Ronald Bauerle

1.9k total citations
46 papers, 1.6k citations indexed

About

Ronald Bauerle is a scholar working on Molecular Biology, Materials Chemistry and Genetics. According to data from OpenAlex, Ronald Bauerle has authored 46 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 33 papers in Molecular Biology, 19 papers in Materials Chemistry and 6 papers in Genetics. Recurrent topics in Ronald Bauerle's work include Enzyme Structure and Function (19 papers), Biochemical and Molecular Research (15 papers) and Plant Gene Expression Analysis (9 papers). Ronald Bauerle is often cited by papers focused on Enzyme Structure and Function (19 papers), Biochemical and Molecular Research (15 papers) and Plant Gene Expression Analysis (9 papers). Ronald Bauerle collaborates with scholars based in United States, Switzerland and India. Ronald Bauerle's co-authors include Paul Margolin, Robert H. Kretsinger, I.A. Shumilin, Maureen Caligiuri, Edith Wilson Miles, Manfred K. Grieshaber, J. M. Ray, Anthony A. Morollo, H. E. Umbarger and Fredrik C. Størmer and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.

In The Last Decade

Ronald Bauerle

46 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Ronald Bauerle United States	24	1.4k	707	199	197	175	46	1.6k
Charlotta Filling Sweden	10	981 0.7×	342 0.5×	79 0.4×	160 0.8×	157 0.9×	12	1.5k
Saburo Komatsubara Japan	24	1.3k 0.9×	213 0.3×	491 2.5×	170 0.9×	164 0.9×	95	1.9k
Isamu Shiio United States	22	2.0k 1.4×	575 0.8×	67 0.3×	453 2.3×	273 1.6×	179	2.3k
Peter A. Jekel Netherlands	22	902 0.6×	171 0.2×	87 0.4×	125 0.6×	68 0.4×	42	1.3k
Gunter B. Kohlhaw United States	28	2.2k 1.6×	468 0.7×	37 0.2×	188 1.0×	173 1.0×	61	2.5k
Haruo Misono Japan	22	1.2k 0.9×	459 0.6×	57 0.3×	513 2.6×	103 0.6×	99	1.5k
David R. J. Palmer Canada	18	804 0.6×	422 0.6×	145 0.7×	211 1.1×	63 0.4×	62	1.1k
Akio Ozaki Japan	21	928 0.7×	201 0.3×	288 1.4×	198 1.0×	111 0.6×	48	1.2k
Sudhamoy Ghosh India	12	738 0.5×	226 0.3×	146 0.7×	214 1.1×	196 1.1×	20	1.1k
R.D. Seidel United States	21	1.1k 0.8×	230 0.3×	137 0.7×	92 0.5×	81 0.5×	35	1.4k

Countries citing papers authored by Ronald Bauerle

Since Specialization

Citations

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

Fields of papers citing papers by Ronald Bauerle

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ronald Bauerle. 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 Ronald Bauerle. The network helps show where Ronald Bauerle may publish in the future.

Co-authorship network of co-authors of Ronald Bauerle

This figure shows the co-authorship network connecting the top 25 collaborators of Ronald Bauerle. A scholar is included among the top collaborators of Ronald Bauerle 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 Ronald Bauerle. Ronald Bauerle 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

Wu, Jing, J. Vijayalakshmi, I.A. Shumilin, et al.. (2011). Structure and characterization of the 3-deoxy-d-arabino-heptulosonate 7-phosphate synthase from Aeropyrum pernix. Bioorganic Chemistry. 40(1). 79–86. 21 indexed citations

Shumilin, I.A., Ronald Bauerle, Jing Wu, Ronald W. Woodard, & Robert H. Kretsinger. (2004). Crystal Structure of the Reaction Complex of 3-Deoxy- d - arabino -heptulosonate-7-phosphate Synthase from Thermotoga maritima Refines the Catalytic Mechanism and Indicates a New Mechanism of Allosteric Regulation. Journal of Molecular Biology. 341(2). 455–466. 64 indexed citations

Shumilin, I.A., Ronald Bauerle, & Robert H. Kretsinger. (2003). The High-Resolution Structure of 3-Deoxy-d-arabino-heptulosonate-7-phosphate Synthase Reveals a Twist in the Plane of Bound Phosphoenolpyruvate^,. Biochemistry. 42(13). 3766–3776. 36 indexed citations

Shumilin, I.A., Chang Zhao, Ronald Bauerle, & Robert H. Kretsinger. (2002). Allosteric Inhibition of 3-Deoxy-d-arabino-heptulosonate-7-phosphate Synthase Alters the Coordination of Both Substrates. Journal of Molecular Biology. 320(5). 1147–1156. 44 indexed citations

Wagner, Trixie, Robert H. Kretsinger, Ronald Bauerle, & William D. Tolbert. (2000). 3-Deoxy- d - manno -octulosonate-8-phosphate synthase from Escherichia coli . Model of binding of phospho enol pyruvate and d -arabinose-5-phosphate 1 1Edited by D. Rees. Journal of Molecular Biology. 301(2). 233–238. 24 indexed citations

Wagner, Trixie, I.A. Shumilin, Ronald Bauerle, & Robert H. Kretsinger. (2000). Structure of 3-deoxy- d - arabino -heptulosonate-7-phosphate synthase from Escherichia coli : comparison of the Mn 2+ ∗2-phosphoglycolate and the Pb 2+ ∗2-Phospho enol pyruvate complexes and implications for catalysis 1 1Edited by D. Rees. Journal of Molecular Biology. 301(2). 389–399. 45 indexed citations

Shumilin, I.A., Robert H. Kretsinger, & Ronald Bauerle. (1999). Crystal structure of phenylalanine-regulated 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. Structure. 7(7). 865–875. 105 indexed citations

Tolbert, William D., et al.. (1999). Crystallization and preliminary crystallographic studies of the anthranilate synthase partial complex fromSalmonella typhimurium. Acta Crystallographica Section D Biological Crystallography. 55(1). 305–306. 3 indexed citations

Bauerle, Ronald, et al.. (1997). Steady-State Kinetics and Inhibitor Binding of 3-Deoxy-d-arabino-heptulosonate-7-phosphate Synthase (Tryptophan sensitive) from Escherichia coli. Biochemistry. 36(50). 15817–15822. 19 indexed citations

10.

Shumilin, I.A., Robert H. Kretsinger, & Ronald Bauerle. (1996). Purification, crystallization, and preliminary crystallographic analysis of 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase fromEscherichia coli. Proteins Structure Function and Bioinformatics. 24(3). 404–406. 12 indexed citations

11.

Tolbert, William D., Jonathan R. Moll, Ronald Bauerle, & Robert H. Kretsinger. (1996). Crystallization and preliminary crystallographic studies of 3-deoxy-D-manno-octulosonate-8-phosphate synthase fromEscherichia coli. Proteins Structure Function and Bioinformatics. 24(3). 407–408. 4 indexed citations

12.

Morollo, Anthony A., et al.. (1993). Isolation and structure determination of 2-amino-2-deoxyisochorismate: an intermediate in the biosynthesis of anthranilate. Journal of the American Chemical Society. 115(2). 816–817. 15 indexed citations

13.

Stephens, Craig & Ronald Bauerle. (1992). Essential cysteines in 3-deoxy-D-arabino-heptulosonate-7-phosphate synthase from Escherichia coli. Analysis by chemical modification and site-directed mutagenesis of the phenylalanine-sensitive isozyme.. Journal of Biological Chemistry. 267(9). 5762–5767. 23 indexed citations

14.

Caligiuri, Maureen & Ronald Bauerle. (1991). Subunit Communication in the Anthranilate Synthase Complex from Salmonella typhimurium. Science. 252(5014). 1845–1848. 36 indexed citations

15.

Kawasaki, Haruhiko, et al.. (1988). Site-directed mutagenesis of the α subunit of tryptophan synthase from salmonella typhimurium. Biochemical and Biophysical Research Communications. 151(2). 672–678. 12 indexed citations

16.

Bauerle, Ronald, John F. Hess, & Sarah L. French. (1987). [47] Anthranilate synthase—Anthranilate phosphoribosyltransferase complex and subunits of Salmonella typhimurium. Methods in enzymology on CD-ROM/Methods in enzymology. 142. 366–386. 45 indexed citations

17.

Bauerle, Ronald, et al.. (1980). CONDITIONALLY EXPRESSED MISSENSE MUTATIONS: THE BASIS FOR THE UNUSUAL PHENOTYPE OF AN APPARENT trpD NONSENSE MUTANT OF SALMONELLA TYPHIMURIUM. Genetics. 95(3). 545–559. 3 indexed citations

18.

Bauerle, Ronald, et al.. (1977). Internal reinitiation of translation in polar mutants of the trpB gene of Salmonella typhimurium. Molecular and General Genetics MGG. 153(2). 135–143. 10 indexed citations

19.

Grieshaber, Manfred K. & Ronald Bauerle. (1972). Structure and Evolution of a Bifunctional Enzyme of the Tryptophan Operon. Nature New Biology. 236(69). 232–235. 53 indexed citations

20.

Margolin, Paul & Ronald Bauerle. (1966). Determinants for Regulation and Initiation of Expression of Tryptophan Genes. Cold Spring Harbor Symposia on Quantitative Biology. 31(0). 311–320. 35 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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