Richard F. Parrish

870 total citations
29 papers, 764 citations indexed

About

Richard F. Parrish is a scholar working on Molecular Biology, Cell Biology and Reproductive Medicine. According to data from OpenAlex, Richard F. Parrish has authored 29 papers receiving a total of 764 indexed citations (citations by other indexed papers that have themselves been cited), including 14 papers in Molecular Biology, 7 papers in Cell Biology and 4 papers in Reproductive Medicine. Recurrent topics in Richard F. Parrish's work include Enzyme function and inhibition (6 papers), Redox biology and oxidative stress (5 papers) and Hemoglobin structure and function (4 papers). Richard F. Parrish is often cited by papers focused on Enzyme function and inhibition (6 papers), Redox biology and oxidative stress (5 papers) and Hemoglobin structure and function (4 papers). Richard F. Parrish collaborates with scholars based in United States. Richard F. Parrish's co-authors include K. L. Polakoski, Kenneth L. Polakoski, William R. Fair, Donald J. Graves, Ronald J. Uhing, Richard R. Tidwell, J. D. Geratz, Richard A. Anderson, William P. Kennedy and Frederick A. Dombrose and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Richard F. Parrish

29 papers receiving 701 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Richard F. Parrish United States 17 319 252 145 134 89 29 764
K. L. Polakoski United States 14 318 1.0× 369 1.5× 101 0.7× 174 1.3× 91 1.0× 22 786
James G. Chafouleas United States 12 739 2.3× 82 0.3× 149 1.0× 81 0.6× 65 0.7× 16 1.1k
Fulvio Micali Italy 19 432 1.4× 178 0.7× 36 0.2× 106 0.8× 66 0.7× 22 1.0k
N. Swaminathan United States 13 323 1.0× 207 0.8× 39 0.3× 140 1.0× 176 2.0× 22 798
E Leone Italy 15 440 1.4× 98 0.4× 68 0.5× 35 0.3× 49 0.6× 36 720
Angela Ostuni Italy 18 390 1.2× 83 0.3× 142 1.0× 80 0.6× 31 0.3× 71 1.1k
Yuichi Kawai Japan 17 404 1.3× 98 0.4× 38 0.3× 90 0.7× 52 0.6× 58 1.0k
C S Teng United States 14 683 2.1× 78 0.3× 42 0.3× 68 0.5× 39 0.4× 34 1.0k
Olga Castro Chile 17 339 1.1× 158 0.6× 201 1.4× 143 1.1× 60 0.7× 28 787
June Findlay Australia 7 404 1.3× 63 0.3× 87 0.6× 38 0.3× 49 0.6× 7 757

Countries citing papers authored by Richard F. Parrish

Since Specialization
Citations

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

Fields of papers citing papers by Richard F. Parrish

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Richard F. Parrish. 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 F. Parrish. The network helps show where Richard F. Parrish may publish in the future.

Co-authorship network of co-authors of Richard F. Parrish

This figure shows the co-authorship network connecting the top 25 collaborators of Richard F. Parrish. A scholar is included among the top collaborators of Richard F. Parrish 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 F. Parrish. Richard F. Parrish 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.
Allen, Michael P., et al.. (1991). Inactivation of aminated horseradish peroxidase by interaction with S-Sepharose. Analytical Biochemistry. 192(2). 453–457. 1 indexed citations
2.
Parrish, Richard F., et al.. (1987). An internal clock reaction used in a one-step enzyme immunochromatographic assay of theophylline in whole blood.. PubMed. 33(9). 1521–5. 23 indexed citations
3.
Parrish, Richard F., et al.. (1987). Vasectomy and Vasovasostomy have no Effect on Seminal Plasma Zinc Concentrations. The Journal of Urology. 137(2). 228–229. 6 indexed citations
4.
Heston, Warren D.W., et al.. (1985). Mitogenic Factors in Prostatic Tissue and Expressed Prostatic Secretion. The Journal of Urology. 133(1). 45–48. 17 indexed citations
5.
Parrish, Richard F., et al.. (1983). Evidence against a zinc binding peptide in pilocarpine‐stimulated canine prostatic secretions. The Prostate. 4(2). 189–193. 3 indexed citations
6.
Kennedy, William P., A. Swift, Richard F. Parrish, & K. L. Polakoski. (1982). Proacrosin conversion inhibitor. Purification and initial characterization of a boar sperm protein which prevents the conversion of proacrosin into acrosin.. Journal of Biological Chemistry. 257(6). 3095–3099. 11 indexed citations
7.
Parrish, Richard F. & K. L. Polakoski. (1981). Stimulation of proteolytic activity of boar sperm acrosin by divalent metal ions. Reproduction. 62(2). 417–422. 11 indexed citations
8.
Parrish, Richard F., et al.. (1981). Boar acrosin. Association of an endogenous membrane proteinase with phospholipid membranes.. Journal of Biological Chemistry. 256(11). 5662–5668. 17 indexed citations
9.
Parrish, Richard F., Jessie C. Goodpasture, Lourens J.D. Zaneveld, & K. L. Polakoski. (1979). Polyamine inhibition of the conversion of human proacrosin to acrosin. Reproduction. 57(1). 239–243. 11 indexed citations
10.
Uhing, Ronald J., et al.. (1979). A role for pyridoxal phosphate in the control of dephosphorylation of phosphorylase a.. Journal of Biological Chemistry. 254(17). 8263–8269. 12 indexed citations
11.
Parrish, Richard F. & Kenneth L. Polakoski. (1979). Mammalian sperm proacrosin-acrosin system. International Journal of Biochemistry. 10(5). 391–395. 54 indexed citations
12.
Paulson, John D., Richard F. Parrish, & K. L. Polakoski. (1979). Comparative synthetic substrate kinetics of porcine acrosin and porcine β-trypsin. International Journal of Biochemistry. 10(3). 247–249. 3 indexed citations
13.
Parrish, Richard F., et al.. (1979). Fertilization: A Uterine Glycosaminoglycan Stimulates the Conversion of Sperm Proacrosin to Acrosin. Science. 203(4380). 553–554. 41 indexed citations
14.
Parrish, Richard F. & K. L. Polakoski. (1978). Boar malpha-acrosin. Purification and characterization of the inital active enzyme resulting from the conversion of boar proacrosin to acrosin.. Journal of Biological Chemistry. 253(23). 8428–8432. 31 indexed citations
15.
Parrish, Richard F. & Kenneth L. Polakoski. (1978). An apparent high molecular weight form of boar proacrosin resulting from the presence of a protein that binds to proacrosin. Analytical Biochemistry. 87(1). 108–113. 21 indexed citations
16.
Parrish, Richard F., Werner Straus, K. L. Polakoski, & Frederick A. Dombrose. (1978). Phospholipid vesicle stimulation of proacrosin activation.. Proceedings of the National Academy of Sciences. 75(1). 149–152. 19 indexed citations
17.
Parrish, Richard F., Ronald J. Uhing, & Donald J. Graves. (1977). Effect of phosphate analogs on the activity of pyridoxal reconstituted glycogen phosphorylase. Biochemistry. 16(22). 4824–4831. 56 indexed citations
18.
Polakoski, Kenneth L. & Richard F. Parrish. (1977). PURIFICATION AND PRELIMINARY ACTIVATION STUDIES OF PROACROSIN ISOLATED FROM EJACULATED BOAR SPERM. 16 indexed citations
19.
Parrish, Richard F. & Donald J. Graves. (1976). Irreversible inhibition of phosphorylase phosphatase by fluorophosphate. Biochemical and Biophysical Research Communications. 70(4). 1290–1296. 2 indexed citations
20.
Anderson, Richard A., Richard F. Parrish, & Donald J. Graves. (1973). Chemistry of the adenosine monophosphate site of rabbit muscle glycogen phosphorylase. II. Properties of 8-[m-(m-fluorosulfonylbenzamido)benzylthio]adenine-modified phosphorylase. Biochemistry. 12(10). 1901–1906. 21 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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