J.S. Kavanaugh

3.0k total citations
39 papers, 2.2k citations indexed

About

J.S. Kavanaugh is a scholar working on Molecular Biology, Infectious Diseases and Cell Biology. According to data from OpenAlex, J.S. Kavanaugh has authored 39 papers receiving a total of 2.2k indexed citations (citations by other indexed papers that have themselves been cited), including 26 papers in Molecular Biology, 19 papers in Infectious Diseases and 12 papers in Cell Biology. Recurrent topics in J.S. Kavanaugh's work include Antimicrobial Resistance in Staphylococcus (19 papers), Bacterial biofilms and quorum sensing (15 papers) and Hemoglobin structure and function (12 papers). J.S. Kavanaugh is often cited by papers focused on Antimicrobial Resistance in Staphylococcus (19 papers), Bacterial biofilms and quorum sensing (15 papers) and Hemoglobin structure and function (12 papers). J.S. Kavanaugh collaborates with scholars based in United States, Italy and Russia. J.S. Kavanaugh's co-authors include Alexander R. Horswill, Matthew Thoendel, A. Arnone, Caralyn E. Flack, P.H. Rogers, Cheryl L. Malone, Nadja B. Cech, Kenneth W. Bayles, Jovanka M. Voyich and Megan R. Kiedrowski and has published in prestigious journals such as Chemical Reviews, Journal of Biological Chemistry and The Journal of Immunology.

In The Last Decade

J.S. Kavanaugh

38 papers receiving 2.2k citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
J.S. Kavanaugh United States 26 1.5k 863 363 324 210 39 2.2k
Antonio Nakouzi United States 22 839 0.6× 680 0.8× 191 0.5× 281 0.9× 102 0.5× 43 2.0k
Kai Sohn Germany 26 1.2k 0.8× 578 0.7× 480 1.3× 56 0.2× 99 0.5× 64 2.3k
Manoj Raje India 31 1.3k 0.8× 407 0.5× 310 0.9× 113 0.3× 139 0.7× 79 2.5k
Elaine G. Rodrigues Brazil 29 705 0.5× 501 0.6× 114 0.3× 204 0.6× 126 0.6× 75 2.3k
Ana Traven Australia 31 2.0k 1.3× 990 1.1× 210 0.6× 362 1.1× 121 0.6× 74 3.3k
Fikri Y. Avci United States 24 1.3k 0.9× 278 0.3× 288 0.8× 302 0.9× 124 0.6× 52 2.4k
Daniel Gozalbo Spain 29 1.2k 0.8× 1.3k 1.5× 144 0.4× 217 0.7× 97 0.5× 99 3.1k
Stephen P. Saville United States 24 1.3k 0.8× 2.3k 2.6× 331 0.9× 232 0.7× 60 0.3× 36 3.3k
Dorothea Sesardic United Kingdom 32 963 0.6× 372 0.4× 54 0.1× 341 1.1× 111 0.5× 128 3.6k
Elsa Anes Portugal 26 1.1k 0.7× 836 1.0× 120 0.3× 186 0.6× 115 0.5× 61 2.4k

Countries citing papers authored by J.S. Kavanaugh

Since Specialization
Citations

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

Fields of papers citing papers by J.S. Kavanaugh

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

This network shows the impact of papers produced by J.S. Kavanaugh. 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 J.S. Kavanaugh. The network helps show where J.S. Kavanaugh may publish in the future.

Co-authorship network of co-authors of J.S. Kavanaugh

This figure shows the co-authorship network connecting the top 25 collaborators of J.S. Kavanaugh. A scholar is included among the top collaborators of J.S. Kavanaugh 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 J.S. Kavanaugh. J.S. Kavanaugh 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.
Hook, Jessica S., et al.. (2024). Role for IRAK-4 and p38 in Neutrophil Signaling in Response to Bacterial Lipoproteins from Staphylococcus aureus. Inflammation. 48(4). 1704–1715. 2 indexed citations
2.
Langouët-Astrié, Christophe, et al.. (2022). Group B Streptococcus adaptation promotes survival in a hyperinflammatory diabetic wound environment. Science Advances. 8(45). eadd3221–eadd3221. 27 indexed citations
3.
Langouët-Astrié, Christophe, K. Oshima, Sarah A. McMurtry, et al.. (2022). The influenza-injured lung microenvironment promotes MRSA virulence, contributing to severe secondary bacterial pneumonia. Cell Reports. 41(9). 111721–111721. 25 indexed citations
4.
Cau, Laura, Michael R. Williams, Anna M. Butcher, et al.. (2020). Staphylococcus epidermidis protease EcpA can be a deleterious component of the skin microbiome in atopic dermatitis. Journal of Allergy and Clinical Immunology. 147(3). 955–966.e16. 120 indexed citations
5.
Parlet, Corey P., J.S. Kavanaugh, Heidi A. Crosby, et al.. (2019). Apicidin Attenuates MRSA Virulence through Quorum-Sensing Inhibition and Enhanced Host Defense. Cell Reports. 27(1). 187–198.e6. 54 indexed citations
6.
Kavanaugh, J.S., Caralyn E. Flack, Jessica Lister, et al.. (2019). Identification of Extracellular DNA-Binding Proteins in the Biofilm Matrix. mBio. 10(3). 113 indexed citations
7.
Kavanaugh, J.S. & Alexander R. Horswill. (2016). Impact of Environmental Cues on Staphylococcal Quorum Sensing and Biofilm Development. Journal of Biological Chemistry. 291(24). 12556–12564. 76 indexed citations
8.
Todd, Daniel A., et al.. (2016). Hybrid Quadrupole-Orbitrap mass spectrometry for quantitative measurement of quorum sensing inhibition. Journal of Microbiological Methods. 127. 89–94. 17 indexed citations
9.
Daly, Seth M., Bradley O. Elmore, J.S. Kavanaugh, et al.. (2015). ω-Hydroxyemodin Limits Staphylococcus aureus Quorum Sensing-Mediated Pathogenesis and Inflammation. Antimicrobial Agents and Chemotherapy. 59(4). 2223–2235. 106 indexed citations
10.
Figueroa, Mario, Alan K. Jarmusch, Huzefa A. Raja, et al.. (2014). Polyhydroxyanthraquinones as Quorum Sensing Inhibitors from the Guttates ofPenicillium restrictumand Their Analysis by Desorption Electrospray Ionization Mass Spectrometry. Journal of Natural Products. 77(6). 1351–1358. 107 indexed citations
11.
Olson, Michael E., Tyler K. Nygaard, Laynez W. Ackermann, et al.. (2013). Staphylococcus aureus Nuclease Is an SaeRS-Dependent Virulence Factor. Infection and Immunity. 81(4). 1316–1324. 101 indexed citations
12.
Junio, Hiyas A., Daniel A. Todd, Keivan A. Ettefagh, et al.. (2013). Quantitative analysis of autoinducing peptide I (AIP-I) from Staphylococcus aureus cultures using ultrahigh performance liquid chromatography–high resolving power mass spectrometry. Journal of Chromatography B. 930. 7–12. 29 indexed citations
13.
Kiedrowski, Megan R., J.S. Kavanaugh, Cheryl L. Malone, et al.. (2011). Nuclease Modulates Biofilm Formation in Community-Associated Methicillin-Resistant Staphylococcus aureus. PLoS ONE. 6(11). e26714–e26714. 206 indexed citations
14.
Kavanaugh, J.S., Lokesh Gakhar, & Alexander R. Horswill. (2011). The structure of LsrB from Yersinia pestis complexed with autoinducer-2. Acta Crystallographica Section F Structural Biology and Crystallization Communications. 67(12). 1501–1505. 17 indexed citations
15.
Kavanaugh, J.S., P.H. Rogers, & A. Arnone. (2005). Crystallographic Evidence for a New Ensemble of Ligand-Induced Allosteric Transitions in Hemoglobin:  The T-to-THigh Quaternary Transitions,. Biochemistry. 44(16). 6101–6121. 60 indexed citations
16.
Kavanaugh, J.S., P.H. Rogers, A. Arnone, et al.. (2005). Intersubunit Interactions Associated with Tyr42α Stabilize the Quaternary-T Tetramer but Are Not Major Quaternary Constraints in Deoxyhemoglobin,. Biochemistry. 44(10). 3806–3820. 13 indexed citations
17.
Kavanaugh, J.S., Jamie A. Weydert, P.H. Rogers, et al.. (2001). Site‐directed mutations of human hemoglobin at residue 35β: A residue at the intersection of the α1β1, α1β2, and α1α2 interfaces. Protein Science. 10(9). 1847–1855. 13 indexed citations
18.
Bettati, Stefano, Laura D. Kwiatkowski, J.S. Kavanaugh, et al.. (1997). Structure and Oxygen Affinity of Crystalline des-His-146β Human Hemoglobin in the T State. Journal of Biological Chemistry. 272(52). 33077–33084. 19 indexed citations
19.
Kavanaugh, J.S., Winston F. Moo-Penn, & A. Arnone. (1993). Accommodation of insertions in helixes: The mutation in hemoglobin catonsville (Pro 37.alpha.-Glu-Thr 38.alpha.) generates a 310 .fwdarw. .alpha. bulge. Biochemistry. 32(10). 2509–2513. 41 indexed citations
20.
Kavanaugh, J.S., P.H. Rogers, & A. Arnone. (1992). High-resolution x-ray study of deoxy recombinant human hemoglobins synthesized from .beta.-globins having mutated amino termini. Biochemistry. 31(36). 8640–8647. 32 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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