Kathleen M. Meneely

712 total citations
25 papers, 591 citations indexed

About

Kathleen M. Meneely is a scholar working on Molecular Biology, Materials Chemistry and Biochemistry. According to data from OpenAlex, Kathleen M. Meneely has authored 25 papers receiving a total of 591 indexed citations (citations by other indexed papers that have themselves been cited), including 20 papers in Molecular Biology, 13 papers in Materials Chemistry and 7 papers in Biochemistry. Recurrent topics in Kathleen M. Meneely's work include Enzyme Structure and Function (13 papers), Amino Acid Enzymes and Metabolism (7 papers) and Protein Structure and Dynamics (5 papers). Kathleen M. Meneely is often cited by papers focused on Enzyme Structure and Function (13 papers), Amino Acid Enzymes and Metabolism (7 papers) and Protein Structure and Dynamics (5 papers). Kathleen M. Meneely collaborates with scholars based in United States and New Zealand. Kathleen M. Meneely's co-authors include Audrey L. Lamb, Emily E. Scott, Patrick Porubsky, José Olucha, J. Martin Bollinger, Eric W. Barr, Natasha M. DeVore, Qianyi Luo, K.P. Battaile and Trey A. Ronnebaum and has published in prestigious journals such as Journal of the American Chemical Society, Journal of Biological Chemistry and Biochemistry.

In The Last Decade

Kathleen M. Meneely

25 papers receiving 589 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Kathleen M. Meneely United States 13 320 178 109 103 83 25 591
Hwei‐Jen Lee Taiwan 14 575 1.8× 50 0.3× 61 0.6× 153 1.5× 30 0.4× 41 840
Ronald L. Hanson United States 21 888 2.8× 174 1.0× 152 1.4× 124 1.2× 43 0.5× 52 1.2k
D.A. Lysek United Kingdom 11 1.1k 3.4× 472 2.7× 56 0.5× 137 1.3× 109 1.3× 14 1.4k
G.L. Kedderis United States 15 237 0.7× 203 1.1× 80 0.7× 50 0.5× 16 0.2× 20 730
Kerstin Maria Ewen Germany 11 595 1.9× 523 2.9× 29 0.3× 24 0.2× 88 1.1× 11 939
Steven J. Pernecky United States 11 228 0.7× 419 2.4× 56 0.5× 42 0.4× 77 0.9× 18 645
Zhoupeng Zhang United States 17 249 0.8× 283 1.6× 81 0.7× 18 0.2× 107 1.3× 26 634
Rachel J. Lawson United Kingdom 7 260 0.8× 182 1.0× 16 0.1× 43 0.4× 42 0.5× 7 430
I. I. Karuzina Russia 14 298 0.9× 189 1.1× 42 0.4× 26 0.3× 61 0.7× 51 542
Cathaline den Besten Netherlands 17 346 1.1× 114 0.6× 45 0.4× 14 0.1× 33 0.4× 22 695

Countries citing papers authored by Kathleen M. Meneely

Since Specialization
Citations

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

Fields of papers citing papers by Kathleen M. Meneely

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by Kathleen M. Meneely. 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 Kathleen M. Meneely. The network helps show where Kathleen M. Meneely may publish in the future.

Co-authorship network of co-authors of Kathleen M. Meneely

This figure shows the co-authorship network connecting the top 25 collaborators of Kathleen M. Meneely. A scholar is included among the top collaborators of Kathleen M. Meneely 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 Kathleen M. Meneely. Kathleen M. Meneely 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.
Meneely, Kathleen M., et al.. (2023). The 2.4 Å structure of Zymomonas mobilis pyruvate kinase: Implications for stability and regulation. Archives of Biochemistry and Biophysics. 744. 109679–109679. 4 indexed citations
2.
3.
Shelton, Catherine L., Kathleen M. Meneely, Trey A. Ronnebaum, et al.. (2022). Rational inhibitor design for Pseudomonas aeruginosa salicylate adenylation enzyme PchD. JBIC Journal of Biological Inorganic Chemistry. 27(6). 541–551. 10 indexed citations
4.
Meneely, Kathleen M., et al.. (2022). Evidence for the Chemical Mechanism of RibB (3,4-Dihydroxy-2-butanone 4-phosphate Synthase) of Riboflavin Biosynthesis. Journal of the American Chemical Society. 144(28). 12769–12780. 7 indexed citations
5.
Meneely, Kathleen M., et al.. (2021). Substitutions at a rheostat position in human aldolase A cause a shift in the conformational population. Protein Science. 31(2). 357–370. 12 indexed citations
6.
Smith, Madison M., et al.. (2021). Finding Ways to Relax: A Revisionistic Analysis of the Chemistry of E. coli GTP Cyclohydrolase II. Biochemistry. 60(40). 3027–3039. 1 indexed citations
7.
Meneely, Kathleen M., et al.. (2020). The 3-His Metal Coordination Site Promotes the Coupling of Oxygen Activation to Cysteine Oxidation in Cysteine Dioxygenase. Biochemistry. 59(21). 2022–2031. 11 indexed citations
8.
Bhattarai, Sanjay, et al.. (2020). Design of Substrate Transmembrane Mimetics as Structural Probes for γ-Secretase. Journal of the American Chemical Society. 142(7). 3351–3355. 9 indexed citations
9.
Bhattarai, Sanjay, et al.. (2019). Designed Helical Peptides as Functional Probes for γ-Secretase. Biochemistry. 58(44). 4398–4407. 5 indexed citations
10.
Ronnebaum, Trey A., et al.. (2019). Changes in the allosteric site of human liver pyruvate kinase upon activator binding include the breakage of an intersubunit cation–π bond. Acta Crystallographica Section F Structural Biology Communications. 75(6). 461–469. 15 indexed citations
11.
Meneely, Kathleen M., et al.. (2016). Ligand binding phenomena that pertain to the metabolic function of renalase. Archives of Biochemistry and Biophysics. 612. 46–56. 11 indexed citations
12.
Meneely, Kathleen M., Jesse A. Sundlov, Andrew M. Gulick, Graham R. Moran, & Audrey L. Lamb. (2016). An Open and Shut Case: The Interaction of Magnesium with MST Enzymes. Journal of the American Chemical Society. 138(29). 9277–9293. 17 indexed citations
13.
Meneely, Kathleen M., Qianyi Luo, Andrew P. Riley, et al.. (2014). Expanding the results of a high throughput screen against an isochorismate-pyruvate lyase to enzymes of a similar scaffold or mechanism. Bioorganic & Medicinal Chemistry. 22(21). 5961–5969. 7 indexed citations
14.
Meneely, Kathleen M., Qianyi Luo, & Audrey L. Lamb. (2013). Redesign of MST enzymes to target lyase activity instead promotes mutase and dehydratase activities. Archives of Biochemistry and Biophysics. 539(1). 70–80. 5 indexed citations
15.
Meneely, Kathleen M., Qianyi Luo, Prajnaparamita Dhar, & Audrey L. Lamb. (2013). Lysine221 is the general base residue of the isochorismate synthase from Pseudomonas aeruginosa (PchA) in a reaction that is diffusion limited. Archives of Biochemistry and Biophysics. 538(1). 49–56. 13 indexed citations
16.
DeVore, Natasha M., et al.. (2011). Structural comparison of cytochromes P450 2A6, 2A13, and 2E1 with pilocarpine. FEBS Journal. 279(9). 1621–1631. 58 indexed citations
17.
Olucha, José, et al.. (2011). Two Structures of an N-Hydroxylating Flavoprotein Monooxygenase. Journal of Biological Chemistry. 286(36). 31789–31798. 56 indexed citations
18.
Meneely, Kathleen M., Eric W. Barr, J. Martin Bollinger, & Audrey L. Lamb. (2009). Kinetic Mechanism of Ornithine Hydroxylase (PvdA) from Pseudomonas aeruginosa: Substrate Triggering of O2 Addition but Not Flavin Reduction. Biochemistry. 48(20). 4371–4376. 47 indexed citations
19.
Zaitseva, Jelena, Kathleen M. Meneely, & Audrey L. Lamb. (2009). Structure ofEscherichia colimalate dehydrogenase at 1.45 Å resolution. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 65(9). 866–869. 17 indexed citations
20.
Porubsky, Patrick, Kathleen M. Meneely, & Emily E. Scott. (2008). Structures of Human Cytochrome P-450 2E1. Journal of Biological Chemistry. 283(48). 33698–33707. 176 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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