Jonathan D. Caranto

1.5k total citations
26 papers, 1.2k citations indexed

About

Jonathan D. Caranto is a scholar working on Molecular Biology, Cell Biology and Inorganic Chemistry. According to data from OpenAlex, Jonathan D. Caranto has authored 26 papers receiving a total of 1.2k indexed citations (citations by other indexed papers that have themselves been cited), including 12 papers in Molecular Biology, 10 papers in Cell Biology and 10 papers in Inorganic Chemistry. Recurrent topics in Jonathan D. Caranto's work include Hemoglobin structure and function (10 papers), Metal-Catalyzed Oxygenation Mechanisms (9 papers) and Photosynthetic Processes and Mechanisms (6 papers). Jonathan D. Caranto is often cited by papers focused on Hemoglobin structure and function (10 papers), Metal-Catalyzed Oxygenation Mechanisms (9 papers) and Photosynthetic Processes and Mechanisms (6 papers). Jonathan D. Caranto collaborates with scholars based in United States, Germany and Romania. Jonathan D. Caranto's co-authors include Kyle M. Lancaster, Donald M. Kurtz, Avery Vilbert, Andrew C. Weitz, Michael P. Hendrich, Pierre Moënne‐Loccoz, Takahiro Hayashi, David Wampler, Carlos D. García and Hirotoshi Matsumura 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

Jonathan D. Caranto

26 papers receiving 1.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Jonathan D. Caranto United States 17 382 335 277 230 185 26 1.2k
David M. Arciero United States 23 622 1.6× 691 2.1× 220 0.8× 289 1.3× 340 1.8× 33 1.5k
Sofia R. Pauleta Portugal 21 169 0.4× 414 1.2× 290 1.0× 117 0.5× 179 1.0× 66 1.2k
D.M. Arciero United States 18 686 1.8× 865 2.6× 384 1.4× 333 1.4× 301 1.6× 20 1.7k
Taketomo Fujiwara Japan 23 321 0.8× 892 2.7× 81 0.3× 362 1.6× 197 1.1× 66 1.6k
David J. Richardson United Kingdom 26 677 1.8× 652 1.9× 97 0.4× 481 2.1× 576 3.1× 52 1.9k
Heinz Körner Germany 11 407 1.1× 566 1.7× 91 0.3× 329 1.4× 270 1.5× 12 1.3k
Scott A. Ensign United States 30 551 1.4× 1.3k 4.0× 264 1.0× 223 1.0× 207 1.1× 56 2.1k
Pablo J. González Argentina 23 150 0.4× 424 1.3× 350 1.3× 97 0.4× 144 0.8× 61 1.4k
Kurt Frunzke Germany 13 215 0.6× 292 0.9× 71 0.3× 173 0.8× 148 0.8× 15 689
Frauke Baymann France 22 196 0.5× 968 2.9× 107 0.4× 223 1.0× 246 1.3× 41 1.5k

Countries citing papers authored by Jonathan D. Caranto

Since Specialization
Citations

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

Fields of papers citing papers by Jonathan D. Caranto

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Jonathan D. Caranto. 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 Jonathan D. Caranto. The network helps show where Jonathan D. Caranto may publish in the future.

Co-authorship network of co-authors of Jonathan D. Caranto

This figure shows the co-authorship network connecting the top 25 collaborators of Jonathan D. Caranto. A scholar is included among the top collaborators of Jonathan D. Caranto 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 Jonathan D. Caranto. Jonathan D. Caranto 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.
Martin, Christopher P., Jonathan D. Caranto, Parag Banerjee, et al.. (2024). Multivariate Analysis on the Structure–Activity Parameters for Nano-CuOx-Catalyzed Reduction Reactions. ACS Applied Nano Materials. 7(1). 928–939. 2 indexed citations
2.
Wagner, S A, et al.. (2024). Activity assays of NnlA homologs suggest the natural product N -nitroglycine is degraded by diverse bacteria. Beilstein Journal of Organic Chemistry. 20. 830–840. 1 indexed citations
3.
Logan, Matthew W., Zhihengyu Chen, Demetrius A. Vazquez-Molina, et al.. (2023). Synergistic Steric and Electronic Effects on the Photoredox Catalysis by a Multivariate Library of Titania Metal–Organic Frameworks. Journal of the American Chemical Society. 145(8). 4589–4600. 40 indexed citations
4.
Beazley, Melanie J., et al.. (2022). Reduction of a Heme Cofactor Initiates N -Nitroglycine Degradation by NnlA. Applied and Environmental Microbiology. 88(16). e0102322–e0102322. 2 indexed citations
5.
Anagnostopoulos, Vasileios, et al.. (2022). The hemerythrin-like diiron protein from Mycobacterium kansasii is a nitric oxide peroxidase. Journal of Biological Chemistry. 298(3). 101696–101696. 5 indexed citations
6.
Martin, Christopher P., et al.. (2021). The Ferric-Superoxo Intermediate of the TxtE Nitration Pathway Resists Reduction, Facilitating Its Reaction with Nitric Oxide. Biochemistry. 60(31). 2436–2446. 11 indexed citations
7.
Caranto, Jonathan D.. (2019). The emergence of nitric oxide in the biosynthesis of bacterial natural products. Current Opinion in Chemical Biology. 49. 130–138. 26 indexed citations
8.
Dong, Min, Michael K. Fenwick, Andrew T. Torelli, et al.. (2018). Organometallic and radical intermediates reveal mechanism of diphthamide biosynthesis. Science. 359(6381). 1247–1250. 53 indexed citations
9.
Lancaster, Kyle M., et al.. (2018). Alternative Bioenergy: Updates to and Challenges in Nitrification Metalloenzymology. Joule. 2(3). 421–441. 92 indexed citations
10.
Weitz, Andrew C., et al.. (2017). Spectroscopy and DFT Calculations of a Flavo-diiron Enzyme Implicate New Diiron Site Structures. Journal of the American Chemical Society. 139(34). 12009–12019. 29 indexed citations
11.
Caranto, Jonathan D. & Kyle M. Lancaster. (2017). Nitric oxide is an obligate bacterial nitrification intermediate produced by hydroxylamine oxidoreductase. Proceedings of the National Academy of Sciences. 114(31). 8217–8222. 344 indexed citations
12.
Vilbert, Avery, Jonathan D. Caranto, & Kyle M. Lancaster. (2017). Influences of the heme-lysine crosslink in cytochrome P460 over redox catalysis and nitric oxide sensitivity. Chemical Science. 9(2). 368–379. 24 indexed citations
13.
Caranto, Jonathan D., Avery Vilbert, & Kyle M. Lancaster. (2016). Nitrosomonas europaea cytochrome P460 is a direct link between nitrification and nitrous oxide emission. Proceedings of the National Academy of Sciences. 113(51). 14704–14709. 164 indexed citations
14.
Caranto, Jonathan D., Andrew C. Weitz, Michael P. Hendrich, & Donald M. Kurtz. (2014). The Nitric Oxide Reductase Mechanism of a Flavo-Diiron Protein: Identification of Active-Site Intermediates and Products. Journal of the American Chemical Society. 136(22). 7981–7992. 63 indexed citations
15.
Han, Fang, et al.. (2012). Histidine ligand variants of a flavo-diiron protein: effects on structure and activities. JBIC Journal of Biological Inorganic Chemistry. 17(8). 1231–1239. 31 indexed citations
16.
Caranto, Jonathan D., et al.. (2012). Treponema denticola Superoxide Reductase: In Vivo Role, in Vitro Reactivities, and a Novel [Fe(Cys)4] Site. Biochemistry. 51(28). 5601–5610. 9 indexed citations
17.
Hayashi, Takahiro, Jonathan D. Caranto, Hirotoshi Matsumura, Donald M. Kurtz, & Pierre Moënne‐Loccoz. (2012). Vibrational Analysis of Mononitrosyl Complexes in Hemerythrin and Flavodiiron Proteins: Relevance to Detoxifying NO Reductase. Journal of the American Chemical Society. 134(15). 6878–6884. 47 indexed citations
18.
Caranto, Jonathan D., et al.. (2010). Adsorption Kinetics of Catalase to Thin Films of Carbon Nanotubes. Langmuir. 26(22). 17178–17183. 34 indexed citations
19.
Hillmann, Falk, et al.. (2008). Reductive dioxygen scavenging by flavo‐diiron proteins of Clostridium acetobutylicum. FEBS Letters. 583(1). 241–245. 41 indexed citations
20.
Leone, Amanda, Jennifer Jihye Chun, Christopher L. Koehler, Jonathan D. Caranto, & Jonathan M. King. (2007). Effect of Proinflammatory Cytokines, Tumor Necrosis Factor-α and Interferon-γ on Epithelial Barrier Function and Matrix Metalloproteinase-9 in Madin Darby Canine Kidney Cells. Cellular Physiology and Biochemistry. 19(1-4). 99–112. 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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