Thomas C. Pochapsky

5.1k total citations · 1 hit paper
108 papers, 4.3k citations indexed

About

Thomas C. Pochapsky is a scholar working on Molecular Biology, Spectroscopy and Inorganic Chemistry. According to data from OpenAlex, Thomas C. Pochapsky has authored 108 papers receiving a total of 4.3k indexed citations (citations by other indexed papers that have themselves been cited), including 53 papers in Molecular Biology, 41 papers in Spectroscopy and 35 papers in Inorganic Chemistry. Recurrent topics in Thomas C. Pochapsky's work include Metal-Catalyzed Oxygenation Mechanisms (30 papers), Analytical Chemistry and Chromatography (22 papers) and Pharmacogenetics and Drug Metabolism (21 papers). Thomas C. Pochapsky is often cited by papers focused on Metal-Catalyzed Oxygenation Mechanisms (30 papers), Analytical Chemistry and Chromatography (22 papers) and Pharmacogenetics and Drug Metabolism (21 papers). Thomas C. Pochapsky collaborates with scholars based in United States, Argentina and United Kingdom. Thomas C. Pochapsky's co-authors include William H. Pirkle, Susan Sondej Pochapsky, Huaping Mo, Sophia Kazanis, Gayathri Ratnaswamy, Stephen G. Sligar, Iva Perovic, Tingting Ju, Dagmar Ringe and Michael J. Maroney and has published in prestigious journals such as Science, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

Thomas C. Pochapsky

107 papers receiving 4.1k citations

Hit Papers

Considerations of chiral recognition relevant to the liqu... 1989 2026 2001 2013 1989 250 500 750
What are hit papers?

Hit papers significantly outperform the citation benchmark for their cohort. A paper qualifies if it has ≥500 total citations, achieves ≥1.5× the top-1% citation threshold for papers in the same subfield and year (this is the minimum needed to enter the top 1%, not the average within it), or reaches the top citation threshold in at least one of its specific research topics.

  1. Considerations of chiral recognition relevant to the liquid chromatography separation of enantiomers
    1989 757 citations Thomas C. Pochapsky et al. profile →

Peers

Thomas C. Pochapsky
Graham Palmer United States
Stephen K. Chapman United Kingdom
Janez Mavri Slovenia
Stephen E. J. Rigby United Kingdom
Thomas Schräder Germany
David B. Goodin United States
Keiji Mori Japan
Joseph J. Villafranca United States
Masanori Sono United States
Graham Palmer United States
Thomas C. Pochapsky
Citations per year, relative to Thomas C. Pochapsky Thomas C. Pochapsky (= 1×) peers Graham Palmer

Countries citing papers authored by Thomas C. Pochapsky

Since Specialization
Citations

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

Fields of papers citing papers by Thomas C. Pochapsky

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Thomas C. Pochapsky

This figure shows the co-authorship network connecting the top 25 collaborators of Thomas C. Pochapsky. A scholar is included among the top collaborators of Thomas C. Pochapsky 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 C. Pochapsky. Thomas C. Pochapsky 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.
Estrada, D. Fernando, et al.. (2024). Tracking protein–protein interactions by NMR: conformational selection in human steroidogenic cytochrome P450 CYP17A1 induced by cytochrome b 5. Physical Chemistry Chemical Physics. 26(24). 16980–16988. 1 indexed citations
2.
Álvarez, Guadalupe, et al.. (2022). Hydroxylation Regiochemistry Is Robust to Active Site Mutations in Cytochrome P450cam (CYP101A1). Biochemistry. 61(17). 1790–1800. 3 indexed citations
3.
Liu, Xinyue, et al.. (2018). A new approach to understanding structure-function relationships in cytochromes P450 by targeting terpene metabolism in the wild. Journal of Inorganic Biochemistry. 188. 96–101. 4 indexed citations
4.
Pochapsky, Thomas C., et al.. (2016). Dual chemistry catalyzed by human acireductone dioxygenase. Protein Engineering Design and Selection. 30(3). 197–204. 11 indexed citations
5.
Pochapsky, Thomas C., et al.. (2016). Detection of substrate-dependent conformational changes in the P450 fold by nuclear magnetic resonance. Scientific Reports. 6(1). 22035–22035. 37 indexed citations
6.
Zhang, Ye, Ning Zhou, Junfeng Shi, et al.. (2015). Unfolding a molecular trefoil derived from a zwitterionic metallopeptide to form self-assembled nanostructures. Nature Communications. 6(1). 6165–6165. 31 indexed citations
7.
Li, Shengying, Florentine U. Rutaganira, P.M. Kells, et al.. (2012). Substrate Recognition by the Multifunctional Cytochrome P450 MycG in Mycinamicin Hydroxylation and Epoxidation Reactions. Journal of Biological Chemistry. 287(45). 37880–37890. 58 indexed citations
8.
Pochapsky, Susan Sondej, et al.. (2010). Spring-loading the active site of cytochrome P450cam. Metallomics. 3(4). 339–343. 12 indexed citations
9.
Hamuro, Yoshitomo, Kathleen S. Molnar, Stephen J. Coales, et al.. (2007). Hydrogen–deuterium exchange mass spectrometry for investigation of backbone dynamics of oxidized and reduced cytochrome P450cam. Journal of Inorganic Biochemistry. 102(2). 364–370. 17 indexed citations
10.
Pochapsky, Thomas C. & Susan Sondej Pochapsky. (2006). NMR for Physical and Biological Scientists. 9 indexed citations
11.
Ju, Tingting, et al.. (2006). One Protein, Two Enzymes Revisited: A Structural Entropy Switch Interconverts the Two Isoforms of Acireductone Dioxygenase. Journal of Molecular Biology. 363(4). 823–834. 49 indexed citations
12.
13.
Pochapsky, Thomas C., et al.. (2002). Modeling and experiment yields the structure of acireductone dioxygenase from Klebsiella pneumoniae. Nature Structural Biology. 9(12). 966–972. 68 indexed citations
14.
15.
Pochapsky, Thomas C., et al.. (1996). A structure-based model for cytochrome P450cam-putidaredoxin interactions. Biochimie. 78(8-9). 723–733. 82 indexed citations
16.
Ratnaswamy, Gayathri, et al.. (1996). Redox‐dependent dynamics of putidaredoxin characterized by amide proton exchange. Protein Science. 5(4). 627–639. 36 indexed citations
17.
Pochapsky, Thomas C., et al.. (1994). Redox-Dependent 1H NMR Spectral Features and Tertiary Structural Constraints on the C-Terminal Region of Putidaredoxin. Biochemistry. 33(21). 6433–6441. 26 indexed citations
18.
Lee, Kang‐Bong, et al.. (1993). Interpretation of hyperfine shift patterns in ferricytochromes b5 in terms of angular position of the heme: a sensitive probe for peripheral heme protein interactions. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology. 1202(2). 189–199. 25 indexed citations
19.
Pochapsky, Thomas C., et al.. (1991). Proton NMR identification of a .beta.-sheet structure and description of folding topology in putidaredoxin. Biochemistry. 30(16). 3850–3856. 21 indexed citations
20.
Mar, Gerd N. La, Ravindra K. Pandey, Irene Rezzano, et al.. (1991). Proton NMR study of the role of heme carboxylate side chains in modulating heme pocket structure and the mechanism of reconstitution of cytochrome b5. Biochemistry. 30(7). 1878–1887. 13 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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