World's Best Scientists 2026 revealed!
Richard N. Armstrong

Richard N. Armstrong

D-Index & Metrics

Chemistry

D-Index
58
Citations
10469
World Ranking
10766
National Ranking
2960

Biology and Biochemistry

D-Index
58
Citations
11051
World Ranking
13274
National Ranking
5651

Research.com Recognitions

  • 2002 - Fellow of the American Association for the Advancement of Science (AAAS)
  • 1981 - Fellow of the Royal Society of Canada

Overview

Richard N. Armstrong is affiliated with Vanderbilt University in the United States. Their research primarily spans the fields of Biochemistry, Genetics and Molecular Biology as well as Immunology and Microbiology. Within these broader domains, Armstrong has contributed notably to Molecular Biology, Immunology, Genetics, and Oncology subfields.

The scientist's work covers multiple topics including RNA modifications and cancer, blood disorders and treatments, immunodeficiency and autoimmune disorders, CAR-T cell therapy research, CRISPR and genetic engineering, immune cell function and interaction, and neutrophil, myeloperoxidase and oxidative mechanisms.

Armstrong has coauthored works frequently with colleagues such as Hongbing Li, Houtan Moshiri, Yigal Dror, Mariana Benicio, and John E. Dick.

Their recent publication record includes the following papers:

  • CRISPR/Cas9-Mediated Foxp1 Silencing Restores Immune Surveillance in an Immunocompetent A20 Lymphoma Model, 2020, Frontiers in Oncology
  • Germline PTPN13 mutations in patients with bone marrow failure and acute lymphoblastic leukemia, 2022, Leukemia
  • Aberrant early hematopoietic progenitor formation marks the onset of hematopoietic defects in Shwachman-Diamond syndrome, 2024, European Journal Of Haematology
  • Erythropoiesis Failure in Diamond-Blackfan Anemia Starts at the Oligopotent Common Myeloid and Megakaryocyte-Erythroid Progenitor Stage, 2020, Blood
  • Cellular and Molecular Analysis of Hematopoietic Stem and Progenitor Cells in Shwachman-Diamond Syndrome, 2023, Blood

Armstrong commonly publishes in venues such as Blood, Frontiers in Oncology, European Journal Of Haematology, Leukemia, and Genetics in Medicine Open.

Among recognitions in their career, Armstrong has been named Fellow of the American Association for the Advancement of Science (AAAS) in 2002 and Fellow of the Royal Society of Canada in 1981.

Best Publications

  • Structure, catalytic mechanism, and evolution of the glutathione transferases.

    Richard N. Armstrong

  • Structure determination and refinement of human alpha class glutathione transferase A1-1, and a comparison with the Mu and Pi class enzymes.

    I. Sinning;G. J. Kleywegt;S. W. Cowan;P. Reinemer

  • The three-dimensional structure of a glutathione S-transferase from the mu gene class. Structural analysis of the binary complex of isoenzyme 3-3 and glutathione at 2.2-A resolution.

    Xinhua Ji;Pinghui Zhang;Richard N. Armstrong;Gary L. Gilliland

  • Glutathione S-transferases: reaction mechanism, structure, and function

    Richard N. Armstrong

  • Three-dimensional structure, catalytic properties, and evolution of a sigma class glutathione transferase from squid, a progenitor of the lens S-crystallins of cephalopods.

    Xinhua Ji;E. C. Van Rosenvinge;W. W. Johnson;S. I. Tomarev

  • Insights into enzyme structure and dynamics elucidated by amide H/D exchange mass spectrometry

    Laura S. Busenlehner;Richard N. Armstrong

  • Impact of spliceosome mutations on RNA splicing in myelodysplasia: dysregulated genes/pathways and clinical associations

    Andrea Pellagatti;Richard N. Armstrong;Violetta Steeples;Eshita Sharma

  • Mechanistic diversity in a metalloenzyme superfamily.

    Richard N. Armstrong

  • Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase

    Gerard F. Graminski;Yasuo Kubo;Richard N. Armstrong

  • The catalytic mechanism of microsomal epoxide hydrolase involves an ester intermediate

    Gerard M. Lacourciere;Richard N. Armstrong

  • The Enzyme Function Initiative

    John A. Gerlt;Karen N. Allen;Steven C. Almo;Richard N. Armstrong

  • FosB, a Cysteine-Dependent Fosfomycin Resistance Protein under the Control of ςW, an Extracytoplasmic-Function ς Factor in Bacillus subtilis

    Min Cao;Bryan A. Bernat;Zhepeng Wang;Richard N. Armstrong

  • Fosfomycin resistance protein (FosA) is a manganese metalloglutathione transferase related to glyoxalase I and the extradiol dioxygenases.

    Bryan A. Bernat;and L. Timothy Laughlin;Richard N. Armstrong

  • Dissection of the catalytic mechanism of isozyme 4-4 of glutathione S-transferase with alternative substrates.

    Wen Jian Chen;Gerard F. Graminski;Richard N. Armstrong

  • Magnetic resonance and kinetic studies of the manganese(II) ion and substrate complexes of the catalytic subunit of adenosine 3',5'-monophosphate dependent protein kinase from bovine heart.

    Richard Neil Armstrong;Hiroki Kondo;Joseph Granot;E. T. Kaiser

  • Tyrosine 115 participates both in chemical and physical steps of the catalytic mechanism of a glutathione S-transferase.

    W. W. Johnson;Suxing Liu;Xinhua Ji;G. L. Gilliland

  • Parallel evolutionary pathways for glutathione transferases: structure and mechanism of the mitochondrial class kappa enzyme rGSTK1-1.

    Jane E Ladner;James F Parsons;Chris L Rife;Gary L Gilliland

  • Structure and function of the xenobiotic substrate binding site of a glutathione S-transferase as revealed by X-ray crystallographic analysis of product complexes with the diastereomers of 9-(S-glutathionyl)-10-hydroxy-9,10-dihydrophenanthrene.

    Xinhua Ji;William W. Johnson;Muctarr A. Sesay;Laura Dickert

  • Mechanistic Diversity of Fosfomycin Resistance in Pathogenic Microorganisms

    Kerry L Fillgrove;Svetlana Pakhomova;Marcia E Newcomer;Richard N Armstrong

  • Fosfomycin resistance proteins: a nexus of glutathione transferases and epoxide hydrolases in a metalloenzyme superfamily.

    Rachel E Rigsby;Kerry L Fillgrove;Lauren A Beihoffer;Richard N Armstrong

  • Spectroscopic and kinetic evidence for the thiolate anion of glutathione at the active site of glutathione S-transferase [Erratum to document cited in CA110(19):169169n]

    Gerard F. Graminski;Yasuo Kubo;Richard N. Armstrong

Frequent Co-Authors

Gary L. Gilliland
Gary L. Gilliland National Institute of Standards and Technology
Ralf Morgenstern
Ralf Morgenstern Karolinska Institute
Xinhua Ji
Xinhua Ji National Institutes of Health
Patricia C. Babbitt
Patricia C. Babbitt University of California, San Francisco
Joshua Telser
Joshua Telser Roosevelt University
Per-Johan Jakobsson
Per-Johan Jakobsson Karolinska University Hospital
Brian K. Shoichet
Brian K. Shoichet University of California, San Francisco
Jeffrey L. Benovic
Jeffrey L. Benovic Thomas Jefferson University
Heidi E. Hamm
Heidi E. Hamm Vanderbilt University
Eric P. Skaar
Eric P. Skaar Vanderbilt University Medical Center

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