Elizabeth Heyde

511 total citations
23 papers, 444 citations indexed

About

Elizabeth Heyde is a scholar working on Molecular Biology, Cell Biology and Materials Chemistry. According to data from OpenAlex, Elizabeth Heyde has authored 23 papers receiving a total of 444 indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 9 papers in Cell Biology and 8 papers in Materials Chemistry. Recurrent topics in Elizabeth Heyde's work include Enzyme Structure and Function (8 papers), Biochemical and Molecular Research (7 papers) and Protein Structure and Dynamics (6 papers). Elizabeth Heyde is often cited by papers focused on Enzyme Structure and Function (8 papers), Biochemical and Molecular Research (7 papers) and Protein Structure and Dynamics (6 papers). Elizabeth Heyde collaborates with scholars based in Australia and United Kingdom. Elizabeth Heyde's co-authors include John F. Morrison, Stanley Ainsworth, C. C. Heyde, Les Copeland, Stuart R. Stone, Peter R. Andrews, S. Venkataraman, Richard I. Christopherson and Julian I. Rood and has published in prestigious journals such as Journal of Biological Chemistry, Annual Review of Biochemistry and Biochemistry.

In The Last Decade

Elizabeth Heyde

23 papers receiving 384 citations

Peers

Elizabeth Heyde

BIOCH

C. M. Anderson Australia

Ira E. Smiley United States

Paul J. Lentz United States

Y Anraku Japan

Beulah M. Woodfin United States

N.A. Aldanova Russia

Hubert G. Britton United Kingdom

Robert M. Fink United States

J.M. van der Laan Netherlands

Paolo Dell’Antone Italy

C. M. Anderson Australia

Elizabeth Heyde

409 ×1.5

216 ×1.9

66 ×0.6

BIOCH

91 ×0.9

23 ×0.5

Citations per year, relative to Elizabeth Heyde Elizabeth Heyde (= 1×) peers C. M. Anderson

Countries citing papers authored by Elizabeth Heyde

Since Specialization

Citations

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

Fields of papers citing papers by Elizabeth Heyde

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Elizabeth Heyde. 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 Elizabeth Heyde. The network helps show where Elizabeth Heyde may publish in the future.

Co-authorship network of co-authors of Elizabeth Heyde

This figure shows the co-authorship network connecting the top 25 collaborators of Elizabeth Heyde. A scholar is included among the top collaborators of Elizabeth Heyde 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 Elizabeth Heyde. Elizabeth Heyde is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Christopherson, Richard I., Elizabeth Heyde, & John F. Morrison. (1983). Chorismate mutase-prephenate dehydrogenase from Escherichia coli: spatial relationship of the mutase and dehydrogenase sites. Biochemistry. 22(7). 1650–1656. 9 indexed citations

Rood, Julian I., et al.. (1982). Characterization of Monofunctional Chorismate Mutase/Prephenate Dehydrogenase Enzymes Obtained via Mutagenesis of Recombinant Plasmids in vitro. European Journal of Biochemistry. 124(3). 513–519. 13 indexed citations

Stone, Stuart R., Elizabeth Heyde, & Les Copeland. (1980). Glutamate dehydrogenase of lupin nodules: Kinetics of the amination reaction. Archives of Biochemistry and Biophysics. 199(2). 560–571. 20 indexed citations

Andrews, Peter R. & Elizabeth Heyde. (1979). A common active site model for catalysis by chorismate mutase-prephenate dehydrogenase. Journal of Theoretical Biology. 78(3). 393–403. 9 indexed citations

Heyde, Elizabeth. (1979). Chorismate mutase-prephenate dehydrogenase from Aerobacter aerogenes: evidence that the two reactions occur at one active site. Biochemistry. 18(13). 2766–2775. 22 indexed citations

Heyde, Elizabeth & John F. Morrison. (1978). Kinetic studies on the reactions catalyzed by chorismate mutase-prephenate dehydrogenase from Aerobacter aerogenes. Biochemistry. 17(8). 1573–1580. 34 indexed citations

Heyde, Elizabeth & John F. Morrison. (1976). Studies on inosine monophosphate dehydrogenase. Isotope exchange at equilibrium. Biochimica et Biophysica Acta (BBA) - Enzymology. 429(3). 661–671. 10 indexed citations

Heyde, Elizabeth. (1976). A unifying concept for the active site region in aspartate transcarbamylase. Biochimica et Biophysica Acta (BBA) - Enzymology. 452(1). 81–88. 13 indexed citations

Heyde, Elizabeth. (1973). Difficulties encountered with an ultrafiltration method for measuring the binding of ligands to protein. Analytical Biochemistry. 51(1). 61–66. 16 indexed citations

10.

Heyde, Elizabeth, et al.. (1973). Mechanism of the reaction catalyzed by the catalytic subunit of aspartate transcarbamylase. Kinetic studies with acetyl phosphate as substrate. Biochemistry. 12(23). 4727–4732. 7 indexed citations

11.

Heyde, Elizabeth, et al.. (1973). Mechanism of the Reaction Catalyzed by the Catalytic Subunit of Asparate Transcarbamylase. Kinetic Studies with Carbamyl Phosphate as Substrate. Biochemistry. 12(23). 4718–4726. 34 indexed citations

12.

Heyde, Elizabeth, et al.. (1973). Enzyme forms produced from aspartate transcarbamoylase by digestion with trypsin. Biochemical Journal. 135(1). 125–132. 12 indexed citations

13.

Heyde, Elizabeth. (1973). Interaction between polypeptide chains within the catalytic subunit of aspartate transcarbamylase. Biochimica et Biophysica Acta (BBA) - Enzymology. 293(2). 351–358. 10 indexed citations

14.

Morrison, John F. & Elizabeth Heyde. (1972). Enzymic Phosphoryl Group Transfer. Annual Review of Biochemistry. 41(1). 29–54. 79 indexed citations

15.

Heyde, C. C. & Elizabeth Heyde. (1971). Stochastic fluctuations in a one substrate one product enzyme system: Are they ever relevant?. Journal of Theoretical Biology. 30(2). 395–404. 12 indexed citations

16.

Heyde, Elizabeth & John F. Morrison. (1970). Studies on the inhibition of ATP: Creatine phosphotransferase by NaCl. Biochimica et Biophysica Acta (BBA) - Enzymology. 212(2). 288–299. 14 indexed citations

17.

Heyde, C. C. & Elizabeth Heyde. (1969). A stochastic approach to a one substrate, one product enzyme reaction in the initial velocity phase. Journal of Theoretical Biology. 25(1). 159–172. 22 indexed citations

18.

Heyde, Elizabeth & John F. Morrison. (1969). The interaction of Mg2+ and ATP4− with ATP:creatine phosphotransferase. Biochimica et Biophysica Acta (BBA) - Enzymology. 178(1). 47–60. 9 indexed citations

19.

Heyde, Elizabeth & Stanley Ainsworth. (1968). Kinetic Studies on the Mechanism of the Malate Dehydrogenase Reaction. Journal of Biological Chemistry. 243(9). 2413–2423. 39 indexed citations

20.

Heyde, Elizabeth & Stanley Ainsworth. (1968). A reappraisal of some structural features of bovine heart malate dehydrogenase. Biochemical Journal. 109(4). 663–668. 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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