of the Human Immunodeficiency Virus Type 1 GagPol Precursor by Its Activated Protease Occurs by an Intramolecular Mechanism

    Steven C. Pettit;Lorraine E. Everitt;Sumana Choudhury;Ben M. Dunn

  • Viral proteinases: weakness in strength.

    John Kay;Ben M. Dunn

  • High resolution X-ray analyses of renin inhibitor-aspartic proteinase complexes

    S. I. Foundling;J. Cooper;F. E. Watson;A. Cleasby

  • Quantitative affinity chromatography. Determination of binding constants by elution with competitive inhibitors.

    Ben M. Dunn;Irwin M. Chaiken

  • Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum.

    John B. Dame;G.Roman Reddy;Charles A. Yowell;Ben M. Dunn

  • Different requirements for productive interaction between the active site of HIV-1 proteinase and substrates containing -hydrophobic*hydrophobic- or -aromatic*pro- cleavage sites.

    Jonathan T. Griffiths;Lowri H. Phylip;Jan Konvalinka;Petr Strop

  • High level expression and characterisation of Plasmepsin II, an aspartic proteinase from Plasmodium falciparum

    Jeffrey Hill;Lorraine Tyas;Lowri H. Phylip;John Kay

  • Expression and characterisation of plasmepsin I from Plasmodium falciparum.

    Richard P. Moon;Lorraine Tyas;Ulrich Certa;Katharina Rupp

  • Exploration of subsite binding specificity of human cathepsin D through kinetics and rule-based molecular modeling

    Paula E. Scarborough;Ben M. Dunn;Kunchur Guruprasad;Chris Topham

  • Effect of point mutations on the kinetics and the inhibition of human immunodeficiency virus type 1 protease: relationship to drug resistance.

    Lin Y;Lin X;Hong L;Foundling S

  • Carboxyl proteinase from Pseudomonas defines a novel family of subtilisin-like enzymes

    Alexander Wlodawer;Mi Li;Mi Li;Zbigniew Dauter;Alla Gustchina

  • Structural and enzymatic properties of the sedolisin family of serine-carboxyl peptidases.

    Alexander Wlodawer;M i Li;Alla Gustchina;Hiroshi Oyama

  • The aspartic proteinase from Saccharomyces cerevisiae folds its own inhibitor into a helix.

    Mi Li;Lowri H. Phylip;Wendy E. Lees;Jakob R. Winther

  • Evaluation of quantitative affinity chromatography by comparison with kinetic and equilibrium dialysis methods for the analysis of nucleotide binding to staphylococcal nuclease.

    Ben M. Dunn;Irwin M. Chaiken

  • Comparing the accumulation of active- and nonactive-site mutations in the HIV-1 protease.

    José C Clemente;Rebecca E Moose;Reena Hemrajani;Lisa R S Whitford

Frequent Co-Authors

John Kay
John Kay Cardiff University
Robert McKenna
Robert McKenna University of Florida
John B. Dame
John B. Dame University of Florida
Alexander Wlodawer
Alexander Wlodawer National Institutes of Health
Mavis Agbandje-McKenna
Mavis Agbandje-McKenna University of Florida
Thomas C. Bruice
Thomas C. Bruice University of California, Santa Barbara
Michael W. Pennington
Michael W. Pennington University of Florida
Tom L. Blundell
Tom L. Blundell University of Cambridge
Colin Berry
Colin Berry University of Glasgow
Johan Åqvist
Johan Åqvist Uppsala University

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