Thomas E. Barman

1.2k total citations
30 papers, 1.0k citations indexed

About

Thomas E. Barman is a scholar working on Molecular Biology, Cell Biology and Cardiology and Cardiovascular Medicine. According to data from OpenAlex, Thomas E. Barman has authored 30 papers receiving a total of 1.0k indexed citations (citations by other indexed papers that have themselves been cited), including 17 papers in Molecular Biology, 7 papers in Cell Biology and 6 papers in Cardiology and Cardiovascular Medicine. Recurrent topics in Thomas E. Barman's work include Protein Structure and Dynamics (8 papers), Hemoglobin structure and function (6 papers) and Cardiomyopathy and Myosin Studies (6 papers). Thomas E. Barman is often cited by papers focused on Protein Structure and Dynamics (8 papers), Hemoglobin structure and function (6 papers) and Cardiomyopathy and Myosin Studies (6 papers). Thomas E. Barman collaborates with scholars based in France, United Kingdom and Germany. Thomas E. Barman's co-authors include Daniel E. Koshland, Franck Travers, Pierre Douzou, Claude Balny, Corinne Lionne, Raoul Bertrand, Chiara Tesi, Christian Herrmann, Robin Candau and Bogdan Iorga 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

Thomas E. Barman

30 papers receiving 930 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Thomas E. Barman France 17 615 153 124 120 102 30 1.0k
Jens G. Nørby Denmark 19 1.3k 2.0× 208 1.4× 57 0.5× 75 0.6× 45 0.4× 41 1.5k
Harvey Kaplan Canada 28 1.9k 3.1× 164 1.1× 323 2.6× 130 1.1× 78 0.8× 132 2.8k
A.G. Lee United Kingdom 22 1.5k 2.5× 120 0.8× 62 0.5× 56 0.5× 113 1.1× 45 1.9k
Rolf A. Løvstad Norway 16 509 0.8× 81 0.5× 31 0.3× 151 1.3× 151 1.5× 54 962
Morten J. Buch-Pedersen Denmark 17 1.1k 1.8× 150 1.0× 56 0.5× 104 0.9× 106 1.0× 26 1.6k
Florent Guillain France 26 1.4k 2.3× 191 1.2× 331 2.7× 78 0.7× 213 2.1× 47 1.8k
Kim Oikawa Canada 18 751 1.2× 270 1.8× 148 1.2× 71 0.6× 30 0.3× 33 1.1k
M. Rovery France 25 1.2k 1.9× 174 1.1× 35 0.3× 107 0.9× 88 0.9× 64 1.7k
Frits C. Stevens Canada 23 1.1k 1.8× 107 0.7× 86 0.7× 124 1.0× 48 0.5× 32 1.5k
Ivanov As Russia 22 944 1.5× 132 0.9× 45 0.4× 107 0.9× 83 0.8× 183 1.8k

Countries citing papers authored by Thomas E. Barman

Since Specialization
Citations

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

Fields of papers citing papers by Thomas E. Barman

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Thomas E. Barman. 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 Thomas E. Barman. The network helps show where Thomas E. Barman may publish in the future.

Co-authorship network of co-authors of Thomas E. Barman

This figure shows the co-authorship network connecting the top 25 collaborators of Thomas E. Barman. A scholar is included among the top collaborators of Thomas E. Barman 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 Thomas E. Barman. Thomas E. Barman 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.
Candau, Robin, Bogdan Iorga, Franck Travers, Thomas E. Barman, & Corinne Lionne. (2003). At Physiological Temperatures the ATPase Rates of Shortening Soleus and Psoas Myofibrils Are Similar. Biophysical Journal. 85(5). 3132–3141. 20 indexed citations
2.
Lionne, Corinne, Franck Travers, & Thomas E. Barman. (1996). Mechanochemical coupling in muscle: attempts to measure simultaneously shortening and ATPase rates in myofibrils. Biophysical Journal. 70(2). 887–895. 26 indexed citations
3.
Herrmann, Christian, et al.. (1992). Early steps of the magnesium-ATPase of relaxed myofibrils. A comparison with calcium-activated myofibrils and myosin subfragment 1. Biochemistry. 31(34). 8036–8042. 19 indexed citations
4.
Tesi, Chiara, Franck Travers, & Thomas E. Barman. (1990). Cryoenzymic studies on actomyosin ATPase. Evidence that the degree of saturation of actin with myosin subfragment 1 affects the kinetics of the binding of ATP. Biochemistry. 29(7). 1846–1852. 12 indexed citations
5.
Tesi, Chiara, et al.. (1989). Cryoenzymic studies on myosin: transient kinetic evidence for two types of head with different ATP binding properties. Biochimie. 71(3). 363–372. 13 indexed citations
6.
7.
Amemiya, Yoshiyuki, Y. Honda, Patrice Vachette, et al.. (1987). Kinetics of structure and activity changes during the allosteric transition of aspartate transcarbamylase. Journal of Molecular Biology. 198(4). 745–748. 9 indexed citations
8.
Balny, Claude, Franck Travers, Thomas E. Barman, & Pierre Douzou. (1987). Thermodynamics of the two step formation of horseradish peroxidase compound I. European Biophysics Journal. 14(6). 375–83. 34 indexed citations
9.
Barman, Thomas E., Franck Travers, Claude Balny, Gaston Hui Bon Hoa, & Pierre Douzou. (1986). New trends in cryoenzymology: Probing the functional role of protein dynamics by single-step kinetics. Biochimie. 68(9). 1041–1051. 14 indexed citations
10.
Barman, Thomas E. & Franck Travers. (1985). The Rapid‐Flow‐Quench Method in the Study of Fast Reactions in Biochemistry: Extension to Subzero Conditions. Methods of biochemical analysis. 31. 1–59. 41 indexed citations
11.
Kihara, Hiroshi, Thomas E. Barman, Patricia Jones, & Michael F. Moody. (1984). Kinetics of the allosteric transition of aspartate transcarbamylase chemical quench studies. Journal of Molecular Biology. 176(4). 523–534. 6 indexed citations
12.
Travers, Franck & Thomas E. Barman. (1980). Cryoenzymic Studies on the Transition‐State Analog Complex Creatine Kinase ‐ ADPMg ‐ Nitrate ‐ Creatine. European Journal of Biochemistry. 110(2). 405–412. 27 indexed citations
13.
Bertrand, Raoul, Thomas E. Barman, & Franck Travers. (1979). Substrate binding sites on arginine phosphokinase (Homarus vulgaris). Biochimie. 61(5-6). 705–709. 1 indexed citations
14.
Barman, Thomas E.. (1978). The Chemistry of the Reaction of 2-Hydroxy-5-nitrobenzyl Bromide with His-32 of alpha-Lactalbumin. European Journal of Biochemistry. 83(2). 465–471. 1 indexed citations
15.
Kitchen, Barry J. & Thomas E. Barman. (1973). Maleyl-α-lactalbumin as lactose synthetase specifier protein. Biochimica et Biophysica Acta (BBA) - Biomembranes. 298(4). 861–867. 5 indexed citations
16.
Barman, Thomas E.. (1973). The Isolation of an α‐Lactalbumin with Three Disulphide Bonds. European Journal of Biochemistry. 37(1). 86–89. 14 indexed citations
17.
18.
Barman, Thomas E.. (1970). Reactivities of the tryptophan residues of α-lactalbumin and lysozyme to 2-hydroxy-5-nitrobenzyl bromide. Journal of Molecular Biology. 52(2). 391–394. 27 indexed citations
19.
Barman, Thomas E.. (1969). Enzyme Handbook. 269 indexed citations
20.
Barman, Thomas E. & Daniel E. Koshland. (1967). A Colorimetric Procedure for the Quantitative Determination of Tryptophan Residues in Proteins. Journal of Biological Chemistry. 242(24). 5771–5776. 260 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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