Richard N. Armstrong

9.6k total citations · 1 hit paper
142 papers, 7.4k citations indexed

About

Richard N. Armstrong is a scholar working on Molecular Biology, Biochemistry and Pharmacology. According to data from OpenAlex, Richard N. Armstrong has authored 142 papers receiving a total of 7.4k indexed citations (citations by other indexed papers that have themselves been cited), including 107 papers in Molecular Biology, 25 papers in Biochemistry and 22 papers in Pharmacology. Recurrent topics in Richard N. Armstrong's work include Glutathione Transferases and Polymorphisms (63 papers), Genomics, phytochemicals, and oxidative stress (34 papers) and Pharmacogenetics and Drug Metabolism (22 papers). Richard N. Armstrong is often cited by papers focused on Glutathione Transferases and Polymorphisms (63 papers), Genomics, phytochemicals, and oxidative stress (34 papers) and Pharmacogenetics and Drug Metabolism (22 papers). Richard N. Armstrong collaborates with scholars based in United States, United Kingdom and Sweden. Richard N. Armstrong's co-authors include Gary L. Gilliland, Xinhua Ji, Pinghui Zhang, Laura S. Busenlehner, Gerard F. Graminski, Bryan A. Bernat, L. Timothy Laughlin, Gerard M. Lacourciere, E. T. Kaiser and Heini W. Dirr and has published in prestigious journals such as Chemical Reviews, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Richard N. Armstrong

140 papers receiving 7.2k citations

Hit Papers

Structure, Catalytic Mech... 1997 2026 2006 2016 1997 250 500 750
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. Structure, Catalytic Mechanism, and Evolution of the Glutathione Transferases
    1997 938 citations Richard N. Armstrong profile →

Peers — A (Enhanced Table)

Peers by citation overlap · career bar shows stage (early→late) cites · hero ref

Name h Career Trend Papers Cites
Richard N. Armstrong United States 45 5.7k 1.1k 833 594 497 142 7.4k
Marcia E. Newcomer United States 41 3.4k 0.6× 210 0.2× 552 0.7× 663 1.1× 332 0.7× 102 5.7k
Sherry L. Mowbray Sweden 42 3.8k 0.7× 258 0.2× 521 0.6× 545 0.9× 249 0.5× 111 5.3k
Kazuo Nagai Japan 48 4.1k 0.7× 531 0.5× 163 0.2× 955 1.6× 1.1k 2.1× 202 7.0k
Kenji Takahashi Japan 36 3.6k 0.6× 251 0.2× 264 0.3× 319 0.5× 592 1.2× 269 5.7k
Peter Macheroux Austria 49 4.9k 0.9× 383 0.4× 693 0.8× 1.1k 1.9× 331 0.7× 205 7.1k
Francis Johnson United States 42 4.5k 0.8× 457 0.4× 169 0.2× 2.3k 3.8× 628 1.3× 236 7.6k
Patrick M. Woster United States 43 5.8k 1.0× 480 0.4× 1.7k 2.0× 612 1.0× 688 1.4× 136 7.5k
Santosh Panjikar Australia 34 2.8k 0.5× 363 0.3× 187 0.2× 649 1.1× 230 0.5× 151 4.6k
Heidi R. Bokesch United States 25 5.4k 1.0× 607 0.6× 447 0.5× 3.7k 6.2× 2.0k 4.1× 61 10.9k
Xiaoguang Lei China 42 4.5k 0.8× 338 0.3× 299 0.4× 2.1k 3.6× 568 1.1× 208 7.5k

Countries citing papers authored by Richard N. Armstrong

Since Specialization
Citations

This map shows the geographic impact of Richard N. Armstrong's research. It shows the number of citations coming from papers published by authors working in each country. You can also color the map by specialization and compare the number of citations received by Richard N. Armstrong with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Richard N. Armstrong more than expected).

Fields of papers citing papers by Richard N. Armstrong

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Richard N. Armstrong. Nodes represent research fields, and links connect fields that are likely to share authors. Colored nodes show fields that tend to cite the papers produced by Richard N. Armstrong. The network helps show where Richard N. Armstrong may publish in the future.

Co-authorship network of co-authors of Richard N. Armstrong

This figure shows the co-authorship network connecting the top 25 collaborators of Richard N. Armstrong. A scholar is included among the top collaborators of Richard N. Armstrong based on the total number of citations received by their joint publications. Widths of edges represent the number of papers authors have co-authored together. Node borders signify the number of papers an author published with Richard N. Armstrong. Richard N. Armstrong is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

20 of 20 papers shown
1.
Lim, Yeon Jung, Ronit Elhasid, Francisco A. Bonilla, et al.. (2022). Germline PTPN13 mutations in patients with bone marrow failure and acute lymphoblastic leukemia. Leukemia. 36(8). 2132–2135. 2 indexed citations
2.
Yip, Bon Ham, Violetta Steeples, Emmanouela Repapi, et al.. (2017). The U2AF1S34F mutation induces lineage-specific splicing alterations in myelodysplastic syndromes. Journal of Clinical Investigation. 127(6). 2206–2221. 70 indexed citations
3.
Lavallée, Vincent‐Philippe, Patrick Gendron, Geneviève Boucher, et al.. (2015). Mutational and Transcriptomic Landscape of AML with Core-Binding Factor Rearrangements. Blood. 126(23). 802–802. 2 indexed citations
4.
Gerlt, J.A., Karen N. Allen, Steven C. Almo, et al.. (2011). The Enzyme Function Initiative. Biochemistry. 50(46). 9950–9962. 141 indexed citations
5.
Brown, Daniel W., Matthew R. Schaab, William R. Birmingham, & Richard N. Armstrong. (2009). Evolution of the Antibiotic Resistance Protein, FosA, Is Linked to a Catalytically Promiscuous Progenitor. Biochemistry. 48(9). 1847–1849. 15 indexed citations
6.
Codreanu, Simona G., et al.. (2005). Influence of the Dimer Interface on Glutathione Transferase Structure and Dynamics Revealed by Amide H/D Exchange Mass Spectrometry. Biochemistry. 44(31). 10605–10612. 14 indexed citations
7.
Stourman, Nina V., James Rose, Stéphane Vuilleumier, & Richard N. Armstrong. (2003). Catalytic Mechanism of Dichloromethane Dehalogenase from Methylophilus sp. Strain DM11. Biochemistry. 42(37). 11048–11056. 20 indexed citations
8.
Armstrong, Richard N. & Constance S. Cassidy. (2000). NEW STRUCTURAL AND CHEMICAL INSIGHT INTO THE CATALYTIC MECHANISM OF EPOXIDE HYDROLASES*. Drug Metabolism Reviews. 32(3-4). 327–338. 33 indexed citations
9.
Luo, Jiann-Kae, Julie M. Stevens, Louise Wallace, et al.. (2000). Equilibrium Folding of Dimeric Class μ Glutathione Transferases Involves a Stable Monomeric Intermediate. Biochemistry. 39(40). 12336–12344. 46 indexed citations
10.
Bernat, Bryan A., L. Timothy Laughlin, & Richard N. Armstrong. (1999). Elucidation of a Monovalent Cation Dependence and Characterization of the Divalent Cation Binding Site of the Fosfomycin Resistance Protein (FosA). Biochemistry. 38(23). 7462–7469. 39 indexed citations
11.
Armstrong, Richard N.. (1999). KINETIC AND CHEMICAL MECHANISM OF EPOXIDE HYDROLASE*. Drug Metabolism Reviews. 31(1). 71–86. 38 indexed citations
12.
Parsons, James F., Gaoyi Xiao, Gary L. Gilliland, & Richard N. Armstrong. (1998). Enzymes Harboring Unnatural Amino Acids:  Mechanistic and Structural Analysis of the Enhanced Catalytic Activity of a Glutathione Transferase Containing 5-Fluorotryptophan,. Biochemistry. 37(18). 6286–6294. 42 indexed citations
13.
Laughlin, L. Timothy, Bryan A. Bernat, & Richard N. Armstrong. (1998). Mechanistic imperative for the evolution of a metalloglutathione transferase of the vicinal oxygen chelate superfamily. Chemico-Biological Interactions. 111-112. 41–50. 14 indexed citations
14.
15.
Armstrong, Richard N.. (1994). Glutathione S‐Transferases: Structure and Mechanism of an Archetypical Detoxication Enzyme. Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects. 69. 1–44. 71 indexed citations
16.
17.
Liu, Suxing, Xinhua Ji, Gary L. Gilliland, Walter J. Stevens, & Richard N. Armstrong. (1993). Second-sphere electrostatic effects in the active site of glutathione S-transferase. Observation of an on-face hydrogen bond between the side chain of threonine 13 and the .pi.-cloud of tyrosine 6 and its influence on catalysis. Journal of the American Chemical Society. 115(17). 7910–7911. 43 indexed citations
18.
Zhang, Pinghui, Gerard F. Graminski, & Richard N. Armstrong. (1991). Are the histidine residues of glutathione S-transferase important in catalysis? An assessment by 13C NMR spectroscopy and site-specific mutagenesis.. Journal of Biological Chemistry. 266(29). 19475–19479. 30 indexed citations
19.
20.
Armstrong, Richard N.. (1987). Enzyme-Catalyzed Detoxication Reactions: Mechanisms and Stereochemistr. PubMed. 22(1). 39–88. 94 indexed citations

Rankless uses publication and citation data sourced from OpenAlex, an open and comprehensive bibliographic database. While OpenAlex provides broad and valuable coverage of the global research landscape, it—like all bibliographic datasets—has inherent limitations. These include incomplete records, variations in author disambiguation, differences in journal indexing, and delays in data updates. As a result, some metrics and network relationships displayed in Rankless may not fully capture the entirety of a scholar's output or impact.

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