Frank Jordan
About
Frank Jordan is a scholar working on Biochemistry, Molecular Biology and Clinical Biochemistry.
According to data from OpenAlex, Frank Jordan has authored 266 papers receiving a total of 8.7k indexed citations (citations by other indexed papers that have themselves been cited), including 137 papers in Biochemistry, 96 papers in Molecular Biology and 95 papers in Clinical Biochemistry. Recurrent topics in Frank Jordan's work include Biochemical Acid Research Studies (134 papers), Metabolism and Genetic Disorders (94 papers) and Alcoholism and Thiamine Deficiency (79 papers). Frank Jordan is often cited by papers focused on Biochemical Acid Research Studies (134 papers), Metabolism and Genetic Disorders (94 papers) and Alcoholism and Thiamine Deficiency (79 papers). Frank Jordan collaborates with scholars based in United States, Germany and Netherlands. Frank Jordan's co-authors include Natalia S. Nemeria, William Furey, Michal Szostak, Pradeep Nareddy, Mulchand S. Patel, Masayori Inouye, Palaniappa Arjunan, Jean‐Paul Malrieu, M. Gilbert and Eduard Sergienko and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of the American Chemical Society.
In The Last Decade
Frank Jordan
260 papers receiving 8.4k citations
Hit Papers
Peers — A (Enhanced Table)
Peers by citation overlap · career bar shows stage (early→late) cites · hero ref
| Name | h | Career | Trend | Papers | Cites | |||||
|---|---|---|---|---|---|---|---|---|---|---|
| Frank Jordan United States | 46 | 3.4k | 3.4k | 2.1k | 2.0k | 1.9k | 266 | 8.7k | ||
| Dagmar Ringe United States | 69 | 10.5k 3.1× | 1.5k 0.4× | 579 0.3× | 1.7k 0.8× | 1.2k 0.7× | 230 | 16.2k | ||
| Donald B. McCormick United States | 39 | 2.1k 0.6× | 1.1k 0.3× | 1.1k 0.5× | 267 0.1× | 614 0.3× | 238 | 5.3k | ||
| B. H. Robinson Canada | 42 | 3.5k 1.0× | 787 0.2× | 2.0k 1.0× | 139 0.1× | 856 0.5× | 153 | 6.1k | ||
| Efraim Racker United States | 64 | 11.9k 3.5× | 1.1k 0.3× | 1.2k 0.6× | 170 0.1× | 500 0.3× | 164 | 15.2k | ||
| Gustav E. Lienhard United States | 69 | 11.3k 3.3× | 1.1k 0.3× | 473 0.2× | 301 0.2× | 650 0.3× | 143 | 15.2k | ||
| Bernhard Witkop United States | 56 | 6.0k 1.8× | 945 0.3× | 324 0.2× | 217 0.1× | 3.5k 1.9× | 296 | 11.9k | ||
| William Furey United States | 38 | 2.0k 0.6× | 1.5k 0.4× | 924 0.4× | 941 0.5× | 330 0.2× | 86 | 6.2k | ||
| Esmond E. Snell United States | 53 | 6.3k 1.9× | 3.1k 0.9× | 1.1k 0.5× | 131 0.1× | 1.2k 0.6× | 242 | 10.0k | ||
| Youssef Hatefi United States | 57 | 9.3k 2.7× | 957 0.3× | 1.5k 0.7× | 102 0.1× | 563 0.3× | 190 | 11.6k | ||
| Torgeir Flatmark Norway | 49 | 5.0k 1.5× | 791 0.2× | 2.0k 0.9× | 313 0.2× | 179 0.1× | 231 | 7.8k |
Countries citing papers authored by Frank Jordan
Since
Specialization
Citations
This map shows the geographic impact of Frank Jordan'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 Frank Jordan with the expected number of citations based on a country's size and research output (numbers larger than one mean the country cites Frank Jordan more than expected).
Fields of papers citing papers by Frank Jordan
Since
Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences
This network shows the impact of papers produced by Frank Jordan. 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 Frank Jordan. The network helps show where Frank Jordan may publish in the future.
Co-authorship network of co-authors of Frank Jordan
This figure shows the co-authorship network connecting the top 25 collaborators of Frank Jordan. A scholar is included among the top collaborators of Frank Jordan 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 Frank Jordan. Frank Jordan is excluded from the visualization to improve readability, since they are connected to all nodes in the network.
All Works
1.
Ozohanics, Olivér, Xu Zhang, Natalia S. Nemeria, Attila Ambrus, & Frank Jordan. (2023). Probing the E1o-E2o and E1a-E2o Interactions in Binary Subcomplexes of the Human 2-Oxoglutarate Dehydrogenase and 2-Oxoadipate Dehydrogenase Complexes by Chemical Cross-Linking Mass Spectrometry and Molecular Dynamics Simulation. International Journal of Molecular Sciences. 24(5). 4555–4555.
2.
Nemeria, Natalia S., Bálint Nagy, Roberto Sánchez, et al.. (2022). Functional Versatility of the Human 2-Oxoadipate Dehydrogenase in the L-Lysine Degradation Pathway toward Its Non-Cognate Substrate 2-Oxopimelic Acid. International Journal of Molecular Sciences. 23(15). 8213–8213.
3.
Nemeria, Natalia S., Yujeong Shim, Xu Zhang, et al.. (2022). Engineering the 2-Oxoglutarate Dehydrogenase Complex to Understand Catalysis and Alter Substrate Recognition. SHILAP Revista de lepidopterología. 3(1). 139–159.
4.
Nemeria, Natalia S., João Leandro, Jieyu Zhou, et al.. (2021). Toward an Understanding of the Structural and Mechanistic Aspects of Protein-Protein Interactions in 2-Oxoacid Dehydrogenase Complexes. Life. 11(5). 407–407.
5.
Nagy, Bálint, Martin Polák, Olivér Ozohanics, et al.. (2021). Structure of the dihydrolipoamide succinyltransferase (E2) component of the human alpha-ketoglutarate dehydrogenase complex (hKGDHc) revealed by cryo-EM and cross-linking mass spectrometry: Implications for the overall hKGDHc structure. Biochimica et Biophysica Acta (BBA) - General Subjects. 1865(6). 129889–129889.
6.
Leandro, João, Tetyana Dodatko, Jan Aten, et al.. (2020). DHTKD1 and OGDH display substrate overlap in cultured cells and form a hybrid 2-oxo acid dehydrogenase complex in vivo. Human Molecular Genetics. 29(7). 1168–1179.
7.
Zhang, Xu, Natalia S. Nemeria, João Leandro, et al.. (2020). Structure–function analyses of the G729R 2-oxoadipate dehydrogenase genetic variant associated with a disorder of l-lysine metabolism. Journal of Biological Chemistry. 295(23). 8078–8095.
8.
Zhang, Xu, et al.. (2019). Active Site Histidines Link Conformational Dynamics with Catalysis on Anti-Infective Target 1-Deoxy-d -xylulose 5-Phosphate Synthase. Biochemistry. 58(49). 4970–4982.
9.
Zhou, Jieyu, Luying Yang, Olivér Ozohanics, et al.. (2018). A multipronged approach unravels unprecedented protein–protein interactions in the human 2-oxoglutarate dehydrogenase multienzyme complex. Journal of Biological Chemistry. 293(50). 19213–19227.
10.
Nareddy, Pradeep, Frank Jordan, & Michal Szostak. (2017). Recent Developments in Ruthenium-Catalyzed C–H Arylation: Array of Mechanistic Manifolds. ACS Catalysis. 7(9). 5721–5745.
11.
Nareddy, Pradeep, Frank Jordan, & Michal Szostak. (2017). Ruthenium(II)-Catalyzed Direct C–H Arylation of Indoles with Arylsilanes in Water. Organic Letters. 20(2). 341–344.
12.
Zhou, Jieyu, et al.. (2017). Conformational dynamics of 1-deoxy- d -xylulose 5-phosphate synthase on ligand binding revealed by H/D exchange MS. Proceedings of the National Academy of Sciences. 114(35). 9355–9360.
13.
Hu, Feng, Pradeep Nareddy, Roger A. Lalancette, Frank Jordan, & Michal Szostak. (2017). σ N–C Bond Difunctionalization in Bridged Twisted Amides: Sew-and-Cut Activation Approach to Functionalized Isoquinolines. Organic Letters. 19(9). 2386–2389.
14.
Nemeria, Natalia S., Gary J. Gerfen, Pradeep Nareddy, et al.. (2017). The mitochondrial 2-oxoadipate and 2-oxoglutarate dehydrogenase complexes share their E2 and E3 components for their function and both generate reactive oxygen species. Free Radical Biology and Medicine. 115. 136–145.
15.
Ambrus, Attila, Natalia S. Nemeria, Beáta Törőcsik, et al.. (2015). Formation of reactive oxygen species by human and bacterial pyruvate and 2-oxoglutarate dehydrogenase multienzyme complexes reconstituted from recombinant components. Free Radical Biology and Medicine. 89. 642–650.
16.
Jordan, Frank & Natalia S. Nemeria. (2014). Progress in the experimental observation of thiamin diphosphate-bound intermediates on enzymes and mechanistic information derived from these observations. Bioorganic Chemistry. 57. 251–262.
17.
Jordan, Frank. (2005). Generating Time Code Information from Analog Sources. Journal of the Audio Engineering Society.
18.
Wei, Wen, Hong Li, Natalia S. Nemeria, & Frank Jordan. (2003). Expression and purification of the dihydrolipoamide acetyltransferase and dihydrolipoamide dehydrogenase subunits of the Escherichia coli pyruvate dehydrogenase multienzyme complex: a mass spectrometric assay for reductive acetylation of dihydrolipoamide acetyltransferase. Protein Expression and Purification. 28(1). 140–150.
19.
Mattsson, Lars, et al.. (1995). A Library of Monoclonal Antibodies to Escherichia coli K-12 Pyruvate Dehydrogenase Complex. Journal of Biological Chemistry. 270(34). 19744–19751.
20.
Jordan, Frank. (1976). C2H6N+異性体イオンの電子構造・分子構造ならびに安定についての非経験的な分子軌道法による計算. The Journal of Physical Chemistry. 80(1). 76–82.
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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