Patrick J. Baker

6.3k total citations
126 papers, 4.7k citations indexed

About

Patrick J. Baker is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, Patrick J. Baker has authored 126 papers receiving a total of 4.7k indexed citations (citations by other indexed papers that have themselves been cited), including 76 papers in Molecular Biology, 73 papers in Materials Chemistry and 30 papers in Biochemistry. Recurrent topics in Patrick J. Baker's work include Enzyme Structure and Function (71 papers), Protein Structure and Dynamics (28 papers) and Amino Acid Enzymes and Metabolism (28 papers). Patrick J. Baker is often cited by papers focused on Enzyme Structure and Function (71 papers), Protein Structure and Dynamics (28 papers) and Amino Acid Enzymes and Metabolism (28 papers). Patrick J. Baker collaborates with scholars based in United Kingdom, United States and Netherlands. Patrick J. Baker's co-authors include David W. Rice, K.L. Britton, Timothy J. Stillman, Svetlana E. Sedelnikova, John B. Rafferty, Paul C. Engel, Antoine R. Stuitje, Antoni R. Slabas, Clair Baldock and Alessandra Pasquo and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Nucleic Acids Research.

In The Last Decade

Patrick J. Baker

122 papers receiving 4.6k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Patrick J. Baker United Kingdom	36	3.1k	1.7k	898	519	503	126	4.7k
Karen N. Allen United States	43	4.0k 1.3×	1.9k 1.1×	687 0.8×	613 1.2×	473 0.9×	137	5.8k
James B. Thoden United States	45	4.7k 1.5×	2.4k 1.4×	884 1.0×	744 1.4×	392 0.8×	153	6.6k
Sherry L. Mowbray Sweden	42	3.8k 1.2×	1.1k 0.6×	521 0.6×	545 1.1×	816 1.6×	111	5.3k
Michail N. Isupov United Kingdom	34	3.7k 1.2×	1.3k 0.8×	445 0.5×	402 0.8×	466 0.9×	116	5.2k
Rudolf Ladenstein Sweden	47	5.8k 1.9×	2.7k 1.6×	516 0.6×	389 0.7×	583 1.2×	131	7.8k
Debra Dunaway‐Mariano United States	46	5.0k 1.6×	2.3k 1.4×	1.1k 1.2×	906 1.7×	413 0.8×	203	7.2k
Jack F. Kirsch United States	41	4.1k 1.3×	1.7k 1.0×	1.2k 1.4×	1.0k 2.0×	389 0.8×	145	5.8k
Joseph D. Schrag Canada	40	5.8k 1.9×	760 0.5×	616 0.7×	600 1.2×	417 0.8×	71	7.4k
Seiki Kuramitsu Japan	50	6.8k 2.2×	2.1k 1.2×	913 1.0×	312 0.6×	1.5k 3.0×	328	8.3k
Se Won Suh South Korea	40	4.2k 1.4×	906 0.5×	329 0.4×	300 0.6×	496 1.0×	196	5.7k

Countries citing papers authored by Patrick J. Baker

Since Specialization

Citations

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

Fields of papers citing papers by Patrick J. Baker

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Patrick J. Baker. 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 Patrick J. Baker. The network helps show where Patrick J. Baker may publish in the future.

Co-authorship network of co-authors of Patrick J. Baker

This figure shows the co-authorship network connecting the top 25 collaborators of Patrick J. Baker. A scholar is included among the top collaborators of Patrick J. Baker 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 Patrick J. Baker. Patrick J. Baker 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

Baxter, Nicola J., et al.. (2024). Peri active site catalysis of proline isomerisation is the molecular basis of allomorphy in β-phosphoglucomutase. Communications Biology. 7(1). 909–909.

Sedelnikova, Svetlana E., et al.. (2020). The A component (SmhA) of a tripartite pore-forming toxin from Serratia marcescens: expression, purification and crystallographic analysis. Acta Crystallographica Section F Structural Biology Communications. 76(12). 577–582. 2 indexed citations

Wilson, Jason S., Svetlana E. Sedelnikova, Svetomir B. Tzokov, et al.. (2019). Identification and structural analysis of the tripartite α-pore forming toxin of Aeromonas hydrophila. Nature Communications. 10(1). 19 indexed citations

Harris, Matthew J., et al.. (2018). TssA from Aeromonas hydrophila: expression, purification and crystallographic studies. Acta Crystallographica Section F Structural Biology Communications. 74(9). 578–582. 1 indexed citations

Bisson, C., Nathan B. P. Adams, Amanda A. Brindley, et al.. (2017). The molecular basis of phosphite and hypophosphite recognition by ABC-transporters. Nature Communications. 8(1). 1746–1746. 50 indexed citations

Iwig, Jeffrey S., C. Bisson, Matthew D. Rolfe, et al.. (2016). The mechanism of a formaldehyde-sensing transcriptional regulator. Scientific Reports. 6(1). 38879–38879. 52 indexed citations

Sedelnikova, Svetlana E., et al.. (2013). Crystallization and preliminary crystallographic analysis of a surface antigen glycoprotein, SAG19, fromEimeria tenella. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 69(12). 1380–1383. 8 indexed citations

Haydon, David J., Neil R. Stokes, James M. Bennett, et al.. (2008). An Inhibitor of FtsZ with Potent and Selective Anti-Staphylococcal Activity. Science. 321(5896). 1673–1675. 379 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

10.

Glynn, Steven E., Patrick J. Baker, Svetlana E. Sedelnikova, et al.. (2005). Purification, crystallization and preliminary crystallographic analysis ofArabidopsis thalianaimidazoleglycerol-phosphate dehydratase. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 61(8). 776–778. 2 indexed citations

11.

Rafferty, John B., Edward L. Bolt, T. A. Muranova, et al.. (2003). The Structure of Escherichia coli RusA Endonuclease Reveals a New Holliday Junction DNA Binding Fold. Structure. 11(12). 1557–1567. 20 indexed citations

12.

Roujeinikova, Anna, et al.. (2001). The crystal structure of Thermotoga maritima maltosyltransferase and its implications for the molecular basis of the novel transfer specificity. Journal of Molecular Biology. 312(1). 119–131. 14 indexed citations

13.

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

14.

Ruzheinikov, S.N., Sveta Sedelnikova, Patrick J. Baker, et al.. (2001). Purification, crystallization and quaternary structure analysis of a glycerol dehydrogenase S305C mutant fromBacillus stearothermophilus. Acta Crystallographica Section D Biological Crystallography. 57(1). 165–167. 3 indexed citations

15.

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

16.

Rafferty, John B., Jörg Simon, Clair Baldock, et al.. (1995). Common themes in redox chemistry emerge from the X-ray structure of oilseed rape (Brassica napus) enoyl acyl carrier protein reductase. Structure. 3(9). 927–938. 97 indexed citations

17.

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

18.

Rizkallah, P.J., Teresa K. Attwood, John C. Wootton, et al.. (1993). Crystallization of the NADP+-dependent Glutamate Dehydrogenase from Escherichia coli. Journal of Molecular Biology. 234(4). 1270–1273. 10 indexed citations

19.

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

20.

Baker, Patrick J., David W. Rice, Timothy J. Stillman, et al.. (1991). Use of chemical modification in the crystallization of isocitrate lyase from Escherichia coli. Journal of Molecular Biology. 220(1). 13–16. 9 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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