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Biology and Biochemistry

D-Index
58
Citations
13782
World Ranking
13075
National Ranking
5575

Overview

David S. Waugh is affiliated with the National Institutes of Health in the United States. Their research primarily focuses on biochemistry, genetics, and molecular biology, with a significant body of work spreading across related subfields including molecular biology, genetics, public health, environmental and occupational health, organic chemistry, and biochemistry.

The main topics covered in Waugh's research include:

  • Mosquito-borne diseases and control
  • RNA and protein synthesis mechanisms
  • Cancer therapeutics and mechanisms
  • Phenothiazines and benzothiazines synthesis and activities
  • Synthesis and catalytic reactions
  • Polyamine metabolism and applications
  • Amino acid enzymes and metabolism

Waugh has contributed to several recent papers spanning various journals and areas of study. Selected publications include:

  • "Small molecule microarray identifies inhibitors of tyrosyl-DNA phosphodiesterase 1 that simultaneously access the catalytic pocket and two substrate binding sites," 2021, Chemical Science
  • "Characterization of a broadly specific cadaverine N-hydroxylase involved in desferrioxamine B biosynthesis in Streptomyces sviceus," 2021, PLoS ONE
  • "Specificity Studies of the Venezuelan Equine Encephalitis Virus Non-Structural Protein 2 Protease Using Recombinant Fluorescent Substrates," 2020, International Journal of Molecular Sciences
  • "Self-inhibited State of Venezuelan Equine Encephalitis Virus (VEEV) nsP2 Cysteine Protease: A Crystallographic and Molecular Dynamics Analysis," 2023, Journal of Molecular Biology
  • "Sustainable and effective antimicrobial surface based on cellulose thin films," 2022, arXiv (Cornell University)

Frequent co-authors collaborating with Waugh include:

  • G.T. Lountos
  • Joseph E. Tropea
  • D. Needle
  • Gyula Hoffka
  • József Tőzsér

Waugh regularly publishes in specialized venues such as:

  • Faculty Opinions - Post-Publication Peer Review of the Biomedical Literature
  • Chemical Science
  • PLoS ONE
  • Journal of Molecular Biology
  • International Journal of Molecular Sciences

Best Publications

  • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused.

    Rachel B. Kapust;David S. Waugh

  • Tobacco etch virus protease: mechanism of autolysis and rational design of stable mutants with wild-type catalytic proficiency.

    Rachel B. Kapust;József Tözsér;Jeffrey D. Fox;D.Eric Anderson

  • Expression and Purification of Soluble His 6 -Tagged TEV Protease

    Joseph E. Tropea;Scott Cherry;David S. Waugh

  • The P1' specificity of tobacco etch virus protease.

    Rachel B Kapust;József Tözsér;Terry D Copeland;David S Waugh

  • An overview of enzymatic reagents for the removal of affinity tags

    David S. Waugh

  • Crystallographic and Modeling Studies of RNase III Suggest a Mechanism for Double-Stranded RNA Cleavage

    Jaroslaw Blaszczyk;Joseph E. Tropea;Mikhail Bubunenko;Karen M. Routzahn

  • Structural basis for the substrate specificity of tobacco etch virus protease.

    Jason Phan;Alexander Zdanov;Artem G. Evdokimov;Joseph E. Tropea

  • Structural Insight into the Mechanism of Double-Stranded RNA Processing by Ribonuclease III

    Jianhua Gan;Joseph E. Tropea;Brian P. Austin;Donald L. Court

  • The 8-nucleotide-long RNA:DNA hybrid is a primary stability determinant of the RNA polymerase II elongation complex.

    Maria L. Kireeva;Natalia Komissarova;David S. Waugh;Mikhail Kashlev

  • Controlled intracellular processing of fusion proteins by TEV protease.

    Rachel B. Kapust;David S. Waugh

  • Gateway vectors for the production of combinatorially-tagged His6-MBP fusion proteins in the cytoplasm and periplasm of Escherichia coli

    Sreedevi Nallamsetty;Brian P. Austin;Kerri J. Penrose;David S. Waugh

  • Solubility-enhancing proteins MBP and NusA play a passive role in the folding of their fusion partners.

    Sreedevi Nallamsetty;David S. Waugh

  • Crystal structure of plant aspartic proteinase prophytepsin: inactivation and vacuolar targeting.

    Jukka Kervinen;Gregory J. Tobin;Júlia Costa;David S. Waugh

  • Single amino acid substitutions on the surface of Escherichia coli maltose-binding protein can have a profound impact on the solubility of fusion proteins

    Jeffrey D. Fox;Rachel B. Kapust;David S. Waugh

  • Unusual molecular architecture of the Yersinia pestis cytotoxin YopM: a leucine-rich repeat protein with the shortest repeating unit.

    Evdokimov Ag;Anderson De;Routzahn Km;Waugh Ds

  • The structure of Yersinia pestis V-antigen, an essential virulence factor and mediator of immunity against plague.

    Urszula Derewenda;Agnieszka Mateja;Yancho Devedjiev;Karen M. Routzahn

  • Noncatalytic Assembly of Ribonuclease III with Double-Stranded RNA

    Jaroslaw Blaszczyk;Jianhua Gan;Joseph E Tropea;Donald L Court

  • Efficient site-specific processing of fusion proteins by tobacco vein mottling virus protease in vivo and in vitro.

    Sreedevi Nallamsetty;Rachel B. Kapust;József Tözsér;Scott Cherry

  • Differential effects of short affinity tags on the crystallization of Pyrococcus furiosus maltodextrin-binding protein.

    Matthew H. Bucher;Artem G. Evdokimov;David S. Waugh

  • Maltodextrin-binding proteins from diverse bacteria and archaea are potent solubility enhancers

    Jeffrey D. Fox;Karen M. Routzahn;Matthew H. Bucher;David S. Waugh

Frequent Co-Authors

Xinhua Ji
Xinhua Ji National Institutes of Health
Terrence R. Burke
Terrence R. Burke National Institutes of Health
Ruth Nussinov
Ruth Nussinov National Institutes of Health
Yves Pommier
Yves Pommier National Institutes of Health
Buyong Ma
Buyong Ma Shanghai Jiao Tong University
Guanghong Wei
Guanghong Wei Fudan University
Robert H. Shoemaker
Robert H. Shoemaker National Institutes of Health
Terry D. Copeland
Terry D. Copeland National Institutes of Health
Donald L. Court
Donald L. Court National Institutes of Health
Natasha J. Caplen
Natasha J. Caplen National Institutes of Health

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