Mark L. Paddock

3.0k total citations
53 papers, 2.3k citations indexed

About

Mark L. Paddock is a scholar working on Molecular Biology, Renewable Energy, Sustainability and the Environment and Atomic and Molecular Physics, and Optics. According to data from OpenAlex, Mark L. Paddock has authored 53 papers receiving a total of 2.3k indexed citations (citations by other indexed papers that have themselves been cited), including 40 papers in Molecular Biology, 25 papers in Renewable Energy, Sustainability and the Environment and 17 papers in Atomic and Molecular Physics, and Optics. Recurrent topics in Mark L. Paddock's work include Photosynthetic Processes and Mechanisms (27 papers), Metalloenzymes and iron-sulfur proteins (23 papers) and Spectroscopy and Quantum Chemical Studies (17 papers). Mark L. Paddock is often cited by papers focused on Photosynthetic Processes and Mechanisms (27 papers), Metalloenzymes and iron-sulfur proteins (23 papers) and Spectroscopy and Quantum Chemical Studies (17 papers). Mark L. Paddock collaborates with scholars based in United States, Israel and France. Mark L. Paddock's co-authors include Patricia A. Jennings, Rachel Nechushtai, M. Y. Okamura, Edward C. Abresch, Andrea R. Conlan, G. Fehér, John A. Zuris, Ron Mittler, José N. Onuchic and Herbert L. Axelrod and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of the American Chemical Society and Journal of Biological Chemistry.

In The Last Decade

Mark L. Paddock

52 papers receiving 2.3k citations

Peers — A (Enhanced Table)

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

Name	h						Papers	Cites
Mark L. Paddock United States	27	1.5k	968	372	308	239	53	2.3k
Edward C. Abresch United States	25	1.7k 1.1×	504 0.5×	283 0.8×	751 2.4×	365 1.5×	38	2.3k
Mario Piccioli Italy	31	1.7k 1.1×	993 1.0×	752 2.0×	95 0.3×	752 3.1×	115	3.1k
Barry D. Howes Italy	28	1.4k 0.9×	326 0.3×	297 0.8×	139 0.5×	340 1.4×	82	2.3k
John C. Salerno United States	31	1.4k 0.9×	213 0.2×	293 0.8×	76 0.2×	173 0.7×	75	2.5k
D.P. Barondeau United States	28	1.6k 1.0×	770 0.8×	345 0.9×	17 0.1×	354 1.5×	41	2.5k
Russell LoBrutto United States	24	850 0.6×	250 0.3×	547 1.5×	158 0.5×	257 1.1×	48	1.5k
Tony A. Mattioli France	31	1.3k 0.9×	494 0.5×	740 2.0×	528 1.7×	467 2.0×	72	2.3k
Lothar Gremer Germany	32	2.6k 1.7×	797 0.8×	440 1.2×	22 0.1×	512 2.1×	83	4.3k
Margareta Nordling Sweden	26	1.0k 0.7×	121 0.1×	166 0.4×	105 0.3×	124 0.5×	50	1.9k
Tina Howard United Kingdom	19	2.3k 1.5×	276 0.3×	70 0.2×	667 2.2×	332 1.4×	29	2.9k

Countries citing papers authored by Mark L. Paddock

Since Specialization

Citations

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

Fields of papers citing papers by Mark L. Paddock

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Mark L. Paddock. 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 Mark L. Paddock. The network helps show where Mark L. Paddock may publish in the future.

Co-authorship network of co-authors of Mark L. Paddock

This figure shows the co-authorship network connecting the top 25 collaborators of Mark L. Paddock. A scholar is included among the top collaborators of Mark L. Paddock 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 Mark L. Paddock. Mark L. Paddock is excluded from the visualization to improve readability, since they are connected to all nodes in the network.

All Works

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20 of 20 papers shown

Lipper, Colin H., Mark L. Paddock, José N. Onuchic, et al.. (2015). Cancer-Related NEET Proteins Transfer 2Fe-2S Clusters to Anamorsin, a Protein Required for Cytosolic Iron-Sulfur Cluster Biogenesis. PLoS ONE. 10(10). e0139699–e0139699. 69 indexed citations

Tamir, Sagi, Mark L. Paddock, Sarah H. Holt, et al.. (2014). Structure–function analysis of NEET proteins uncovers their role as key regulators of iron and ROS homeostasis in health and disease. Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1853(6). 1294–1315. 131 indexed citations

Shultzaberger, Ryan K., Mark L. Paddock, Takeo Katsuki, Ralph J. Greenspan, & Susan S. Golden. (2014). High-Throughput and Quantitative Approaches for Measuring Circadian Rhythms in Cyanobacteria Using Bioluminescence. Methods in enzymology on CD-ROM/Methods in enzymology. 551. 53–72. 3 indexed citations

Tamir, Sagi, Y. Eisenberg-Domovich, Andrea R. Conlan, et al.. (2014). A point mutation in the [2Fe–2S] cluster binding region of the NAF-1 protein (H114C) dramatically hinders the cluster donor properties. Acta Crystallographica Section D Biological Crystallography. 70(6). 1572–1578. 29 indexed citations

Tamir, Sagi, John A. Zuris, Colin H. Lipper, et al.. (2013). Nutrient-Deprivation Autophagy Factor-1 (NAF-1): Biochemical Properties of a Novel Cellular Target for Anti-Diabetic Drugs. PLoS ONE. 8(5). e61202–e61202. 42 indexed citations

Baxter, E.L., John A. Zuris, Charles Wang, et al.. (2012). Allosteric control in a metalloprotein dramatically alters function. Proceedings of the National Academy of Sciences. 110(3). 948–953. 23 indexed citations

Zuris, John A., et al.. (2012). NADPH Inhibits [2Fe-2S] Cluster Protein Transfer from Diabetes Drug Target MitoNEET to an Apo-acceptor Protein. Journal of Biological Chemistry. 287(15). 11649–11655. 26 indexed citations

Conlan, Andrea R., Mark L. Paddock, Christina M. Homer, et al.. (2011). Mutation of the His ligand in mitoNEET stabilizes the 2Fe–2S cluster despite conformational heterogeneity in the ligand environment. Acta Crystallographica Section D Biological Crystallography. 67(6). 516–523. 23 indexed citations

Flores, Marco, R. A. Isaacson, Jennifer N. Shepherd, Mark L. Paddock, & M. Y. Okamura. (2010). Endor Spectrum of the Protonated Rhodosemiquinone in Bacterial Reaction Centers. Biophysical Journal. 98(3). 173a–173a. 1 indexed citations

10.

Homer, Christina M., Herbert L. Axelrod, Aina E. Cohen, et al.. (2009). Structural Basis for Phosphate Stabilization of the Uniquely Coordinated 2Fe-2S Cluster of the Outer Mitochondrial Membrane Protein MitoNEET.∗. Biophysical Journal. 96(3). 442a–443a. 4 indexed citations

11.

Zuris, John A., Mark L. Paddock, Edward C. Abresch, et al.. (2009). Redox Potential of the Outer-Mitochondrial Membrane 2Fe-2S Protein MitoNEET. Biophysical Journal. 96(3). 240a–240a. 4 indexed citations

12.

Conlan, Andrea R., Mark L. Paddock, Herbert L. Axelrod, et al.. (2009). The novel 2Fe–2S outer mitochondrial protein mitoNEET displays conformational flexibility in its N-terminal cytoplasmic tethering domain. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(7). 654–659. 20 indexed citations

13.

Conlan, Andrea R., Herbert L. Axelrod, Aina E. Cohen, et al.. (2009). Crystal Structure of Miner1: The Redox-active 2Fe-2S Protein Causative in Wolfram Syndrome 2. Journal of Molecular Biology. 392(1). 143–153. 104 indexed citations

14.

Conlan, Andrea R., Herbert L. Axelrod, Aina E. Cohen, et al.. (2009). Structural Comparison Of A Diabetes Drug Target, Mitoneet, A 2Fe-2S Cluster Protein To Its More Stable Mutant, H87C. Biophysical Journal. 96(3). 67a–67a. 5 indexed citations

15.

Paddock, Mark L., Sandra E. Wiley, Herbert L. Axelrod, et al.. (2007). MitoNEET is a uniquely folded 2Fe–2S outer mitochondrial membrane protein stabilized by pioglitazone. Proceedings of the National Academy of Sciences. 104(36). 14342–14347. 228 indexed citations

16.

Mezzetti, Alberto, Eliane Nabedryk, Jacques Breton, et al.. (2002). Rapid-scan Fourier transform infrared spectroscopy shows coupling of GLu-L212 protonation and electron transfer to QB in Rhodobacter sphaeroides reaction centers. Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1553(3). 320–330. 35 indexed citations

17.

Beatty, J. Thomas, et al.. (2000). Effect of Metal Binding on Electrogenic Proton Transfer Associated with Reduction of the Secondary Electron Acceptor (Q_B) in Rhodobacter sphaeroides Chromatophores. Biochemistry. 40(2). 429–439. 10 indexed citations

18.

Chirino, Arthur J., E. J. Lous, Martina Huber, et al.. (1994). Crystallographic Analyses of Site-Directed Mutants of the Photosynthetic Reaction Center from Rhodobacter sphaeroides. Biochemistry. 33(15). 4584–4593. 128 indexed citations

19.

Paddock, Mark L., G. Fehér, & M. Y. Okamura. (1991). Reaction centers from three herbicide resistant mutants of Rhodobacter sphaeroides 2.4.1: Kinetics of electron transfer reactions. Photosynthesis Research. 27(2). 109–119. 9 indexed citations

20.

Paddock, Mark L., S. H. Rongey, Edward C. Abresch, G. Fehér, & M. Y. Okamura. (1988). Reaction centers from three herbicide-resistant mutants of Rhodobacter sphaeroides 2.4.1: sequence analysis and preliminary characterization. Photosynthesis Research. 17(1-2). 75–96. 54 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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