Robert L. McKown

1.2k total citations
45 papers, 987 citations indexed

About

Robert L. McKown is a scholar working on Molecular Biology, Public Health, Environmental and Occupational Health and Cell Biology. According to data from OpenAlex, Robert L. McKown has authored 45 papers receiving a total of 987 indexed citations (citations by other indexed papers that have themselves been cited), including 18 papers in Molecular Biology, 18 papers in Public Health, Environmental and Occupational Health and 8 papers in Cell Biology. Recurrent topics in Robert L. McKown's work include Ocular Surface and Contact Lens (18 papers), Salivary Gland Disorders and Functions (7 papers) and Proteoglycans and glycosaminoglycans research (6 papers). Robert L. McKown is often cited by papers focused on Ocular Surface and Contact Lens (18 papers), Salivary Gland Disorders and Functions (7 papers) and Proteoglycans and glycosaminoglycans research (6 papers). Robert L. McKown collaborates with scholars based in United States, Ukraine and United Kingdom. Robert L. McKown's co-authors include Gordon W. Laurie, Gareth Warren, Ronald W. Raab, Nancy L. Craig, Κ. Κ. Tewari, Lidia K. Arciszewska, Ningning Wang, Patricia B. Williams, Peisong Ma and Yinghui Zhang and has published in prestigious journals such as Proceedings of the National Academy of Sciences, Journal of Biological Chemistry and Nature Communications.

In The Last Decade

Robert L. McKown

44 papers receiving 959 citations

Peers — A (Enhanced Table)

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

Name h Career Trend Papers Cites
Robert L. McKown United States 19 405 386 165 156 154 45 987
Kristian W. Sanggaard Denmark 20 74 0.2× 320 0.8× 103 0.6× 34 0.2× 64 0.4× 33 830
Romina D’Aurizio Italy 18 101 0.2× 822 2.1× 345 2.1× 14 0.1× 27 0.2× 44 1.3k
S. Kinoshita Japan 14 428 1.1× 157 0.4× 83 0.5× 70 0.4× 506 3.3× 30 863
Lifang Liang United States 17 476 1.2× 777 2.0× 398 2.4× 10 0.1× 22 0.1× 27 1.4k
Cédric Pionneau France 20 127 0.3× 455 1.2× 90 0.5× 8 0.1× 55 0.4× 39 913
Antonia P. Sagona United Kingdom 20 84 0.2× 717 1.9× 83 0.5× 5 0.0× 94 0.6× 36 1.4k
J. Marshall United Kingdom 20 28 0.1× 870 2.3× 107 0.6× 111 0.7× 87 0.6× 40 1.6k
Julie A. Robinson United States 12 72 0.2× 474 1.2× 132 0.8× 15 0.1× 48 0.3× 18 1.0k
Zuyong He China 21 153 0.4× 810 2.1× 417 2.5× 10 0.1× 10 0.1× 77 1.4k
Judith Kelvin Miller United States 14 84 0.2× 350 0.9× 112 0.7× 71 0.5× 57 0.4× 21 742

Countries citing papers authored by Robert L. McKown

Since Specialization
Citations

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

Fields of papers citing papers by Robert L. McKown

Since Specialization
Physical SciencesHealth SciencesLife SciencesSocial Sciences

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

Co-authorship network of co-authors of Robert L. McKown

This figure shows the co-authorship network connecting the top 25 collaborators of Robert L. McKown. A scholar is included among the top collaborators of Robert L. McKown 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 Robert L. McKown. Robert L. McKown 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.
Maehr, Tanja, Javier López, Frederico Moraes Ferreira, et al.. (2025). A safe, T cell-inducing heterologous vaccine against elephant endotheliotropic herpesvirus in a proof-of-concept study. Nature Communications. 16(1). 8374–8374.
2.
Georgiev, Georgi, Mohammad Sharifian Gh., Craig B Struble, et al.. (2020). Lacritin proteoforms prevent tear film collapse and maintain epithelial homeostasis. Journal of Biological Chemistry. 296. 100070–100070. 16 indexed citations
3.
Hirata, Harumitsu, et al.. (2016). Lacritin acutely enhances corneal nerve sensitivity to ocular surface dryness as a key stimulus for basal tear production: Implications for dry eye disease.. Investigative Ophthalmology & Visual Science. 57(12). 424–424. 1 indexed citations
4.
Hong, Liu, et al.. (2014). Cytoprotective Effect of Lacritin on Human Corneal Epithelial Cells Exposed to Benzalkonium ChlorideIn Vitro. Current Eye Research. 39(6). 604–610. 12 indexed citations
5.
Zhang, Yinghui, Ningning Wang, Ronald W. Raab, et al.. (2013). Targeting of Heparanase-modified Syndecan-1 by Prosecretory Mitogen Lacritin Requires Conserved Core GAGAL plus Heparan and Chondroitin Sulfate as a Novel Hybrid Binding Site That Enhances Selectivity. Journal of Biological Chemistry. 288(17). 12090–12101. 30 indexed citations
6.
McKown, Robert L., Liwen Zhang, Ronald W. Raab, et al.. (2013). Tissue Transglutaminase Is a Negative Regulator of Monomeric Lacritin Bioactivity. Investigative Ophthalmology & Visual Science. 54(3). 2123–2123. 18 indexed citations
7.
Laurie, Gordon W., et al.. (2012). Immunodetection of a Lacritin-like Protein in Non-Primate Tears Primarily as a C-Terminal Fragment. Investigative Ophthalmology & Visual Science. 53(14). 4234–4234. 3 indexed citations
8.
Hosseini, Alireza, Frank A. Lattanzio, S. S. Samudre, et al.. (2012). Lacritin, a Novel Tear Glycoprotein, is an Effective Topical Antimicrobial Agent in an Animal Model. Investigative Ophthalmology & Visual Science. 53(14). 6266–6266. 2 indexed citations
9.
Soyars, Cara L., Kraig S. Bower, Rose K. Sia, et al.. (2012). Development of Quantitative Sandwich ELISAs for Lacritin and the Lacritin-c Splice Variant in Human Tears. Investigative Ophthalmology & Visual Science. 53(14). 4233–4233. 2 indexed citations
10.
Wang, Ningning, Ronald W. Raab, Robert L. McKown, & Gordon W. Laurie. (2011). Lacritin Rapidly Suppresses Inflammatory Stress In Human Corneal Epithelial Cells. Investigative Ophthalmology & Visual Science. 52(14). 3712–3712. 1 indexed citations
11.
Powell, Bradford S., et al.. (2010). Purification and characterization of a recombinant Yersinia pestis V-F1 “Reversed” fusion protein for use as a new subunit vaccine against plague. Protein Expression and Purification. 76(1). 136–144. 10 indexed citations
12.
Zhang, Yinghui, Robert L. McKown, Ronald W. Raab, Alan C. Rapraeger, & Gordon W. Laurie. (2010). Focus on Molecules: Syndecan-1. Experimental Eye Research. 93(4). 329–330. 5 indexed citations
13.
McKown, Robert L., et al.. (2008). Antimicrobial Activity in Recombinant Variants of Prosecretory Mitogen Lacritin. Investigative Ophthalmology & Visual Science. 49(13). 5287–5287. 2 indexed citations
14.
McKown, Robert L., Ningning Wang, Ronald W. Raab, et al.. (2008). Lacritin and other new proteins of the lacrimal functional unit. Experimental Eye Research. 88(5). 848–858. 63 indexed citations
15.
Laurie, Gordon W., et al.. (2007). Initial Identification of a Second Mitogenic Site in Lacritin for Human Corneal Epithelial Cell Renewal. Investigative Ophthalmology & Visual Science. 48(13). 2726–2726. 1 indexed citations
16.
Laurie, Gordon W., et al.. (2006). NFAT/mTOR Signaling and Downstream Promotion of MUC16 Expression by Lacrimal Prosecretory Mitogen Lacritin. Investigative Ophthalmology & Visual Science. 47(13). 1606–1606. 3 indexed citations
17.
McKown, Robert L. & Rita Teutonico. (1999). TRANSGENIC ANIMALS FOR PRODUCTION OF PROTEINS. 19(9). 1–1. 5 indexed citations
18.
Yeh, Yung‐Hsin, R.E. Feeney, Robert L. McKown, & Christopher J. Warren. (1994). Measurement of grain growth in the recrystallization of rapidly frozen solutions of antifreeze glycoproteins. Biopolymers. 34(11). 1495–1504. 14 indexed citations
19.
McKown, Robert L. & Gareth Warren. (1991). Enhanced survival of yeast expressing an antifreeze gene analogue after freezing. Cryobiology. 28(5). 474–482. 20 indexed citations
20.
Mueller, G M, Robert L. McKown, Loren V. Corotto, Chuck Hague, & Gareth Warren. (1991). Inhibition of recrystallization in ice by chimeric proteins containing antifreeze domains. Journal of Biological Chemistry. 266(12). 7339–7344. 25 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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