Ronald Kluger

4.9k total citations
196 papers, 3.6k citations indexed

About

Ronald Kluger is a scholar working on Molecular Biology, Organic Chemistry and Cell Biology. According to data from OpenAlex, Ronald Kluger has authored 196 papers receiving a total of 3.6k indexed citations (citations by other indexed papers that have themselves been cited), including 74 papers in Molecular Biology, 70 papers in Organic Chemistry and 61 papers in Cell Biology. Recurrent topics in Ronald Kluger's work include Hemoglobin structure and function (51 papers), Biochemical Acid Research Studies (50 papers) and Alcoholism and Thiamine Deficiency (36 papers). Ronald Kluger is often cited by papers focused on Hemoglobin structure and function (51 papers), Biochemical Acid Research Studies (50 papers) and Alcoholism and Thiamine Deficiency (36 papers). Ronald Kluger collaborates with scholars based in Canada, United States and Germany. Ronald Kluger's co-authors include Kai Tittmann, J. Peter Guthrie, Scott D. Taylor, Scott O. C. Mundle, Richard T. Jones, Jik Chin, Wing-Cheong Tsui, Qingyan Hu, Timothy P. Smyth and Jolanta Wodzinska and has published in prestigious journals such as Nature, Chemical Reviews and Proceedings of the National Academy of Sciences.

In The Last Decade

Ronald Kluger

193 papers receiving 3.4k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Ronald Kluger Canada 31 1.4k 1.3k 899 805 530 196 3.6k
Bryce V. Plapp United States 38 2.5k 1.7× 322 0.2× 660 0.7× 788 1.0× 65 0.1× 109 4.0k
David E. Metzler United States 35 2.2k 1.5× 1.1k 0.9× 1.0k 1.1× 236 0.3× 79 0.1× 101 4.7k
Joseph J. Villafranca United States 37 2.6k 1.8× 571 0.4× 805 0.9× 370 0.5× 44 0.1× 154 4.5k
S. Bruce King United States 40 1.7k 1.2× 1.0k 0.8× 1.3k 1.4× 556 0.7× 33 0.1× 126 4.9k
Thomas Nauser Switzerland 33 1.3k 0.9× 853 0.7× 812 0.9× 391 0.5× 35 0.1× 94 4.2k
Tina L. Amyes United States 39 2.6k 1.8× 1.8k 1.4× 550 0.6× 372 0.5× 16 0.0× 118 4.8k
Igor V. Kurnikov United States 30 2.5k 1.7× 214 0.2× 119 0.1× 382 0.5× 61 0.1× 54 3.8k
Hidehiko Nakagawa Japan 40 2.4k 1.6× 1.2k 0.9× 680 0.8× 163 0.2× 52 0.1× 170 4.9k
James W. Whittaker United States 42 2.1k 1.5× 724 0.6× 238 0.3× 216 0.3× 34 0.1× 91 5.8k
Micaël Hardy France 30 2.1k 1.5× 576 0.4× 396 0.4× 82 0.1× 84 0.2× 69 4.3k

Countries citing papers authored by Ronald Kluger

Since Specialization
Citations

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

Fields of papers citing papers by Ronald Kluger

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Ronald Kluger. 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 Ronald Kluger. The network helps show where Ronald Kluger may publish in the future.

Co-authorship network of co-authors of Ronald Kluger

This figure shows the co-authorship network connecting the top 25 collaborators of Ronald Kluger. A scholar is included among the top collaborators of Ronald Kluger 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 Ronald Kluger. Ronald Kluger 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
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Kluger, Ronald, et al.. (2022). Efficient formation of hemoglobin bis-tetramers via selective acetylation of α-subunit amino groups by methyl acetyl phosphate. Organic & Biomolecular Chemistry. 20(41). 8083–8091. 2 indexed citations
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Mundle, Scott O. C., et al.. (2012). Protonated Carbonic Acid and Reactive Intermediates in the Acidic Decarboxylation of Indolecarboxylic Acids. The Journal of Organic Chemistry. 77(15). 6505–6509. 15 indexed citations
6.
Yu, Binglan, et al.. (2011). Hemodynamic responses to a hemoglobin bis‐tetramer and its polyethylene glycol conjugate. Transfusion. 52(5). 974–982. 11 indexed citations
7.
Kluger, Ronald, et al.. (2011). Biomimetic peptide bond formation in water with aminoacyl phosphate esters. Organic & Biomolecular Chemistry. 9(16). 5645–5645. 11 indexed citations
8.
Kluger, Ronald. (2010). Red cell substitutes from hemoglobin — Do we start all over again?. Current Opinion in Chemical Biology. 14(4). 538–543. 38 indexed citations
9.
Kluger, Ronald, et al.. (2010). Protein–protein coupling and its application to functional red cell substitutes. Chemical Communications. 46(8). 1194–1194. 10 indexed citations
10.
Chow, Edwin C.Y., et al.. (2008). Role of Haptoglobin on the Uptake of Native and β-Chain [Trimesoyl-(Lys82)β-(Lys82)β] Cross-Linked Human Hemoglobins in Isolated Perfused Rat Livers. Drug Metabolism and Disposition. 36(5). 937–945. 10 indexed citations
11.
Kluger, Ronald, et al.. (2007). Efficient generation of dendritic arrays of cross-linked hemoglobin: symmetry and redundancy. Organic & Biomolecular Chemistry. 6(1). 151–156. 14 indexed citations
12.
Machius, Mischa, Richard Wynn, Jacinta L. Chuang, et al.. (2006). A Versatile Conformational Switch Regulates Reactivity in Human Branched-Chain α-Ketoacid Dehydrogenase. Structure. 14(2). 287–298. 46 indexed citations
13.
Kluger, Ronald, et al.. (2006). Protein-enhanced decarboxylation of the covalent intermediate in benzoylformate decarboxylase—Desolvation or acid catalysis?. Bioorganic Chemistry. 34(6). 337–344. 6 indexed citations
14.
Westermann, Bernhard, et al.. (2006). Lanthanum-catalyzed aqueous acylation of monosaccharides by benzoyl methyl phosphate. Canadian Journal of Chemistry. 84(4). 620–624. 7 indexed citations
15.
Tseng, Eric, et al.. (2005). Binding of acellular, native and cross-linked human hemoglobins to haptoglobin: enhanced distribution and clearance in the rat. American Journal of Physiology-Gastrointestinal and Liver Physiology. 288(6). G1301–G1309. 13 indexed citations
16.
Golbik, Ralph, L. E. Meshalkina, Tatyana Sandalova, et al.. (2005). Effect of coenzyme modification on the structural and catalytic properties of wild‐type transketolase and of the variant E418A from Saccharomyces cerevisiae. FEBS Journal. 272(6). 1326–1342. 13 indexed citations
17.
Kluger, Ronald, et al.. (2004). Chemical cross-linking and protein–protein interactions—a review with illustrative protocols. Bioorganic Chemistry. 32(6). 451–472. 89 indexed citations
18.
Schumacher, Maria A., M.M. Dixon, Ronald Kluger, Richard T. Jones, & Richard G. Brennan. (1995). Allosteric transition intermediates modelled by crosslinked haemoglobins. Nature. 375(6526). 84–87. 76 indexed citations
19.
Kluger, Ronald & Stephen L. Bearne. (1994). Inactivation of d-3-hydroxybutyrate dehydrogenase by fumaroyl bis(methyl phosphate). Bioorganic & Medicinal Chemistry. 2(6). 379–385. 3 indexed citations
20.

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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