T. Joseph Kappock

1.9k total citations
35 papers, 1.5k citations indexed

About

T. Joseph Kappock is a scholar working on Molecular Biology, Materials Chemistry and Inorganic Chemistry. According to data from OpenAlex, T. Joseph Kappock has authored 35 papers receiving a total of 1.5k indexed citations (citations by other indexed papers that have themselves been cited), including 30 papers in Molecular Biology, 17 papers in Materials Chemistry and 6 papers in Inorganic Chemistry. Recurrent topics in T. Joseph Kappock's work include Enzyme Structure and Function (17 papers), Porphyrin Metabolism and Disorders (10 papers) and Biochemical and Molecular Research (10 papers). T. Joseph Kappock is often cited by papers focused on Enzyme Structure and Function (17 papers), Porphyrin Metabolism and Disorders (10 papers) and Biochemical and Molecular Research (10 papers). T. Joseph Kappock collaborates with scholars based in United States, Sweden and Spain. T. Joseph Kappock's co-authors include John P. Caradonna, JoAnne Stubbe, Julie A. Francois, E.A. Mullins, Ao Pung, Robert V. Cooney, S.E. Ealick, John S. Bertram, S. E. Ealick and JoAnne Stubbe and has published in prestigious journals such as Chemical Reviews, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

T. Joseph Kappock

35 papers receiving 1.5k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
T. Joseph Kappock United States 21 1.1k 396 222 189 125 35 1.5k
Harry W. Duckworth Canada 23 1.0k 0.9× 434 1.1× 80 0.4× 47 0.2× 115 0.9× 56 1.7k
Maria Krook Sweden 15 1.6k 1.5× 495 1.3× 22 0.1× 233 1.2× 137 1.1× 18 2.4k
Fabien Pierrel France 32 1.8k 1.7× 126 0.3× 33 0.1× 214 1.1× 78 0.6× 56 2.6k
Jeremy N. S. Evans United States 17 1.0k 0.9× 362 0.9× 41 0.2× 38 0.2× 35 0.3× 46 1.7k
Alexander Dikiy Norway 23 896 0.8× 307 0.8× 30 0.1× 217 1.1× 12 0.1× 60 1.7k
Charles A. Roessner United States 29 1.6k 1.4× 238 0.6× 16 0.1× 45 0.2× 76 0.6× 58 1.9k
Sergio Martínez‐Rodríguez Spain 21 1.1k 1.0× 400 1.0× 73 0.3× 17 0.1× 19 0.2× 77 1.8k
Javier López-Jaramillo Spain 28 1.4k 1.3× 310 0.8× 26 0.1× 54 0.3× 26 0.2× 67 2.4k
Miaomiao Wang China 24 1.5k 1.3× 338 0.9× 46 0.2× 22 0.1× 23 0.2× 95 2.2k

Countries citing papers authored by T. Joseph Kappock

Since Specialization
Citations

This map shows the geographic impact of T. Joseph Kappock'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 T. Joseph Kappock with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites T. Joseph Kappock more than expected).

Fields of papers citing papers by T. Joseph Kappock

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by T. Joseph Kappock. 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 T. Joseph Kappock. The network helps show where T. Joseph Kappock may publish in the future.

Co-authorship network of co-authors of T. Joseph Kappock

This figure shows the co-authorship network connecting the top 25 collaborators of T. Joseph Kappock. A scholar is included among the top collaborators of T. Joseph Kappock 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 T. Joseph Kappock. T. Joseph Kappock 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.
Mullins, E.A., et al.. (2016). Functional Dissection of the Bipartite Active Site of the Class I Coenzyme A (CoA)-Transferase Succinyl-CoA:Acetate CoA-Transferase. Frontiers in Chemistry. 4. 23–23. 4 indexed citations
2.
Donini, Stefano, et al.. (2015). An active site–tail interaction in the structure of hexahistidine-taggedThermoplasma acidophilumcitrate synthase. Acta Crystallographica Section F Structural Biology Communications. 71(10). 1292–1299. 6 indexed citations
3.
Sullivan, Kelly L., et al.. (2014). Metal stopping reagents facilitate discontinuous activity assays of the de novo purine biosynthesis enzyme PurE. Analytical Biochemistry. 452. 43–45. 4 indexed citations
4.
Mill, Christopher P., Sandra W. Clifton, Vincent Magrini, et al.. (2014). Draft Genome Sequence of Acetobacter aceti Strain 1023, a Vinegar Factory Isolate. Genome Announcements. 2(3). 5 indexed citations
5.
Lamb, Audrey L., T. Joseph Kappock, & N.R. Silvaggi. (2014). You are lost without a map: Navigating the sea of protein structures. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics. 1854(4). 258–268. 19 indexed citations
6.
Mullins, E.A., Kelly L. Sullivan, & T. Joseph Kappock. (2013). Function and X-Ray crystal structure of Escherichia coli YfdE. PLoS ONE. 8(7). e67901–e67901. 11 indexed citations
7.
Mullins, E.A. & T. Joseph Kappock. (2013). Functional analysis of the acetic acid resistance (aar) gene cluster in Acetobacter aceti strain 1023. Purdue e-Pubs (Purdue University System). 2(1s). 3–3. 11 indexed citations
8.
Mullins, E.A., Courtney M. Starks, Julie A. Francois, et al.. (2012). Formyl‐coenzyme A (CoA):oxalate CoA‐transferase from the acidophile Acetobacter aceti has a distinctive electrostatic surface and inherent acid stability. Protein Science. 21(5). 686–696. 18 indexed citations
10.
Pérez‐Jiménez, Raúl, Álvaro Inglés‐Prieto, Ziming Zhao, et al.. (2011). Single-molecule paleoenzymology probes the chemistry of resurrected enzymes. Nature Structural & Molecular Biology. 18(5). 592–596. 155 indexed citations
12.
Nam, Jeong‐Won & T. Joseph Kappock. (2007). Cloning and transcriptional analysis of Crepis alpina fatty acid desaturases affecting the biosynthesis of crepenynic acid. Journal of Experimental Botany. 58(6). 1421–1432. 13 indexed citations
13.
Francois, Julie A. & T. Joseph Kappock. (2006). Alanine racemase from the acidophile Acetobacter aceti. Protein Expression and Purification. 51(1). 39–48. 22 indexed citations
14.
Francois, Julie A., et al.. (2006). Structure of a NADH-Insensitive Hexameric Citrate Synthase that Resists Acid Inactivation. Biochemistry. 45(45). 13487–13499. 43 indexed citations
15.
Starks, Courtney M., et al.. (2006). Atomic‐resolution crystal structure of thioredoxin from the acidophilic bacterium Acetobacter aceti. Protein Science. 16(1). 92–98. 11 indexed citations
16.
Settembre, Ethan C., Johnathan Chittuluru, Christopher P. Mill, T. Joseph Kappock, & S.E. Ealick. (2004). Acidophilic adaptations in the structure ofAcetobacter aceti N5-carboxyaminoimidazole ribonucleotide mutase (PurE). Acta Crystallographica Section D Biological Crystallography. 60(10). 1753–1760. 20 indexed citations
17.
Kappock, T. Joseph, S. E. Ealick, & JoAnne Stubbe. (2000). Modular evolution of the purine biosynthetic pathway. Current Opinion in Chemical Biology. 4(5). 567–572. 81 indexed citations
19.
Mathews, Irimpan I., T. Joseph Kappock, JoAnne Stubbe, & S.E. Ealick. (1999). Crystal structure of Escherichia coli PurE, an unusual mutase in the purine biosynthetic pathway. Structure. 7(11). 1395–1406. 42 indexed citations
20.
Kappock, T. Joseph, et al.. (1995). Spectroscopic and Kinetic Properties of Unphosphorylated Rat Hepatic Phenylalanine Hydroxylase Expressed in Escherichia coli. Journal of Biological Chemistry. 270(51). 30532–30544. 42 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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