Lloyd L. Ingraham

1.7k total citations
67 papers, 1.3k citations indexed

About

Lloyd L. Ingraham is a scholar working on Molecular Biology, Biochemistry and Organic Chemistry. According to data from OpenAlex, Lloyd L. Ingraham has authored 67 papers receiving a total of 1.3k indexed citations (citations by other indexed papers that have themselves been cited), including 24 papers in Molecular Biology, 13 papers in Biochemistry and 12 papers in Organic Chemistry. Recurrent topics in Lloyd L. Ingraham's work include Enzyme-mediated dye degradation (9 papers), Biochemical Acid Research Studies (8 papers) and Various Chemistry Research Topics (7 papers). Lloyd L. Ingraham is often cited by papers focused on Enzyme-mediated dye degradation (9 papers), Biochemical Acid Research Studies (8 papers) and Various Chemistry Research Topics (7 papers). Lloyd L. Ingraham collaborates with scholars based in United States. Lloyd L. Ingraham's co-authors include Joseph Corse, Fred G. White, Benjamin Makower, Harold J. Bright, David E. Green, Gerald M. Maggiora, Damon L. Meyer, Kenneth L. Brown, Glen F. Bailey and Fred Stitt and has published in prestigious journals such as Nature, Science and Journal of the American Chemical Society.

In The Last Decade

Lloyd L. Ingraham

67 papers receiving 1.1k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Lloyd L. Ingraham United States 21 606 330 182 158 137 67 1.3k
Ulrich Schwieter Switzerland 24 650 1.1× 617 1.9× 267 1.5× 54 0.3× 177 1.3× 89 1.8k
P. Hemmerich Switzerland 14 295 0.5× 249 0.8× 186 1.0× 63 0.4× 72 0.5× 24 973
Börje Wickberg Sweden 23 482 0.8× 713 2.2× 120 0.7× 70 0.4× 142 1.0× 102 1.7k
Carolyn Mottley United States 19 396 0.7× 354 1.1× 196 1.1× 51 0.3× 229 1.7× 32 1.3k
Walter A. Prütz Germany 26 963 1.6× 575 1.7× 149 0.8× 123 0.8× 287 2.1× 43 2.2k
Robert L. VanEtten United States 10 553 0.9× 377 1.1× 195 1.1× 54 0.3× 52 0.4× 18 1.2k
Philip J. Geary United Kingdom 11 879 1.5× 110 0.3× 150 0.8× 180 1.1× 251 1.8× 17 1.5k
Michael H. Klapper United States 24 1.1k 1.9× 317 1.0× 313 1.7× 292 1.8× 79 0.6× 66 2.1k
R. Rüegg Switzerland 27 896 1.5× 994 3.0× 141 0.8× 57 0.4× 158 1.2× 58 2.0k
Carl Niemann United States 26 1.4k 2.3× 616 1.9× 140 0.8× 125 0.8× 87 0.6× 127 2.1k

Countries citing papers authored by Lloyd L. Ingraham

Since Specialization
Citations

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

Fields of papers citing papers by Lloyd L. Ingraham

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Lloyd L. Ingraham. 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 Lloyd L. Ingraham. The network helps show where Lloyd L. Ingraham may publish in the future.

Co-authorship network of co-authors of Lloyd L. Ingraham

This figure shows the co-authorship network connecting the top 25 collaborators of Lloyd L. Ingraham. A scholar is included among the top collaborators of Lloyd L. Ingraham 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 Lloyd L. Ingraham. Lloyd L. Ingraham 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.
Doerge, Daniel R., Mark G. McNamee, & Lloyd L. Ingraham. (1979). Modification of Acetylcholine Receptor-Mediated Ion Permeability by Thiamine. Molecular Pharmacology. 15(3). 747–750. 4 indexed citations
2.
Ingraham, Lloyd L., et al.. (1978). Molecular orbital study of optical rotation in a vitamin B6 enzyme. Journal of Theoretical Biology. 75(4). 503–517. 1 indexed citations
3.
Lowe, James N. & Lloyd L. Ingraham. (1974). An introduction to biochemical reaction mechanisms. Prentice Hall eBooks. 3 indexed citations
4.
Ingraham, Lloyd L.. (1972). The mechanism of proton transfers. Biochimica et Biophysica Acta (BBA) - General Subjects. 279(1). 8–14. 9 indexed citations
5.
Ingraham, Lloyd L., et al.. (1971). Carbenes in sulfur and nitrogen heterocycles: A π‐electron‐scf‐mo study. Journal of Heterocyclic Chemistry. 8(4). 551–556. 8 indexed citations
6.
Ingraham, Lloyd L., et al.. (1970). Acid catalyzed reduction of dihydrothiamine in aqueous dimethylsulfoxide. Journal of Heterocyclic Chemistry. 7(3). 711–712. 1 indexed citations
7.
Ingraham, Lloyd L., et al.. (1970). A dihydrothiamine-like substance. Biochimica et Biophysica Acta (BBA) - General Subjects. 208(2). 343–345. 1 indexed citations
8.
Ingraham, Lloyd L., et al.. (1970). The affinity of flavin semiquinones for certain aromatic compounds and disulfides. Archives of Biochemistry and Biophysics. 139(2). 265–268. 35 indexed citations
9.
Ingraham, Lloyd L. & H. Johansen. (1969). Electronic structure of the proflavine cation. Archives of Biochemistry and Biophysics. 132(1). 205–209. 15 indexed citations
10.
Johansen, Helge & Lloyd L. Ingraham. (1969). Calculation of the electronic structures and spectra for corrin and related compounds. Journal of Theoretical Biology. 23(2). 191–204. 6 indexed citations
11.
Lundin, Robert E., et al.. (1964). Activated Hydrogens in Compounds Related to Thiamine. II*. Biochemistry. 3(8). 1072–1076. 5 indexed citations
12.
Maggiora, Gerald M., et al.. (1964). Molecular Orbital Evidence for Weiss's Oxyhæmoglobin Structure. Nature. 203(4941). 183–184. 55 indexed citations
13.
Bright, Harold J., Robert E. Lundin, & Lloyd L. Ingraham. (1964). A Proton Magnetic Resonance Study of the Stereochemistry of the Methylaspartate Ammonia-Lyase Reaction*. Biochemistry. 3(9). 1224–1230. 11 indexed citations
14.
Bright, Harold J., B. J. Wood, & Lloyd L. Ingraham. (1963). COPPER, TYROSINASE, AND THE KINETIC STABILITY OF OXYGEN. Annals of the New York Academy of Sciences. 100(2). 965–976. 14 indexed citations
15.
Nash, Charles P., et al.. (1961). MECHANISM OF THIAMINE ACTION: A NEW TYPE OF “HIGH ENERGY” BOND. Journal of the American Chemical Society. 83(19). 4106–4107. 8 indexed citations
16.
Ingraham, Lloyd L.. (1957). Variation of the Michaelis Constant in Polyphenol Oxidase Catalyzed Oxidations: Substrate Structure and Concentration. Journal of the American Chemical Society. 79(3). 666–669. 29 indexed citations
17.
Ingraham, Lloyd L.. (1955). Reaction-Inactivation of Polyphenol Oxidase: Catechol and Oxygen Dependence. Journal of the American Chemical Society. 77(10). 2875–2876. 20 indexed citations
18.
Ingraham, Lloyd L., Joseph Corse, & Benjamin Makower. (1952). Enzymatic Browning of Fruits. III. Kinetics of the Reaction Inactivation of Polyphenoloxidase. Journal of the American Chemical Society. 74(10). 2623–2626. 24 indexed citations
19.
Corse, Joseph & Lloyd L. Ingraham. (1951). Enzymatic Browning of Fruits. II. Dissociation Constants of Substituted Catechols. Journal of the American Chemical Society. 73(12). 5706–5707. 7 indexed citations
20.
Ingraham, Lloyd L. & Joseph Corse. (1951). Enzymatic Browning of Fruits. I. Autoxidation of Chlorogenic Acid. Journal of the American Chemical Society. 73(12). 5550–5553. 14 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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