Thomas S. Soper

792 total citations
24 papers, 649 citations indexed

About

Thomas S. Soper is a scholar working on Molecular Biology, Biochemistry and Materials Chemistry. According to data from OpenAlex, Thomas S. Soper has authored 24 papers receiving a total of 649 indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 13 papers in Biochemistry and 9 papers in Materials Chemistry. Recurrent topics in Thomas S. Soper's work include Amino Acid Enzymes and Metabolism (11 papers), Photosynthetic Processes and Mechanisms (9 papers) and Enzyme Structure and Function (9 papers). Thomas S. Soper is often cited by papers focused on Amino Acid Enzymes and Metabolism (11 papers), Photosynthetic Processes and Mechanisms (9 papers) and Enzyme Structure and Function (9 papers). Thomas S. Soper collaborates with scholars based in United States. Thomas S. Soper's co-authors include James M. Manning, Frank W. Larimer, Richard Mural, F.C. Hartman, Richard Machanoff, Fred C. Hartman, Wanda M. Jones, Robert S. Foote, Niyogi Sk and Christopher T. Walsh and has published in prestigious journals such as Journal of Biological Chemistry, Biochemistry and Biochemical and Biophysical Research Communications.

In The Last Decade

Thomas S. Soper

24 papers receiving 604 citations

Peers

Thomas S. Soper
François Talfournier France
Jodie E. Guy Sweden
H. Lauble Germany
Carlo A. Raia Italy
Matti Nikkola Sweden
Roberto Orrù Italy
B.M. Wood United States
V.V. Borisov Russia
Leonard B. Spector United States
L. M. Cunane United States
François Talfournier France
Thomas S. Soper
Citations per year, relative to Thomas S. Soper Thomas S. Soper (= 1×) peers François Talfournier

Countries citing papers authored by Thomas S. Soper

Since Specialization
Citations

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

Fields of papers citing papers by Thomas S. Soper

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Thomas S. Soper

This figure shows the co-authorship network connecting the top 25 collaborators of Thomas S. Soper. A scholar is included among the top collaborators of Thomas S. Soper 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 S. Soper. Thomas S. Soper 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.
Soper, Thomas S., et al.. (2003). Revisiting the steady state kinetic mechanism of glutamine-dependent asparagine synthetase from Escherichia coli. Archives of Biochemistry and Biophysics. 413(1). 23–31. 34 indexed citations
2.
Larimer, Frank W. & Thomas S. Soper. (1993). Overproduction of Anabaena 7120 ribulose-bisphosphate carboxylase/oxygenase in Escherichia coli. Gene. 126(1). 85–92. 32 indexed citations
3.
Larimer, Frank W., Richard Mural, & Thomas S. Soper. (1990). Versatile protein engineering vectors for mutagenesis, expression and hybrid enzyme formation. Protein Engineering Design and Selection. 3(3). 227–231. 25 indexed citations
4.
5.
Soper, Thomas S., et al.. (1988). Essentiality of Lys-329 of ribulose-1,5-bisphosphate carboxylase/oxygenase from Rhodospirillum rubrum as demonstrated by site-directed mutagenesis. Protein Engineering Design and Selection. 2(1). 39–44. 38 indexed citations
6.
Niyogi, Salil K., Thomas S. Soper, Robert S. Foote, et al.. (1987). Site-directed mutagenesis to determine essential residues of ribulose-bisphosphate carboxylase ofRhodospirillum rubrum. Journal of Biosciences. 11(1-4). 203–214. 2 indexed citations
7.
Larimer, Frank W., et al.. (1987). Intersubunit location of the active site of ribulose-bisphosphate carboxylase/oxygenase as determined by in vivo hybridization of site-directed mutants.. Journal of Biological Chemistry. 262(32). 15327–15329. 60 indexed citations
8.
Hartman, F.C., Thomas S. Soper, Niyogi Sk, et al.. (1987). Function of Lys-166 of Rhodospirillum rubrum ribulosebisphosphate carboxylase/oxygenase as examined by site-directed mutagenesis.. Journal of Biological Chemistry. 262(8). 3496–3501. 50 indexed citations
9.
Hartman, Fred C., Frank W. Larimer, Richard Mural, Richard Machanoff, & Thomas S. Soper. (1987). Essentiality of Glu-48 of ribulose bisphosphate carboxylase/oxygenase as demonstrated by site-directed mutagenesis. Biochemical and Biophysical Research Communications. 145(3). 1158–1163. 23 indexed citations
10.
Sk, Niyogi, Robert S. Foote, Richard Mural, et al.. (1986). Nonessentiality of histidine 291 of Rhodospirillum rubrum ribulose-bisphosphate carboxylase/oxygenase as determined by site-directed mutagenesis.. Journal of Biological Chemistry. 261(22). 10087–10092. 60 indexed citations
11.
Jones, Wanda M., Thomas S. Soper, Hiroshi Ueno, & James M. Manning. (1985). [21] d-glutamate-d-amino acid transaminase from bacteria. Methods in enzymology on CD-ROM/Methods in enzymology. 113. 108–113. 18 indexed citations
12.
Soper, Thomas S., Hiroshi Ueno, & James M. Manning. (1985). Substrate-induced changes in sulfhydryl reactivity of bacterial d-amino acid transaminase. Archives of Biochemistry and Biophysics. 240(1). 1–8. 5 indexed citations
13.
Soper, Thomas S. & James M. Manning. (1982). Inactivation of pyridoxal phosphate enzymes by gabaculine. Correlation with enzymic exchange of beta-protons.. Journal of Biological Chemistry. 257(23). 13930–13936. 48 indexed citations
14.
Soper, Thomas S. & James M. Manning. (1981). Different modes of action of inhibitors of bacterial D-amino acid transaminase. A target enzyme for the design of new antibacterial agents.. Journal of Biological Chemistry. 256(9). 4263–4268. 37 indexed citations
15.
Soper, Thomas S., Wanda M. Jones, & James M. Manning. (1979). Effects of substrates on the selective modification of the cysteinyl residues of D-amino acid transaminase.. Journal of Biological Chemistry. 254(21). 10901–10905. 12 indexed citations
16.
17.
Soper, Thomas S., James M. Manning, Patrick A. Marcotte, & Christopher T. Walsh. (1977). Inactivation of bacterial D-amino acid transaminases by the olefinic amino acid D-vinylglycine.. Journal of Biological Chemistry. 252(5). 1571–1575. 48 indexed citations
18.
Soper, Thomas S., et al.. (1977). Inactivation of bacterial D-amino acid transaminase by beta-chloro-D-alanine.. Journal of Biological Chemistry. 252(10). 3170–3175. 35 indexed citations
19.
Soper, Thomas S. & James M. Manning. (1976). Synergy in the Antimicrobial Action of Penicillin and β-Chloro- d -Alanine In Vitro. Antimicrobial Agents and Chemotherapy. 9(2). 347–349. 8 indexed citations
20.
Soper, Thomas S., George J. Doellgast, & Gunter B. Kohlhaw. (1976). Mechanism of feedback inhibition by leucine. Archives of Biochemistry and Biophysics. 173(1). 362–374. 15 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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