K.L. Britton

2.6k total citations
40 papers, 2.2k citations indexed

About

K.L. Britton is a scholar working on Materials Chemistry, Molecular Biology and Biochemistry. According to data from OpenAlex, K.L. Britton has authored 40 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 35 papers in Materials Chemistry, 31 papers in Molecular Biology and 18 papers in Biochemistry. Recurrent topics in K.L. Britton's work include Enzyme Structure and Function (35 papers), Protein Structure and Dynamics (18 papers) and Amino Acid Enzymes and Metabolism (17 papers). K.L. Britton is often cited by papers focused on Enzyme Structure and Function (35 papers), Protein Structure and Dynamics (18 papers) and Amino Acid Enzymes and Metabolism (17 papers). K.L. Britton collaborates with scholars based in United Kingdom, Ireland and United States. K.L. Britton's co-authors include David W. Rice, Patrick J. Baker, Timothy J. Stillman, Paul C. Engel, Kitty S. P. Yip, Frank T. Robb, Alessandra Pasquo, Dennis Maeder, Roberta Chiaraluce and Valerio Consalvi and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Angewandte Chemie International Edition.

In The Last Decade

K.L. Britton

40 papers receiving 2.2k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
K.L. Britton United Kingdom	24	1.7k	1.3k	682	275	184	40	2.2k
Kasper Kirschner Switzerland	35	3.0k 1.8×	1.9k 1.5×	590 0.9×	95 0.3×	128 0.7×	79	3.5k
Alessio Peracchi Italy	28	2.0k 1.2×	609 0.5×	477 0.7×	159 0.6×	55 0.3×	63	2.6k
Ann Ginsburg United States	31	2.1k 1.3×	1.2k 0.9×	901 1.3×	171 0.6×	64 0.3×	88	3.3k
Cynthia Kinsland United States	23	1.5k 0.9×	460 0.4×	270 0.4×	153 0.6×	98 0.5×	27	2.0k
Subramanyam Swaminathan United States	27	1.4k 0.8×	385 0.3×	237 0.3×	135 0.5×	91 0.5×	80	2.6k
Brian J. Bahnson United States	27	1.3k 0.8×	422 0.3×	180 0.3×	124 0.5×	62 0.3×	58	2.0k
M.E. Fraser Canada	24	1.3k 0.8×	587 0.5×	96 0.1×	88 0.3×	195 1.1×	60	2.1k
Bruno Curti Italy	24	1.2k 0.7×	396 0.3×	499 0.7×	256 0.9×	28 0.2×	49	1.6k
Sergio Martínez‐Rodríguez Spain	21	1.1k 0.7×	400 0.3×	266 0.4×	314 1.1×	138 0.8×	77	1.8k
C.A. Bingman United States	34	2.4k 1.4×	380 0.3×	208 0.3×	417 1.5×	206 1.1×	126	3.2k

Countries citing papers authored by K.L. Britton

Since Specialization

Citations

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

Fields of papers citing papers by K.L. Britton

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by K.L. Britton. 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 K.L. Britton. The network helps show where K.L. Britton may publish in the future.

Co-authorship network of co-authors of K.L. Britton

This figure shows the co-authorship network connecting the top 25 collaborators of K.L. Britton. A scholar is included among the top collaborators of K.L. Britton 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 K.L. Britton. K.L. Britton 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

Bisson, C., K.L. Britton, Svetlana E. Sedelnikova, et al.. (2015). Crystal Structures Reveal that the Reaction Mechanism of Imidazoleglycerol-Phosphate Dehydratase Is Controlled by Switching Mn(II) Coordination. Structure. 23(7). 1236–1245. 24 indexed citations

Britton, K.L., Patrick J. Baker, Martin Fisher, et al.. (2006). Analysis of protein solvent interactions in glucose dehydrogenase from the extreme halophile Haloferax mediterranei. Proceedings of the National Academy of Sciences. 103(13). 4846–4851. 98 indexed citations

Seah, Stephen Y. K., K.L. Britton, David W. Rice, Yasuhisa Asano, & Paul C. Engel. (2003). Kinetic analysis of phenylalanine dehydrogenase mutants designed for aliphatic amino acid dehydrogenase activity with guidance from homology‐based modelling. European Journal of Biochemistry. 270(23). 4628–4634. 12 indexed citations

Britton, K.L., I. Sarath B. Abeysinghe, Patrick J. Baker, et al.. (2001). The structure and domain organization ofEscherichia coliisocitrate lyase. Acta Crystallographica Section D Biological Crystallography. 57(9). 1209–1218. 40 indexed citations

Coughlan, Suzie, Xingguo Wang, K.L. Britton, et al.. (2001). Contribution of an aspartate residue, D114, in the active site of clostridial glutamate dehydrogenase to the enzyme’s unusual pH dependence. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1544(1-2). 10–17. 4 indexed citations

Wang, Xingguo, K.L. Britton, Timothy J. Stillman, David W. Rice, & Paul C. Engel. (2001). Conversion of a glutamate dehydrogenase into methionine/norleucine dehydrogenase by site‐directed mutagenesis. European Journal of Biochemistry. 268(22). 5791–5799. 15 indexed citations

Britton, K.L., et al.. (2000). The crystal structure and active site location of isocitrate lyase from the fungus Aspergillus nidulans. Structure. 8(4). 349–362. 61 indexed citations

Stillman, Timothy J., Xingguo Wang, Patrick J. Baker, et al.. (1999). Insights into the mechanism of domain closure and substrate specificity of glutamate dehydrogenase from Clostridium symbiosum 1 1Edited by A. R. Fersht. Journal of Molecular Biology. 285(2). 875–885. 35 indexed citations

Britton, K.L., Timothy J. Stillman, Kitty S. P. Yip, et al.. (1998). Insights into the Molecular Basis of Salt Tolerance from the Study of Glutamate Dehydrogenase from Halobacterium salinarum. Journal of Biological Chemistry. 273(15). 9023–9030. 44 indexed citations

10.

Yip, Kitty S. P., K.L. Britton, Timothy J. Stillman, et al.. (1998). Insights into the molecular basis of thermal stability from the analysis of ion‐pair networks in the Glutamate Dehydrogenase family. European Journal of Biochemistry. 255(2). 336–346. 102 indexed citations

11.

Britton, K.L., Yasuhisa Asano, & David W. Rice. (1998). Crystal structure and active site location of N-(1-D-carboxylethyl)-L-norvaline dehydrogenase. Nature Structural Biology. 5(7). 593–601. 33 indexed citations

12.

Pasquo, Alessandra, K.L. Britton, Timothy J. Stillman, et al.. (1996). Construction of a dimeric form of glutamate dehydrogenase from Clostridium symbiosum by site-directed mutagenesis. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1297(2). 149–158. 11 indexed citations

13.

Rice, David W., Kitty S. P. Yip, Timothy J. Stillman, et al.. (1996). Insights into the molecular basis of thermal stability from the structure determination ofPyrococcus furiosusgluatamate dehydrogenase. FEMS Microbiology Reviews. 18(2-3). 105–117. 56 indexed citations

14.

Britton, K.L., P.J. Artymiuk, Patrick J. Baker, et al.. (1995). The structure of Pyrococcus furiosus glutamate dehydrogenase reveals a key role for ion-pair networks in maintaining enzyme stability at extreme temperatures. Structure. 3(11). 1147–1158. 364 indexed citations

15.

Wang, Xingguo, et al.. (1995). Alteration of the amino acid substrate specificity of clostridial glutamate dehydrogenase by site-directed mutagenesis of an active-site lysine residue. Protein Engineering Design and Selection. 8(2). 147–152. 10 indexed citations

16.

Britton, K.L., Patrick J. Baker, Paul C. Engel, et al.. (1995). Insights into Thermal Stability from a Comparison of the Glutamate Dehydrogenases from Pyrococcus furiosus and Thermococcus litoralis. European Journal of Biochemistry. 229(3). 688–695. 69 indexed citations

17.

Britton, K.L., Patrick J. Baker, Paul C. Engel, David W. Rice, & Timothy J. Stillman. (1993). Evolution of Substrate Diversity in the Superfamily of Amino Acid Dehydrogenases. Journal of Molecular Biology. 234(4). 938–945. 52 indexed citations

18.

Baker, Patrick J., K.L. Britton, Paul C. Engel, et al.. (1992). Subunit assembly and active site location in the structure of glutamate dehydrogenase. Proteins Structure Function and Bioinformatics. 12(1). 75–86. 196 indexed citations

19.

Baker, Patrick J., K.L. Britton, David W. Rice, Abdul Rob, & Timothy J. Stillman. (1992). Structural consequences of sequence patterns in the fingerprint region of the nucleotide binding fold. Journal of Molecular Biology. 228(2). 662–671. 149 indexed citations

20.

Lilley, Kathryn S., Patrick J. Baker, K.L. Britton, et al.. (1991). The partial amino acid sequence of the NAD -dependent glutamate dehydrogenase of Clostridium symbiosum: implications for the evolution and structural basis of coenzyme specificity. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1080(3). 191–197. 32 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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