G.D. Brayer

1.9k total citations
29 papers, 1.6k citations indexed

About

G.D. Brayer is a scholar working on Molecular Biology, Materials Chemistry and Cell Biology. According to data from OpenAlex, G.D. Brayer has authored 29 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 10 papers in Materials Chemistry and 6 papers in Cell Biology. Recurrent topics in G.D. Brayer's work include Protein Structure and Dynamics (9 papers), Enzyme Structure and Function (9 papers) and Photosynthetic Processes and Mechanisms (5 papers). G.D. Brayer is often cited by papers focused on Protein Structure and Dynamics (9 papers), Enzyme Structure and Function (9 papers) and Photosynthetic Processes and Mechanisms (5 papers). G.D. Brayer collaborates with scholars based in Canada, United States and Australia. G.D. Brayer's co-authors include Michael N.G. James, Louis T. J. Delbaere, Stephen V. Evans, Anita R. Sielecki, Carl‐Axel Bauer, P. Venugopalan, Michael Levine, Y. Luo, N. Ramasubbu and Gordon V. Louie and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Journal of Molecular Biology.

In The Last Decade

G.D. Brayer

29 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
G.D. Brayer Canada 19 954 302 242 239 213 29 1.6k
Klaus Bartels Germany 18 1.5k 1.5× 569 1.9× 189 0.8× 148 0.6× 146 0.7× 38 2.1k
J.-P. Mornon France 20 1.3k 1.3× 309 1.0× 182 0.8× 265 1.1× 129 0.6× 54 2.1k
J. Symerský United States 18 1.3k 1.4× 149 0.5× 252 1.0× 134 0.6× 225 1.1× 47 2.0k
Roger Bone United States 21 934 1.0× 287 1.0× 245 1.0× 85 0.4× 124 0.6× 33 1.6k
Herbert Treutlein Australia 20 1.2k 1.2× 111 0.4× 358 1.5× 216 0.9× 89 0.4× 37 1.9k
Michael Laskowski United States 20 1.1k 1.2× 200 0.7× 120 0.5× 154 0.6× 105 0.5× 32 1.6k
J. Janin France 22 2.0k 2.0× 794 2.6× 151 0.6× 294 1.2× 70 0.3× 35 2.5k
Valerio Consalvi Italy 22 1.2k 1.3× 599 2.0× 159 0.7× 88 0.4× 114 0.5× 76 1.9k
Richard A. Pauptit United Kingdom 25 1.8k 1.9× 460 1.5× 558 2.3× 226 0.9× 96 0.5× 42 2.6k
Irimpan I. Mathews United States 33 1.8k 1.9× 583 1.9× 435 1.8× 99 0.4× 199 0.9× 85 3.1k

Countries citing papers authored by G.D. Brayer

Since Specialization
Citations

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

Fields of papers citing papers by G.D. Brayer

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by G.D. Brayer. 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 G.D. Brayer. The network helps show where G.D. Brayer may publish in the future.

Co-authorship network of co-authors of G.D. Brayer

This figure shows the co-authorship network connecting the top 25 collaborators of G.D. Brayer. A scholar is included among the top collaborators of G.D. Brayer 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 G.D. Brayer. G.D. Brayer 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.
2.
Williams, Lisa, Chris A. Tarling, Harry C. Brastianos, et al.. (2008). Inhibition of human pancreatic alpha-amylase by montbretin A: a new drug for diabetes and obesity?. Acta Crystallographica Section A Foundations of Crystallography. 64(a1). C346–C347. 2 indexed citations
3.
Ramasubbu, N., P. Venugopalan, Y. Luo, G.D. Brayer, & Michael Levine. (1996). Structure of Human Salivary α-Amylase at 1.6 Å Resolution: Implications for its Role in the Oral Cavity. Acta Crystallographica Section D Biological Crystallography. 52(3). 435–446. 223 indexed citations
4.
Lo, Terence P., et al.. (1995). Structural Studies of the Roles of Residues 82 and 85 at the Interactive Face of Cytochrome c. Biochemistry. 34(1). 163–171. 20 indexed citations
5.
Guillemette, J. Guy, Paul D. Barker, Lindsay D. Eltis, et al.. (1994). Analysis of the bimolecular reduction of ferricytochrome c by ferrocytochrome b5 through mutagenesis and molecular modelling. Biochimie. 76(7). 592–604. 36 indexed citations
6.
Tong, Harry, et al.. (1994). ASIR: an automatic procedure for determining solvent structure in protein crystallography. Journal of Applied Crystallography. 27(3). 421–426. 9 indexed citations
7.
Evans, Stephen V., et al.. (1994). Three-dimensional structure of cyanomet-sulfmyoglobin C.. Proceedings of the National Academy of Sciences. 91(11). 4723–4726. 26 indexed citations
8.
Maurus, R., Ralf Bogumil, Yanru Luo, et al.. (1994). Structural characterization of heme ligation in the His64–>Tyr variant of myoglobin.. Journal of Biological Chemistry. 269(17). 12606–12610. 20 indexed citations
9.
Langen, Ralf, G.D. Brayer, Albert M. Berghuis, et al.. (1992). Effect of the Asn52 → Ile mutation on the redox potential of yeast cytochrome c. Journal of Molecular Biology. 224(3). 589–600. 76 indexed citations
10.
Hamaguchi, Nobuko, et al.. (1991). Expression and characterization of human factor IX. Factor IXthr-397 and factor IXval-397. Journal of Biological Chemistry. 266(23). 15213–15220. 24 indexed citations
11.
Nall, Barry T., et al.. (1989). Crystallization of yeast iso-2-cytochrome c using a novel hair seeding technique. Journal of Molecular Biology. 206(4). 783–785. 23 indexed citations
12.
Evans, Jason P., K. M. Brinkhous, G.D. Brayer, H Reisner, & Katherine A. High. (1989). Canine hemophilia B resulting from a point mutation with unusual consequences.. Proceedings of the National Academy of Sciences. 86(24). 10095–10099. 149 indexed citations
13.
Evans, Stephen V. & G.D. Brayer. (1988). Horse heart metmyoglobin. A 2.8-A resolution three-dimensional structure determination.. Journal of Biological Chemistry. 263(9). 4263–4268. 95 indexed citations
14.
Duckworth, Harry W., et al.. (1987). Structural basis for regulation in gram-negative bacterial citrate synthases.. PubMed. 54. 83–92. 8 indexed citations
15.
Louie, Gordon V., et al.. (1987). MOLECULAR BASIS OF HEMOPHILIA B: IDENTIFICATION OF THE DEFECT IN FACTOR IX VANCOUVER. Thrombosis and Haemostasis. 4 indexed citations
16.
Taketa, F., et al.. (1985). Structural Model for the Trialkyltin Binding Site on Cat Hemoglobin. Journal of Biomolecular Structure and Dynamics. 3(3). 579–584. 10 indexed citations
17.
Cool, D E, C J Edgell, Gordon V. Louie, et al.. (1985). Characterization of human blood coagulation factor XII cDNA. Prediction of the primary structure of factor XII and the tertiary structure of beta-factor XIIa.. Journal of Biological Chemistry. 260(25). 13666–13676. 173 indexed citations
18.
Brayer, G.D. & Michael N.G. James. (1982). A charge-transfer complex: bis(2,4,6-trimethyl-1-pyridyl)iodonium perchlorate. Acta Crystallographica Section B. 38(2). 654–657. 18 indexed citations
19.
James, Michael N.G., Anita R. Sielecki, G.D. Brayer, Louis T. J. Delbaere, & Carl‐Axel Bauer. (1980). Structures of product and inhibitor complexes of Streptomyces griseus protease A at 1.8 Å resolution. Journal of Molecular Biology. 144(1). 43–88. 190 indexed citations
20.
Sielecki, Anita R., et al.. (1979). Protein structure refinement: Streptomyces griseus serine protease A at 1.8 Å resolution. Journal of Molecular Biology. 134(4). 781–804. 95 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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