Sarah Hopper

994 total citations
21 papers, 853 citations indexed

About

Sarah Hopper is a scholar working on Molecular Biology, Materials Chemistry and Endocrinology, Diabetes and Metabolism. According to data from OpenAlex, Sarah Hopper has authored 21 papers receiving a total of 853 indexed citations (citations by other indexed papers that have themselves been cited), including 9 papers in Molecular Biology, 4 papers in Materials Chemistry and 3 papers in Endocrinology, Diabetes and Metabolism. Recurrent topics in Sarah Hopper's work include Redox biology and oxidative stress (5 papers), Enzyme Structure and Function (4 papers) and Metal-Catalyzed Oxygenation Mechanisms (3 papers). Sarah Hopper is often cited by papers focused on Redox biology and oxidative stress (5 papers), Enzyme Structure and Function (4 papers) and Metal-Catalyzed Oxygenation Mechanisms (3 papers). Sarah Hopper collaborates with scholars based in United States and United Kingdom. Sarah Hopper's co-authors include Harold L. Segal, H L Segal, K. Biemann, Richard S. Johnson, Diana S. Beattie, A. E. Axelrod, James E. Vath, W. Rodney Mathews, R. Rosso and D. A. Long and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Methods in enzymology on CD-ROM/Methods in enzymology.

In The Last Decade

Sarah Hopper

21 papers receiving 781 citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Sarah Hopper United States	16	488	167	147	120	116	21	853
J. Schultz United States	8	423 0.9×	94 0.6×	399 2.7×	74 0.6×	103 0.9×	13	1.2k
Frixos C. Charalampous United States	19	525 1.1×	124 0.7×	84 0.6×	59 0.5×	167 1.4×	45	1.1k
John B. Longenecker United States	13	218 0.4×	81 0.5×	75 0.5×	67 0.6×	111 1.0×	27	653
Jan Maciej Zgliczyński Poland	13	324 0.7×	61 0.4×	376 2.6×	32 0.3×	128 1.1×	19	965
Frans J. van der Ouderaa Netherlands	8	774 1.6×	152 0.9×	219 1.5×	72 0.6×	274 2.4×	10	1.2k
Robert Y. Hsu United States	21	828 1.7×	341 2.0×	204 1.4×	129 1.1×	247 2.1×	38	1.3k
Astor Baldesten Sweden	12	430 0.9×	79 0.5×	39 0.3×	32 0.3×	81 0.7×	15	610
Ralph A. Stephani United States	18	434 0.9×	123 0.7×	45 0.3×	38 0.3×	109 0.9×	39	882
Wolfgang J. Baumann United States	20	748 1.5×	301 1.8×	96 0.7×	90 0.8×	76 0.7×	48	1.2k
Marie‐Agnès Sari France	19	674 1.4×	121 0.7×	214 1.5×	24 0.2×	66 0.6×	39	1.5k

Countries citing papers authored by Sarah Hopper

Since Specialization

Citations

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

Fields of papers citing papers by Sarah Hopper

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Sarah Hopper

This figure shows the co-authorship network connecting the top 25 collaborators of Sarah Hopper. A scholar is included among the top collaborators of Sarah Hopper 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 Sarah Hopper. Sarah Hopper 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

Chouljenko, Alexander, et al.. (2024). Combining Fish and Crustacean Byproducts as Primary Ingredients in Pelleted Aquafeed: The Effect of Byproduct Type on Pellet Physical Properties. Aquaculture Research. 2024(1). 2 indexed citations

Hopper, Sarah, et al.. (2010). Integrating psychological formulations into older people’s services – three years on (Part 2): Evaluation of the formulation training programme. 1(112). 12–15. 2 indexed citations

Hopper, Sarah, et al.. (1998). Aspirin after myocardial infarction: the importance of over-the-counter use.. PubMed. 15 Suppl 1. S10–3. 16 indexed citations

Hopper, Sarah. (1990). ?I never thought I'd make it quite this far?: A personal journey in international understanding. Child & Youth Care Forum. 19(3). 177–180. 1 indexed citations

Hopper, Sarah, Richard S. Johnson, James E. Vath, & K. Biemann. (1989). Glutaredoxin from Rabbit Bone Marrow. Journal of Biological Chemistry. 264(34). 20438–20447. 90 indexed citations

Johnson, Richard S., W. Rodney Mathews, K. Biemann, & Sarah Hopper. (1988). Amino acid sequence of thioredoxin isolated from rabbit bone marrow determined by tandem mass spectrometry.. Journal of Biological Chemistry. 263(20). 9589–9597. 57 indexed citations

Hopper, Sarah, Alastair Greig, & C.H. McMurray. (1985). Selenium poisoning in lambs. Veterinary Record. 116(21). 569–571. 18 indexed citations

Hopper, Sarah, et al.. (1983). Properties of a thioredoxin purified from rabbit bone marrow which fails to serve as a hydrogen donor for the homologous ribonucleotide reductase.. Journal of Biological Chemistry. 258(22). 13453–13457. 31 indexed citations

Moore, Paul A., et al.. (1979). Diphenylhydantoin Induced Gingival Hyperplasia in Ferrets: A Precautionary Note. Journal of Dental Research. 58(8). 1812–1814. 3 indexed citations

10.

Hopper, Sarah. (1978). [31] Ribonucleotide reductase of rabbit bone marrow. Methods in enzymology on CD-ROM/Methods in enzymology. 51. 237–246. 18 indexed citations

11.

Bhan, Ashok, et al.. (1974). Substrate and effector binding to ribonucleoside triphosphate reductase of Lactobacillus leichmannii. Biochemistry. 13(4). 654–661. 36 indexed citations

12.

Hopper, Sarah. (1972). Ribonucleotide Reductase of Rabbit Bone Marrow. Journal of Biological Chemistry. 247(10). 3336–3340. 71 indexed citations

13.

Hopper, Sarah, et al.. (1967). Further Characterization of Alanine Aminotransferase of Rat Liver. Journal of Biological Chemistry. 242(10). 2319–2324. 50 indexed citations

14.

Segal, Harold L., Yee S. Kim, & Sarah Hopper. (1965). Glucocorticoid control of rat liver glutamic-alanine transaminase biosynthesis. Advances in Enzyme Regulation. 3. 29–42. 22 indexed citations

15.

Hopper, Sarah & H L Segal. (1964). Comparative properties of glutamic-alanine transaminase from several sources. Archives of Biochemistry and Biophysics. 105(3). 501–505. 78 indexed citations

16.

Segal, H L, Diana S. Beattie, & Sarah Hopper. (1962). Purification and Properties of Liver Glutamic-Alanine Transaminase from Normal and Corticoid-treated Rats. Journal of Biological Chemistry. 237(6). 1914–1920. 91 indexed citations

17.

Segal, Harold L., R. Rosso, Sarah Hopper, & Morton M. Weber. (1962). Direct Evidence for an Increase in Enzyme Level as the Basis for the Glucocorticoid-induced Increase in Glutamic-Alanine Transaminase Activity in Rat Liver. Journal of Biological Chemistry. 237(10). PC3303–PC3305. 38 indexed citations

18.

Hopper, Sarah & Harold L. Segal. (1962). Kinetic Studies of Rat Liver Glutamic-Alanine Transaminase. Journal of Biological Chemistry. 237(10). 3189–3195. 161 indexed citations

19.

Axelrod, A. E., Sarah Hopper, & D. A. Long. (1961). Effects of Pyridoxine Deficiency upon Circulating Antibody Formation and Skin Hypersensitivity Reactions to Diphtheria Toxoid in Guinea Pigs. Journal of Nutrition. 74(1). 58–64. 30 indexed citations

20.

Axelrod, A. E. & Sarah Hopper. (1960). Effects of Pantothenic Acid, Pyridoxine and Thiamine Deficiencies upon Antibody Formation to Influenza Virus PR-8 in Rats. Journal of Nutrition. 72(3). 325–330. 31 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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