Kathleen Beckingham

1.9k total citations
34 papers, 1.6k citations indexed

About

Kathleen Beckingham is a scholar working on Molecular Biology, Cellular and Molecular Neuroscience and Materials Chemistry. According to data from OpenAlex, Kathleen Beckingham has authored 34 papers receiving a total of 1.6k indexed citations (citations by other indexed papers that have themselves been cited), including 23 papers in Molecular Biology, 12 papers in Cellular and Molecular Neuroscience and 8 papers in Materials Chemistry. Recurrent topics in Kathleen Beckingham's work include Neurobiology and Insect Physiology Research (12 papers), Protein Structure and Dynamics (5 papers) and Genetics, Aging, and Longevity in Model Organisms (5 papers). Kathleen Beckingham is often cited by papers focused on Neurobiology and Insect Physiology Research (12 papers), Protein Structure and Dynamics (5 papers) and Genetics, Aging, and Longevity in Model Organisms (5 papers). Kathleen Beckingham collaborates with scholars based in United States, United Kingdom and Poland. Kathleen Beckingham's co-authors include John F. Maune, Rebecca A. Simonette, R. Bruce Weisman, Sergei M. Bachilo, Claude B. Klee, Saunab Ghosh, John S. Sack, Florante A. Quiocho, Denise Taylor and Michael J. Texada and has published in prestigious journals such as Science, Proceedings of the National Academy of Sciences and Journal of Biological Chemistry.

In The Last Decade

Kathleen Beckingham

34 papers receiving 1.5k 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 Beckingham United States 19 774 632 241 236 171 34 1.6k
Gerhard Vogt Germany 16 962 1.2× 419 0.7× 139 0.6× 266 1.1× 349 2.0× 25 1.9k
Iain Johnson United States 18 1.2k 1.5× 355 0.6× 315 1.3× 223 0.9× 70 0.4× 28 2.3k
Mickaël Lelimousin France 15 1.0k 1.3× 242 0.4× 216 0.9× 249 1.1× 45 0.3× 18 1.4k
Masanori Osawa Japan 27 1.6k 2.1× 324 0.5× 84 0.3× 410 1.7× 110 0.6× 70 2.3k
Vladimir Kiss Israel 19 1.1k 1.4× 240 0.4× 128 0.5× 202 0.9× 81 0.5× 26 1.6k
Jayanti Pande United States 27 1.8k 2.3× 754 1.2× 174 0.7× 245 1.0× 111 0.6× 56 2.6k
Ammasi Periasamy United States 11 901 1.2× 171 0.3× 198 0.8× 125 0.5× 105 0.6× 19 1.5k
Mark Lorch United Kingdom 21 801 1.0× 288 0.5× 69 0.3× 149 0.6× 69 0.4× 36 1.3k
Reiko Sakaguchi Japan 23 785 1.0× 220 0.3× 152 0.6× 155 0.7× 81 0.5× 48 1.3k
Fedor V. Subach Russia 26 1.8k 2.3× 239 0.4× 370 1.5× 648 2.7× 110 0.6× 64 2.8k

Countries citing papers authored by Kathleen Beckingham

Since Specialization
Citations

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

Fields of papers citing papers by Kathleen Beckingham

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Kathleen Beckingham

This figure shows the co-authorship network connecting the top 25 collaborators of Kathleen Beckingham. A scholar is included among the top collaborators of Kathleen Beckingham 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 Beckingham. Kathleen Beckingham 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.
Li, Jing, Henry W. Rohrs, Saketh Chemuru, et al.. (2024). Hydrogen/Deuterium Exchange Mass Spectrometry Provides Insights into the Role of Drosophila Testis-Specific Myosin VI Light Chain AndroCaM. Biochemistry. 63(5). 610–624. 2 indexed citations
2.
Beckingham, Kathleen, et al.. (2020). The roles of jim lovell and uninflatable in different endopolyploid larval tissues of Drosophila melanogaster. PLoS ONE. 15(8). e0237662–e0237662. 3 indexed citations
3.
Beckingham, Kathleen, et al.. (2018). A Burrowing/Tunneling Assay for Detection of Hypoxia in <em>Drosophila melanogaster</em> Larvae. Journal of Visualized Experiments. 1 indexed citations
4.
Lin, Ching‐Wei, Sergei M. Bachilo, Michael Vu, Kathleen Beckingham, & R. Bruce Weisman. (2016). Spectral triangulation: a 3D method for locating single-walled carbon nanotubes in vivo. Nanoscale. 8(19). 10348–10357. 19 indexed citations
5.
Beckingham, Kathleen, et al.. (2016). Failure to Burrow and Tunnel Reveals Roles for jim lovell in the Growth and Endoreplication of the Drosophila Larval Tracheae. PLoS ONE. 11(8). e0160233–e0160233. 7 indexed citations
6.
Taylor, Katherine, Michael D. George, Rachel Morgan, et al.. (2014). Toll Mediated Infection Response Is Altered by Gravity and Spaceflight in Drosophila. PLoS ONE. 9(1). e86485–e86485. 21 indexed citations
7.
Ghosh, Saunab, Sergei M. Bachilo, Rebecca A. Simonette, Kathleen Beckingham, & R. Bruce Weisman. (2010). Oxygen Doping Modifies Near-Infrared Band Gaps in Fluorescent Single-Walled Carbon Nanotubes. Science. 330(6011). 1656–1659. 323 indexed citations
8.
Texada, Michael J., Rebecca A. Simonette, William J. Deery, & Kathleen Beckingham. (2010). Tropomyosin is an interaction partner of the Drosophila coiled coil protein Yuri Gagarin. Experimental Cell Research. 317(4). 474–487. 7 indexed citations
9.
Baker, Dean A., Kathleen Beckingham, & J. Douglas Armstrong. (2007). Functional dissection of the neural substrates for gravitaxic maze behavior in Drosophila melanogaster. The Journal of Comparative Neurology. 501(5). 756–764. 23 indexed citations
10.
Leeuw, Tonya K., R. Michelle Reith, Rebecca A. Simonette, et al.. (2007). Single-Walled Carbon Nanotubes in the Intact Organism:  Near-IR Imaging and Biocompatibility Studies in Drosophila. Nano Letters. 7(9). 2650–2654. 176 indexed citations
11.
Frank, Deborah J., Stephen R. Martin, Rebecca A. Simonette, et al.. (2006). Androcam Is a Tissue-specific Light Chain for Myosin VI in the Drosophila Testis. Journal of Biological Chemistry. 281(34). 24728–24736. 14 indexed citations
12.
Konduri, Vanaja, et al.. (2006). A dicistronic gene pair within a cluster of “EF-hand” protein genes in the genomes of Drosophila species. Genomics. 88(3). 347–359. 4 indexed citations
13.
Armstrong, J. Douglas, Michael J. Texada, Ravi P. Munjaal, Dean A. Baker, & Kathleen Beckingham. (2005). Gravitaxis in Drosophila melanogaster: a forward genetic screen. Genes Brain & Behavior. 5(3). 222–239. 70 indexed citations
14.
Wang, Bo, Stephen R. Martin, Susan L. Hamilton, et al.. (2004). Biochemical properties of V91G calmodulin: A calmodulin point mutation that deregulates muscle contraction in Drosophila. Protein Science. 13(12). 3285–3297. 10 indexed citations
15.
Gajewski, Kathleen, et al.. (1999). Mutations in the predicted aspartyl tRNA synthetase of Drosophila are lethal and function as dosage-sensitive maternal modifiers of the sex determination gene Sex-lethal. Molecular and General Genetics MGG. 261(1). 142–151. 15 indexed citations
16.
Beckingham, Kathleen. (1995). 13 Calcium regulation of Drosophila development. PubMed. 30. 359–394. 3 indexed citations
17.
Gao, Zhipeng, Joachim Krebs, Mark F.A. VanBerkum, et al.. (1993). Activation of four enzymes by two series of calmodulin mutants with point mutations in individual Ca2+ binding sites.. Journal of Biological Chemistry. 268(27). 20096–20104. 65 indexed citations
18.
Beckingham, Kathleen. (1991). Use of site-directed mutations in the individual Ca2(+)-binding sites of calmodulin to examine Ca2(+)-induced conformational changes.. Journal of Biological Chemistry. 266(10). 6027–6030. 64 indexed citations
19.
Taylor, Denise, John S. Sack, John F. Maune, Kathleen Beckingham, & Florante A. Quiocho. (1991). Structure of a recombinant calmodulin from Drosophila melanogaster refined at 2.2-A resolution.. Journal of Biological Chemistry. 266(32). 21375–21380. 91 indexed citations
20.
Taylor, Denise, John S. Sack, John F. Maune, Kathleen Beckingham, & Florante A. Quiocho. (1991). STRUCTURE OF A RECOMBINANT CALMODULIN FROM DROSOPHILA MELANOGASTER REFINED AT 2.2-ANGSTROMS RESOLUTION. PubMed. 266(32). 21375–80. 108 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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