Edwin T. Harper

881 total citations
22 papers, 736 citations indexed

About

Edwin T. Harper is a scholar working on Molecular Biology, Organic Chemistry and Clinical Biochemistry. According to data from OpenAlex, Edwin T. Harper has authored 22 papers receiving a total of 736 indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 6 papers in Organic Chemistry and 4 papers in Clinical Biochemistry. Recurrent topics in Edwin T. Harper's work include Metabolism and Genetic Disorders (4 papers), Enzyme Structure and Function (4 papers) and Amino Acid Enzymes and Metabolism (3 papers). Edwin T. Harper is often cited by papers focused on Metabolism and Genetic Disorders (4 papers), Enzyme Structure and Function (4 papers) and Amino Acid Enzymes and Metabolism (3 papers). Edwin T. Harper collaborates with scholars based in United States. Edwin T. Harper's co-authors include Maurice M. Kreevoy, William Bosron, Robert A. Dean, A. Paul Schaap, Richard M. Kellogg, John W. Hawes, Robert A. Harris, David W. Crabb, Gary M. Smith and Albert S. Mildvan and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Edwin T. Harper

21 papers receiving 696 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Edwin T. Harper United States 12 401 171 153 82 75 22 736
A. Langemann Switzerland 17 347 0.9× 162 0.9× 298 1.9× 57 0.7× 70 0.9× 30 846
Penelope W. Codding Canada 16 342 0.9× 126 0.7× 396 2.6× 94 1.1× 115 1.5× 79 836
Daniel M. Tal Israel 22 855 2.1× 53 0.3× 115 0.8× 77 0.9× 49 0.7× 44 1.1k
L. Dupont Belgium 19 404 1.0× 127 0.7× 622 4.1× 83 1.0× 113 1.5× 132 1.2k
Owen Callaghan United States 15 385 1.0× 73 0.4× 241 1.6× 61 0.7× 32 0.4× 33 827
Leslie S. Jimenez United States 19 413 1.0× 65 0.4× 585 3.8× 75 0.9× 62 0.8× 29 1.0k
Wilfred L.F. Armarego Australia 19 570 1.4× 88 0.5× 476 3.1× 34 0.4× 84 1.1× 90 1.2k
Richard P. Szajewski 7 494 1.2× 89 0.5× 238 1.6× 18 0.2× 57 0.8× 7 798
W.H. Ojala United States 18 368 0.9× 169 1.0× 389 2.5× 86 1.0× 119 1.6× 53 837
Serge Halazy France 20 681 1.7× 57 0.3× 739 4.8× 224 2.7× 68 0.9× 70 1.4k

Countries citing papers authored by Edwin T. Harper

Since Specialization
Citations

This map shows the geographic impact of Edwin T. Harper'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 Edwin T. Harper with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Edwin T. Harper more than expected).

Fields of papers citing papers by Edwin T. Harper

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Edwin T. Harper. 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 Edwin T. Harper. The network helps show where Edwin T. Harper may publish in the future.

Co-authorship network of co-authors of Edwin T. Harper

This figure shows the co-authorship network connecting the top 25 collaborators of Edwin T. Harper. A scholar is included among the top collaborators of Edwin T. Harper 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 Edwin T. Harper. Edwin T. Harper 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.
Hawes, John W. & Edwin T. Harper. (2000). Synthesis of Methacrylyl-CoA and (R)- and (S)-3-Hydroxyisobutyryl-CoA. Methods in enzymology on CD-ROM/Methods in enzymology. 324. 73–79. 1 indexed citations
2.
Hawes, John W., Jerzy Jaśkiewicz, Yoshiharu Shimomura, et al.. (1996). Primary Structure and Tissue-specific Expression of Human β-Hydroxyisobutyryl-coenzyme A Hydrolase. Journal of Biological Chemistry. 271(42). 26430–26434. 39 indexed citations
3.
Hawes, John W., Edwin T. Harper, David W. Crabb, & Robert A. Harris. (1996). Structural and Mechanistic Aspects of a New Family of Dehydrogenases, the β-Hydroxyacid Dehydrogenases. Advances in experimental medicine and biology. 414. 395–402. 4 indexed citations
4.
Hawes, John W., Edwin T. Harper, David W. Crabb, & Robert A. Harris. (1996). Structural and mechanistic similarities of 6‐phosphogluconate and 3‐hydroxyisobutyrate dehydrogenases reveal a new enzyme family, the 3‐hydroxyacid dehydrogenases. FEBS Letters. 389(3). 263–267. 38 indexed citations
5.
Harper, Edwin T., et al.. (1993). Helix stop signals in proteins and peptides: The capping box. Biochemistry. 32(30). 7605–7609. 263 indexed citations
6.
Dean, Robert A., et al.. (1992). Effects of ethanol on cocaine metabolism: Formation of cocaethylene and norcocaethylene. Toxicology and Applied Pharmacology. 117(1). 1–8. 95 indexed citations
7.
Brzezinski, Monica R., et al.. (1992). Convenient Synthesis of Benzoylecgonine Ethyl Ester, a Homolog of Cocaine. Synthetic Communications. 22(7). 1027–1032. 5 indexed citations
8.
Harper, Edwin T., et al.. (1991). Slow reversible inhibition of rabbit muscle aldolase by D-erythrulose 1-phosphate. Biochemical and Biophysical Research Communications. 176(1). 511–516. 7 indexed citations
9.
Cohen, Michael R. & Edwin T. Harper. (1991). Student‐as‐Scientist and scientist‐as‐Student: Changing Models for Learning From Experience. Teaching Education. 3(2). 31–40. 1 indexed citations
10.
Ray, Bruce D., Edwin T. Harper, & Wilmer K. Fife. (1983). Carbon-13 NMR evidence of carbinolamine formation at the active site of an imine-forming aldolase. Journal of the American Chemical Society. 105(11). 3731–3732. 13 indexed citations
11.
Wong, Pierre & Edwin T. Harper. (1982). Selective arylation of cysteine-237 of rabbit muscle aldolase with 4-chloro-7-nitrobenzofurazan. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 700(1). 33–41. 4 indexed citations
12.
Shahed, Asha, et al.. (1981). STIMULATION OF RAT LIVER PHOSPHORYLASE PHOSPHATASE ACTIVITY BY INSULIN. Biochemical Society Transactions. 9(2). 236P–236P. 6 indexed citations
13.
Harper, Edwin T., et al.. (1980). Are aromatic residues essential at the “active sites” of peptide hormones?. Journal of Theoretical Biology. 83(3). 457–467. 13 indexed citations
14.
Harper, Edwin T.. (1973). Kinetics of the two-sited enzyme. Journal of Theoretical Biology. 39(1). 91–102. 10 indexed citations
15.
Harper, Edwin T.. (1971). Kinetics of the two-sited enzyme. Journal of Theoretical Biology. 32(2). 405–414. 12 indexed citations
16.
Kellogg, Richard M., et al.. (1968). Acid-catalyzed brominations, deuterations, rearrangements, and debrominations of thiophenes under mild conditions. The Journal of Organic Chemistry. 33(7). 2902–2909. 69 indexed citations
17.
Harper, Edwin T. & Myron L. Bender. (1965). Intramolecular Catalysis of Ketone Enolization in o-Acylbenzoic Acids1. Journal of the American Chemical Society. 87(24). 5625–5632. 14 indexed citations
18.
Kreevoy, Maurice M., et al.. (1960). Inductive Effects on the Acid Dissociation Constants of Mercaptans1. Journal of the American Chemical Society. 82(18). 4899–4902. 102 indexed citations
19.
Parham, William E., Edwin T. Harper, & Richard Berger. (1960). Heterocyclic Vinyl Ethers. XVIII. Unsymmetrical 2,5-Diaryl-1,4-dithiadienes1. Journal of the American Chemical Society. 82(18). 4932–4936. 12 indexed citations
20.
Parham, William E. & Edwin T. Harper. (1960). Heterocyclic Vinyl Ethers. XIX. Unsymmetrical 2,4-Diarylthiophenes1. Journal of the American Chemical Society. 82(18). 4936–4939. 4 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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