M.A. Rosemeyer

1.4k total citations
29 papers, 1.2k citations indexed

About

M.A. Rosemeyer is a scholar working on Molecular Biology, Cell Biology and Pediatrics, Perinatology and Child Health. According to data from OpenAlex, M.A. Rosemeyer has authored 29 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 9 papers in Cell Biology and 7 papers in Pediatrics, Perinatology and Child Health. Recurrent topics in M.A. Rosemeyer's work include Neonatal Health and Biochemistry (7 papers), Hemoglobin structure and function (7 papers) and Pancreatic function and diabetes (6 papers). M.A. Rosemeyer is often cited by papers focused on Neonatal Health and Biochemistry (7 papers), Hemoglobin structure and function (7 papers) and Pancreatic function and diabetes (6 papers). M.A. Rosemeyer collaborates with scholars based in United Kingdom, Switzerland and Greece. M.A. Rosemeyer's co-authors include David Worthington, E. R. Huehns, P P Cohen, Barbara M. F. Pearse, John S. Easterby, Philip P. Cohen, A.A. Haritos, Patricia H. Clarke, Raymond J. Ivatt and I M Franklin and has published in prestigious journals such as Journal of Molecular Biology, FEBS Letters and Methods in enzymology on CD-ROM/Methods in enzymology.

In The Last Decade

M.A. Rosemeyer

29 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
M.A. Rosemeyer United Kingdom 17 619 334 280 277 238 29 1.2k
Henry Borsook United States 20 760 1.2× 279 0.8× 87 0.3× 112 0.4× 465 2.0× 43 1.7k
Jessie V.B. Warms United States 17 789 1.3× 244 0.7× 185 0.7× 126 0.5× 406 1.7× 19 1.3k
Emanuel Silverstein United States 23 1.0k 1.7× 160 0.5× 163 0.6× 39 0.1× 253 1.1× 49 1.8k
Haruhisa Yoshikawa Japan 19 676 1.1× 307 0.9× 61 0.2× 369 1.3× 701 2.9× 72 1.6k
H. Stewart Hendrickson United States 21 1.3k 2.1× 409 1.2× 241 0.9× 68 0.2× 258 1.1× 54 2.1k
Frank Eisenberg United States 21 484 0.8× 218 0.7× 118 0.4× 67 0.2× 282 1.2× 42 1.4k
T.M.A.R. Dubbelman Netherlands 27 772 1.2× 168 0.5× 129 0.5× 148 0.5× 237 1.0× 56 1.7k
W S Sly United States 21 1.2k 1.9× 271 0.8× 86 0.3× 56 0.2× 439 1.8× 29 1.6k
Masazumi Takeshita Japan 17 408 0.7× 124 0.4× 121 0.4× 232 0.8× 186 0.8× 50 843
V.R. Potter United States 19 657 1.1× 212 0.6× 271 1.0× 50 0.2× 260 1.1× 36 1.5k

Countries citing papers authored by M.A. Rosemeyer

Since Specialization
Citations

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

Fields of papers citing papers by M.A. Rosemeyer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by M.A. Rosemeyer. 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 M.A. Rosemeyer. The network helps show where M.A. Rosemeyer may publish in the future.

Co-authorship network of co-authors of M.A. Rosemeyer

This figure shows the co-authorship network connecting the top 25 collaborators of M.A. Rosemeyer. A scholar is included among the top collaborators of M.A. Rosemeyer 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 M.A. Rosemeyer. M.A. Rosemeyer 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.
Haritos, A.A., et al.. (1989). Evidence for the monomeric nature of thymosins. FEBS Letters. 244(2). 287–290. 15 indexed citations
2.
Haritos, A.A., et al.. (1987). On the molecular size of thymosins. FEBS Letters. 218(1). 107–112. 17 indexed citations
3.
Haritos, A.A. & M.A. Rosemeyer. (1986). Purification and physical properties of hexokinase from human erythrocytes. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 873(3). 335–339. 6 indexed citations
4.
Rosemeyer, M.A., et al.. (1986). Microtubule formation and the initial association of tubulin dimers. FEBS Letters. 194(1). 78–84. 5 indexed citations
5.
Franklin, I M, E. R. Huehns, & M.A. Rosemeyer. (1986). Increasing haemoglobin oxygen affinity to prevent sickling: abnormal haemoglobin variants as models. British Journal of Haematology. 64(2). 319–329. 1 indexed citations
6.
Franklin, I M, M.A. Rosemeyer, & E. R. Huehns. (1983). Sickle cell disease: the proportion of liganded haemoglobin needed to prevent crises. British Journal of Haematology. 54(4). 579–587. 16 indexed citations
7.
Huehns, E. R., et al.. (1979). Participation of haemoglobins A, F, A2 and C in polymerisation of haemoglobin S. Journal of Molecular Biology. 129(1). 45–59. 30 indexed citations
8.
Rosemeyer, M.A.. (1978). Physical biochemistry. Applications to biochemistry and molecular biology. FEBS Letters. 89(2). 345–345. 20 indexed citations
9.
Worthington, David & M.A. Rosemeyer. (1976). Glutathione Reductase from Human Erythrocytes. European Journal of Biochemistry. 67(1). 231–238. 163 indexed citations
10.
Pearse, Barbara M. F. & M.A. Rosemeyer. (1975). [49] 6-Phosphogluconate dehydrogenase from human erythrocytes. Methods in enzymology on CD-ROM/Methods in enzymology. 41. 220–226. 32 indexed citations
11.
Worthington, David & M.A. Rosemeyer. (1975). Glutathione Reductase from Human Erythrocytes. European Journal of Biochemistry. 60(2). 459–466. 44 indexed citations
12.
Cohen, Philip P. & M.A. Rosemeyer. (1975). [47] Glucose-6-phosphate dehydrogenase from human erythrocytes. Methods in enzymology on CD-ROM/Methods in enzymology. 41. 208–214. 34 indexed citations
13.
Worthington, David & M.A. Rosemeyer. (1974). The Isolation and Properties of Glutathione Reductase from Human Erythrocytes. Biochemical Society Transactions. 2(5). 927–929. 7 indexed citations
14.
Challand, G S & M.A. Rosemeyer. (1974). The correlation between the apparent molecular weight and the enzymic activity of lactose synthetase. FEBS Letters. 47(1). 94–97. 1 indexed citations
15.
Pearse, Barbara M. F. & M.A. Rosemeyer. (1974). Human 6-Phosphogluconate Dehydrogenase. Purification of the Erythrocyte Enzyme and the Influence of Ions and NADPH on its Activity. European Journal of Biochemistry. 42(1). 213–223. 38 indexed citations
16.
Clarke, Patricia H., et al.. (1973). The Subunit Structure of the Aliphatic Amidase from Pseudomonas aeruginosa. European Journal of Biochemistry. 34(1). 177–187. 29 indexed citations
17.
Ivatt, Raymond J. & M.A. Rosemeyer. (1972). The complex formed between the A and B proteins of lactose synthetase. FEBS Letters. 28(2). 195–197. 14 indexed citations
18.
Rosemeyer, M.A., et al.. (1969). The molecular weight and dissociation properties of yeast hexokinase. FEBS Letters. 4(2). 84–86. 17 indexed citations
19.
Cohen, P P & M.A. Rosemeyer. (1969). Human Glucose-6-Phosphate Dehydrogenase: Purification of the Erythrocyte Enzyme and the Influence of Ions on its Activity. European Journal of Biochemistry. 8(1). 1–7. 84 indexed citations
20.
Cohen, P P & M.A. Rosemeyer. (1968). The molecular weight and subunit structure of glucose‐6‐phosphate dehydrogenase from human erythrocytes. FEBS Letters. 1(3). 147–149. 12 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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