K.L. Kavanagh

6.0k total citations · 1 hit paper
56 papers, 4.7k citations indexed

About

K.L. Kavanagh is a scholar working on Molecular Biology, Endocrinology, Diabetes and Metabolism and Cell Biology. According to data from OpenAlex, K.L. Kavanagh has authored 56 papers receiving a total of 4.7k indexed citations (citations by other indexed papers that have themselves been cited), including 37 papers in Molecular Biology, 13 papers in Endocrinology, Diabetes and Metabolism and 13 papers in Cell Biology. Recurrent topics in K.L. Kavanagh's work include Enzyme Structure and Function (13 papers), Aldose Reductase and Taurine (10 papers) and Diet, Metabolism, and Disease (10 papers). K.L. Kavanagh is often cited by papers focused on Enzyme Structure and Function (13 papers), Aldose Reductase and Taurine (10 papers) and Diet, Metabolism, and Disease (10 papers). K.L. Kavanagh collaborates with scholars based in United Kingdom, United States and Austria. K.L. Kavanagh's co-authors include Udo Oppermann, Bengt Persson, Hans Jörnvall, Bernd Nidetzky, R.G.G. Russell, James E. Dunford, David K. Wilson, Frank H. Ebetino, Michael J. Rogers and Petra Lukacik and has published in prestigious journals such as Nature, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

K.L. Kavanagh

54 papers receiving 4.6k citations

Hit Papers

align trajectories sort by overperformance

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.

Medium- and short-chain dehydrogenase/reductase gene and protein families

2008 699 citations K.L. Kavanagh, Hans Jörnvall et al. Cellular and Molecular Life Sciences profile →

Author Peers

Peers are selected by citation overlap in the author's most active subfields. citations · hero ref

Author						Papers	Cites
K.L. Kavanagh	2.8k	889	492	437	398	56	4.7k
Xiaoqiu Wu	2.3k 0.8×	524 0.6×	282 0.6×	209 0.5×	166 0.4×	67	3.2k
Thomas D. Pfister	1.5k 0.5×	766 0.9×	191 0.4×	102 0.2×	197 0.5×	94	3.7k
Kieran F. Geoghegan	3.3k 1.2×	739 0.8×	262 0.5×	116 0.3×	406 1.0×	89	5.7k
Paul B. Lazarow	8.5k 3.1×	556 0.6×	97 0.2×	174 0.4×	918 2.3×	92	9.9k
Jörg Stürzebecher	1.7k 0.6×	742 0.8×	170 0.3×	87 0.2×	150 0.4×	130	4.2k
John de Jersey	2.5k 0.9×	699 0.8×	267 0.5×	208 0.5×	148 0.4×	149	4.7k
Dianne L. Newton	3.1k 1.1×	681 0.8×	202 0.4×	62 0.1×	230 0.6×	87	4.6k
Grant Buchanan	3.2k 1.1×	754 0.8×	192 0.4×	775 1.8×	159 0.4×	117	5.6k
M. Micksche	2.7k 1.0×	1.9k 2.2×	144 0.3×	217 0.5×	296 0.7×	187	6.0k
Indu Parikh	2.4k 0.9×	306 0.3×	154 0.3×	253 0.6×	404 1.0×	57	4.1k

Countries citing papers authored by K.L. Kavanagh

Since Specialization

Citations

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

Fields of papers citing papers by K.L. Kavanagh

Since Specialization

Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of K.L. Kavanagh

This figure shows the co-authorship network connecting the top 25 collaborators of K.L. Kavanagh. A scholar is included among the top collaborators of K.L. Kavanagh 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 K.L. Kavanagh. K.L. Kavanagh 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

Chaikuad, A., Ewa S. Pilka, F. von Delft, et al.. (2012). Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family. BMC Structural Biology. 12(1). 14–14. 29 indexed citations

Egger, Sigrid, A. Chaikuad, K.L. Kavanagh, Udo Oppermann, & Bernd Nidetzky. (2011). Structure and Mechanism of Human UDP-glucose 6-Dehydrogenase. Journal of Biological Chemistry. 286(27). 23877–23887. 58 indexed citations

Kavanagh, K.L., et al.. (2011). Structure of Candida albicans methionine synthase determined by employing surface residue mutagenesis. Archives of Biochemistry and Biophysics. 513(1). 19–26. 11 indexed citations

Zhang, Zhihong, Grazyna Kochan, Stanley S. Ng, et al.. (2011). Crystal structure of PHYHD1A, a 2OG oxygenase related to phytanoyl-CoA hydroxylase. Biochemical and Biophysical Research Communications. 408(4). 553–558. 20 indexed citations

Egger, Sigrid, A. Chaikuad, Mario Klimacek, et al.. (2011). Structural and Kinetic Evidence That Catalytic Reaction of Human UDP-glucose 6-Dehydrogenase Involves Covalent Thiohemiacetal and Thioester Enzyme Intermediates. Journal of Biological Chemistry. 287(3). 2119–2129. 25 indexed citations

Mantri, Monica, T. Krojer, Eleanor A. L. Bagg, et al.. (2010). Crystal Structure of the 2-Oxoglutarate- and Fe(II)-Dependent Lysyl Hydroxylase JMJD6. Journal of Molecular Biology. 401(2). 211–222. 74 indexed citations

Bunkóczi, G., Xiaoqiu Wu, Wen‐Hwa Lee, et al.. (2009). Structural Basis for Different Specificities of Acyltransferases Associated with the Human Cytosolic and Mitochondrial Fatty Acid Synthases. Chemistry & Biology. 16(6). 667–675. 26 indexed citations

Artz, J.D., James E. Dunford, Michael J. Arrowood, et al.. (2008). Targeting a Uniquely Nonspecific Prenyl Synthase with Bisphosphonates to Combat Cryptosporidiosis. Chemistry & Biology. 15(12). 1296–1306. 33 indexed citations

Kavanagh, K.L., Hans Jörnvall, Bengt Persson, & Udo Oppermann. (2008). Medium- and short-chain dehydrogenase/reductase gene and protein families. Cellular and Molecular Life Sciences. 65(24). 3895–906. 699 indexed citations breakdown →

10.

Persson, Bengt, Yvonne Kallberg, James E. Bray, et al.. (2008). The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative. Chemico-Biological Interactions. 178(1-3). 94–98. 323 indexed citations

11.

Dunford, James E., et al.. (2007). Kinetic analysis of conformational changes in farnesyl pyrophosphate synthase induced by nitrogen containing bisphosphonates. Calcified Tissue International. 40. 3 indexed citations

12.

Gileadi, O., Stefan Knapp, Wen‐Hwa Lee, et al.. (2007). The scientific impact of the Structural Genomics Consortium: a protein family and ligand-centered approach to medically-relevant human proteins. Journal of Structural and Functional Genomics. 8(2-3). 107–119. 45 indexed citations

13.

Ng, Stanley S., K.L. Kavanagh, M.A. McDonough, et al.. (2007). Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity. Nature. 448(7149). 87–91. 263 indexed citations

14.

Ebetino, Frank H., B.L. Barnett, B. A. Kashemirov, et al.. (2006). Nitrogen-containing bisphosphonates of varying antiresorptive potency have been co-crystallized in farnesyl diphosphate synthase and modelled to understand the key structural features involved in enzyme inhibition.. Journal of Bone and Mineral Research. 21. 1 indexed citations

15.

Johansson, C., K.L. Kavanagh, O. Gileadi, & Udo Oppermann. (2006). Reversible Sequestration of Active Site Cysteines in a 2Fe-2S-bridged Dimer Provides a Mechanism for Glutaredoxin 2 Regulation in Human Mitochondria. Journal of Biological Chemistry. 282(5). 3077–3082. 117 indexed citations

16.

McDonough, M.A., et al.. (2005). Structure of Human Phytanoyl-CoA 2-Hydroxylase Identifies Molecular Mechanisms of Refsum Disease*. Journal of Biological Chemistry. 280(49). 41101–41110. 67 indexed citations

17.

Klimacek, Mario, et al.. (2003). Altering dimer contacts in xylose reductase from Candida tenuis by site-directed mutagenesis: structural and functional properties of R180A mutant. Chemico-Biological Interactions. 143-144. 523–532. 6 indexed citations

18.

Kavanagh, K.L., Mario Klimacek, Bernd Nidetzky, & David K. Wilson. (2003). Crystal structure of Pseudomonas fluorescens mannitol 2-dehydrogenase: evidence for a very divergent long-chain dehydrogenase family. Chemico-Biological Interactions. 143-144. 551–558. 12 indexed citations

19.

Klimacek, Mario, K.L. Kavanagh, David K. Wilson, & Bernd Nidetzky. (2003). Pseudomonas fluorescens mannitol 2-dehydrogenase and the family of polyol-specific long-chain dehydrogenases/reductases: sequence-based classification and analysis of structure–function relationships. Chemico-Biological Interactions. 143-144. 559–582. 21 indexed citations

20.

Kavanagh, K.L., Mario Klimacek, Bernd Nidetzky, & David K. Wilson. (2002). Crystal Structure of Pseudomonas fluorescens Mannitol 2-Dehydrogenase Binary and Ternary Complexes. Journal of Biological Chemistry. 277(45). 43433–43442. 41 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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