David E. Ash

4.0k total citations
69 papers, 3.2k citations indexed

About

David E. Ash is a scholar working on Biochemistry, Molecular Biology and Clinical Biochemistry. According to data from OpenAlex, David E. Ash has authored 69 papers receiving a total of 3.2k indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Biochemistry, 25 papers in Molecular Biology and 18 papers in Clinical Biochemistry. Recurrent topics in David E. Ash's work include Amino Acid Enzymes and Metabolism (30 papers), Metabolism and Genetic Disorders (18 papers) and Nitric Oxide and Endothelin Effects (15 papers). David E. Ash is often cited by papers focused on Amino Acid Enzymes and Metabolism (30 papers), Metabolism and Genetic Disorders (18 papers) and Nitric Oxide and Endothelin Effects (15 papers). David E. Ash collaborates with scholars based in United States, Germany and France. David E. Ash's co-authors include David W. Christianson, Z.F. Kanyo, Laura R. Scolnick, David W. Christianson, Diana M. Colleluori, Joseph J. Villafranca, Frances A. Emig, Frederick C. Wedler, J. David Cox and Vern L. Schramm and has published in prestigious journals such as Nature, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

David E. Ash

69 papers receiving 3.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
David E. Ash United States 33 1.4k 988 718 603 358 69 3.2k
David Maltby United States 33 2.5k 1.8× 380 0.4× 297 0.4× 175 0.3× 603 1.7× 67 3.9k
Gary Cecchini United States 41 3.9k 2.8× 369 0.4× 284 0.4× 595 1.0× 322 0.9× 112 5.6k
Jean‐Luc Boucher France 34 1.2k 0.9× 723 0.7× 1.6k 2.2× 215 0.4× 114 0.3× 115 4.4k
William Furey United States 38 2.0k 1.5× 1.5k 1.5× 246 0.3× 581 1.0× 924 2.6× 86 6.2k
S. Turley United States 27 1.7k 1.2× 324 0.3× 194 0.3× 486 0.8× 160 0.4× 43 2.9k
Menico Rizzi Italy 39 2.6k 1.9× 360 0.4× 299 0.4× 630 1.0× 102 0.3× 119 4.4k
Johannes Everse United States 27 1.7k 1.3× 263 0.3× 491 0.7× 396 0.7× 169 0.5× 73 3.4k
Alexandre Samouilov United States 28 856 0.6× 642 0.6× 2.2k 3.0× 448 0.7× 76 0.2× 62 4.3k
Thomas Nowak United States 28 1.9k 1.4× 255 0.3× 248 0.3× 587 1.0× 200 0.6× 89 3.1k
Nechama S. Kosower Israel 40 3.1k 2.3× 1.2k 1.2× 1.1k 1.5× 203 0.3× 141 0.4× 118 6.0k

Countries citing papers authored by David E. Ash

Since Specialization
Citations

This map shows the geographic impact of David E. Ash'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 David E. Ash with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites David E. Ash more than expected).

Fields of papers citing papers by David E. Ash

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by David E. Ash. 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 David E. Ash. The network helps show where David E. Ash may publish in the future.

Co-authorship network of co-authors of David E. Ash

This figure shows the co-authorship network connecting the top 25 collaborators of David E. Ash. A scholar is included among the top collaborators of David E. Ash 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 David E. Ash. David E. Ash 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
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Kepka‐Lenhart, Diane, David E. Ash, & Sidney M. Morris. (2008). Determination of Mammalian Arginase Activity. Methods in enzymology on CD-ROM/Methods in enzymology. 440. 221–230. 29 indexed citations
4.
Colleluori, Diana M., Frances A. Emig, E. Cama, et al.. (2005). Probing the role of the hyper-reactive histidine residue of arginase. Archives of Biochemistry and Biophysics. 444(1). 15–26. 13 indexed citations
5.
Emig, Frances A., et al.. (2002). Functional Consequences of the G235R Mutation in Liver Arginase Leading to Hyperargininemia. Archives of Biochemistry and Biophysics. 399(1). 49–55. 4 indexed citations
6.
Brigham‐Burke, Michael, et al.. (2001). Subunit-Subunit Interactions in Trimeric Arginase. Journal of Biological Chemistry. 276(17). 14242–14248. 48 indexed citations
7.
Colleluori, Diana M., Sidney M. Morris, & David E. Ash. (2001). Expression, Purification, and Characterization of Human Type II Arginase. Archives of Biochemistry and Biophysics. 389(1). 135–143. 51 indexed citations
8.
Ash, David E., et al.. (1998). Molecular Basis of Hyperargininemia: Structure-Function Consequences of Mutations in Human Liver Arginase. Molecular Genetics and Metabolism. 64(4). 243–249. 32 indexed citations
9.
Kanyo, Z.F., Laura R. Scolnick, David E. Ash, & David W. Christianson. (1996). Structure of a unique binuclear manganese cluster in arginase. Nature. 383(6600). 554–557. 352 indexed citations
10.
Soprano, Dianne Robert, et al.. (1996). Chemical Modification and Inactivation of Rat Liver Arginase byN-Bromosuccinimide: Reaction with His141. Archives of Biochemistry and Biophysics. 327(1). 107–112. 13 indexed citations
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Merkler, David J., Raviraj Kulathila, & David E. Ash. (1995). The Inactivation of Bifunctional Peptidylglycine α-Amidating Enzyme by Benzylhydrazine: Evidence That the Two Enzyme-Bound Copper Atoms Are Nonequivalent. Archives of Biochemistry and Biophysics. 317(1). 93–102. 16 indexed citations
13.
Khangulov, Sergei V., Peter J. Pessiki, V.V. Barynin, David E. Ash, & G. Charles Dismukes. (1995). Determination of the Metal Ion Separation and Energies of the Three Lowest Electronic States of Dimanganese(II,II) Complexes and Enzymes: Catalase and Liver Arginase. Biochemistry. 34(6). 2015–2025. 114 indexed citations
14.
Daghigh, Faeze, Jon M. Fukuto, & David E. Ash. (1994). Inhibition of Rat Liver Arginase by an Intermediate in NO Biosynthesis, NG-Hydroxy-L-arginine: Implications for the Regulation of Nitric Oxide Biosynthesis by Arginase. Biochemical and Biophysical Research Communications. 202(1). 174–180. 139 indexed citations
15.
Ash, David E., et al.. (1994). Rat Liver Arginase: Kinetic Mechanism, Alternate Substrates, and Inhibitors. Archives of Biochemistry and Biophysics. 312(1). 31–37. 154 indexed citations
16.
Burke, Carl J., et al.. (1994). Mutagenesis of Rat Liver Arginase Expressed in Escherichia coli: Role of Conserved Histidines. Biochemistry. 33(35). 10652–10657. 77 indexed citations
17.
Farrington, G. King, et al.. (1993). Threonine Synthase of Escherichia coli: Inhibition by Classical and Slow-Binding Analogues of Homoserine Phosphate. Archives of Biochemistry and Biophysics. 307(1). 165–174. 21 indexed citations
18.
Kanyo, Z.F., et al.. (1992). Crystallization and oligomeric structure of rat liver arginase. Journal of Molecular Biology. 224(4). 1175–1177. 30 indexed citations
19.
Hoober, J. Kenneth, Albert Kahn, David E. Ash, Simon P. Gough, & C. Gamini Kannangara. (1988). Biosynthesis of Δ-aminolevulinate in greening barley leaves. IX. Structure of the substrate, mode of gabaculine inhibition, and the catalytic mechanism of glutamate 1-semialdehyde aminotransferase. Carlsberg Research Communications. 53(1). 11–25. 81 indexed citations
20.
Jewell, Mark L., et al.. (1979). Aliphatic ketones are acetylcholinesterase inhibitors but not transition state analogs. Biochimica et Biophysica Acta (BBA) - Enzymology. 569(1). 23–30. 5 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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