H.C. Watson

6.5k total citations · 3 hit papers
68 papers, 5.4k citations indexed

About

H.C. Watson is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, H.C. Watson has authored 68 papers receiving a total of 5.4k indexed citations (citations by other indexed papers that have themselves been cited), including 47 papers in Molecular Biology, 40 papers in Materials Chemistry and 17 papers in Biochemistry. Recurrent topics in H.C. Watson's work include Enzyme Structure and Function (40 papers), Protein Structure and Dynamics (23 papers) and Amino Acid Enzymes and Metabolism (16 papers). H.C. Watson is often cited by papers focused on Enzyme Structure and Function (40 papers), Protein Structure and Dynamics (23 papers) and Amino Acid Enzymes and Metabolism (16 papers). H.C. Watson collaborates with scholars based in United Kingdom, Italy and Switzerland. H.C. Watson's co-authors include J Kendrew, Jim Warwicker, David M. Shotton, M. F. Perutz, P.L. Wendell, Linda A. Fothergill‐Gilmore, Jennifer A. Littlechild, T. N. Bryant, Lubert Stryer and Leonard Banaszak and has published in prestigious journals such as Nature, Science and Proceedings of the National Academy of Sciences.

In The Last Decade

H.C. Watson

68 papers receiving 4.9k citations

Hit Papers

Calculation of the electric potential in the active site ... 1961 2026 1982 2004 1982 1965 1961 250 500 750

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
H.C. Watson United Kingdom 35 3.8k 1.9k 1.2k 632 440 68 5.4k
C. C. F. Blake United Kingdom 32 5.4k 1.4× 2.3k 1.2× 1.1k 0.9× 658 1.0× 158 0.4× 65 6.9k
Earle Stellwagen United States 45 4.2k 1.1× 1.2k 0.6× 874 0.7× 713 1.1× 285 0.6× 134 5.7k
J.M. Guss Australia 42 4.6k 1.2× 1.0k 0.5× 811 0.7× 432 0.7× 464 1.1× 154 6.9k
Simon E. V. Phillips United Kingdom 43 5.6k 1.5× 1.3k 0.7× 1.2k 1.0× 458 0.7× 464 1.1× 151 8.4k
Hilary Muirhead United Kingdom 27 2.3k 0.6× 961 0.5× 1.2k 1.0× 319 0.5× 172 0.4× 42 3.6k
Jacqueline A. Reynolds United States 37 5.4k 1.4× 542 0.3× 992 0.8× 1.2k 1.9× 299 0.7× 60 7.6k
Gordon G. Hammes United States 54 7.2k 1.9× 1.9k 1.0× 1.4k 1.1× 1.1k 1.7× 1.0k 2.3× 241 10.0k
Gary K. Ackers United States 47 6.3k 1.7× 776 0.4× 2.8k 2.3× 1.3k 2.0× 244 0.6× 144 8.4k
Lynn F. Ten Eyck United States 39 6.0k 1.6× 2.0k 1.1× 1.0k 0.8× 398 0.6× 156 0.4× 65 7.1k
Yasuhiko Nozaki United States 26 3.5k 0.9× 1.2k 0.6× 607 0.5× 883 1.4× 137 0.3× 32 5.5k

Countries citing papers authored by H.C. Watson

Since Specialization
Citations

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

Fields of papers citing papers by H.C. Watson

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by H.C. Watson. 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 H.C. Watson. The network helps show where H.C. Watson may publish in the future.

Co-authorship network of co-authors of H.C. Watson

This figure shows the co-authorship network connecting the top 25 collaborators of H.C. Watson. A scholar is included among the top collaborators of H.C. Watson 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 H.C. Watson. H.C. Watson 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.
Willetts, Andrew, et al.. (1995). Purification, crystallisation and preliminary X‐ray analysis of the vanadium‐dependent haloperoxidase from Corallina officinalis. FEBS Letters. 359(2-3). 244–246. 31 indexed citations
2.
Davies, G.J., S.J. Gamblin, J.A. Littlechild, et al.. (1994). Structure of the ADP complex of the 3-phosphoglycerate kinase from Bacillus stearothermophilus at 1.65 Å. Acta Crystallographica Section D Biological Crystallography. 50(2). 202–209. 65 indexed citations
3.
Watson, H.C., et al.. (1993). Site‐directed mutagenesis of yeast phosphoglycerate kinase. FEBS Letters. 320(3). 193–197. 6 indexed citations
4.
Littlechild, Jennifer A. & H.C. Watson. (1993). A data-based reaction mechanism for type I fructose bisphosphate aldolase. Trends in Biochemical Sciences. 18(2). 36–39. 41 indexed citations
5.
Davies, G.J., S.J. Gamblin, Jennifer A. Littlechild, & H.C. Watson. (1993). The structure of a thermally stable 3‐phosphoglycerate kinase and a comparison with its mesophilic equivalent. Proteins Structure Function and Bioinformatics. 15(3). 283–289. 65 indexed citations
6.
Walker, P.A., Heidi C. João, Jennifer A. Littlechild, Robert J. P. Williams, & H.C. Watson. (1992). Characterisation of yeast phosphoglycerate kinase modified by mutagenesis at residue 21. European Journal of Biochemistry. 207(1). 29–37. 7 indexed citations
7.
Davies, G.J., et al.. (1992). Purification, crystallization and preliminary X-ray analysis of the 3-phosphoglycerate kinase from Bacillus stearothermophilus. Journal of Molecular Biology. 227(4). 1263–1264. 3 indexed citations
8.
Gamblin, S.J., et al.. (1991). Activity and specificity of human aldolases. Journal of Molecular Biology. 219(4). 573–576. 87 indexed citations
9.
Davies, G.J., J.A. Littlechild, H.C. Watson, & L Hall. (1991). Sequence and expression of the gene encoding 3-phosphoglycerate kinase from Bacillus stearothermophilus. Gene. 109(1). 39–45. 24 indexed citations
10.
Littlechild, Jennifer A., et al.. (1991). A proton‐NMR study of a site‐directed mutation (His388 → Glu) in the interdomain region of yeast phosphoglycerate kinase. European Journal of Biochemistry. 196(2). 261–269. 18 indexed citations
11.
Minard, Philippe, D. J. Bowen, L Hall, J.A. Littlechild, & H.C. Watson. (1990). Site-directed mutagenesis of aspartic acid 372 at the ATP binding site of yeast phosphoglycerate kinase: over-expression and characterization of the mutant enzyme. Protein Engineering Design and Selection. 3(6). 515–521. 20 indexed citations
12.
Fothergill‐Gilmore, Linda A. & H.C. Watson. (1989). The Phosphoglycerate Mutases. Advances in enzymology and related areas of molecular biology/Advances in enzymology and related subjects. 62. 227–313. 195 indexed citations
13.
Fairbrother, Wayne J., P.A. Walker, Philippe Minard, et al.. (1989). NMR analysis of site‐specific mutants of yeast phosphoglycerate kinase. European Journal of Biochemistry. 183(1). 57–67. 37 indexed citations
14.
Fairbrother, Wayne J., et al.. (1989). Site‐directed mutagenesis of histidine 62 in the ‘basic patch’ region of yeast phosphoglycerate kinase. FEBS Letters. 258(2). 247–250. 12 indexed citations
15.
Walker, P.A., et al.. (1989). Site‐directed mutagenesis of yeast phosphoglycerate kinase. European Journal of Biochemistry. 183(1). 49–55. 25 indexed citations
16.
Williams, Robert J. P., et al.. (1988). NMR analysis of the interdomain region of yeast phosphoglycerate kinase. European Journal of Biochemistry. 170(3). 529–538. 44 indexed citations
17.
Watson, H.C., et al.. (1981). Structure and activity of phosphoglycerate mutase. Philosophical transactions of the Royal Society of London. Series B, Biological sciences. 293(1063). 121–130. 99 indexed citations
18.
Shaw, Peter, et al.. (1981). The low-resolution structure of human muscle aldolase. Philosophical transactions of the Royal Society of London. Series B, Biological sciences. 293(1063). 209–214. 16 indexed citations
19.
Banaszak, Leonard, H.C. Watson, & J Kendrew. (1965). The binding of cupric and zinc ions to crystalline sperm whale myoglobin. Journal of Molecular Biology. 12(1). 130–137. 71 indexed citations
20.
Watson, H.C. & Leonard Banaszak. (1964). Structure of Glyceraldehyde-3-Phosphate Dehydrogenase: Structural Symmetry Within the Molecule. Nature. 204(4962). 918–920. 78 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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