Robert L. McKown, Ph.D.
Director, Biomanufacturing Laboratory
- Office: ISAT/CS 326
- Phone: 540-568-2776
- Email: firstname.lastname@example.org
- Mailing Address:
701 Carrier Drive
Harrisonburg, Virginia 22807
- Ph.D., Molecular Biology and Biochemistry, University of California, Irvine
- B.S., Biological Sciences, University of California, Irvine
- Professor, Department of Integrated Science and Technology, James Madison University, Harrisonburg, VA
- Vice President, Biomanufacturing, EyeRx Research, Inc., Norfolk, VA
- Adjunct Professor, Department of Biological Sciences, San Jose State University
- Senior Research Scientist, DNA Plant Technology Corporation, Oakland, CA
- Research Scientist, Advanced Genetic Sciences, Oakland, CA
- Postdoctoral Scholar, Microbiology and Immunology, University of California, San Francisco
Affiliations and Appointments
- Board of Directors, Chesapeake Bay Bioscience Education Foundation www.c-bef.org
- Board of Directors, Virginia Biotechnology Association www.vabio.org
- Board of Corporate Advisors, Biotechnology Training Program, University of Virginia http://faculty.virginia.edu/biotech/Home.html
- NSF National Visiting Committee, Northeast Biomanufacturing Center & Collaborative www.biomanufacturing.org
- Lacritin Research Consortium http://people.virginia.edu/~gwl6s/home.html/Lacritin_Consortium.html
- Affiliate Professor, Biology Department, James Madison University
Scholarly Interests/Research Topics
- Development of Novel Diagnostics and Treatments for Ocular Diseases
- Structure and Function of Human Antimicrobial Proteins
- Modeling Novel Treatments for Dry Eye
- Structure and Function of Ocular Lacritin, a Human Tear Protein
Sandeep, S.S., Lattanzio, F.A., Lossen, V., Hosseini, A., Sheppard, J.D., McKown, R.L., Laurie, G.W., and Williams, P.B. Lacritin, a Novel Human Tear Glycoprotein Promotes Sustained Basel Tearing and is Well Tolerated. Investigative Ophthalmology & Visual Science. Revised manuscript submitted September 2010.
Yinghui Zhang, Robert L. McKown, Ronald W. Raab, Alan C. Rapraeger, Gordon W. Laurie. Focus on Molecules: Syndecan-1. Experimental Eye Research. In Press, available on line June, 2010.
Robert L. McKown, Ningning Wang, Ronald W. Raab, Roy Karnati, Yinghui Zhang, Patricia Williams, Gordon W. Laurie (2009) Lacritin and other new proteins of the lacrimal functional unit. Experimental Eye Research. 88(5): 848-58.
Laurie, G.W., Olsakovsky, L.A., Conway, B.P., McKown, R.L., Kitagawa, K., and Nichols, J.J. (2008) Dry Eye and Designer Ophthalmic Treatments. Optometry & Vision Science. 85(8)1040-5488.
McKown, Robert L., Raab, Ronald W. and Laurie, Gordon W. Antimicrobial Activity in Variants of Lacritin. International Patent Publication Number WO 2008/033477 A2. 20 March, 2008.
Peisong Ma, Ningning Wang, Robert L. McKown, Ronald W. Raab, and Gordon W. Laurie. (2008) Focus on Molecules: Lacritin. Experimental Eye Research. 86(3): 457-458.
Wang, J., Wang, N., Xie, J., Walton, S., McKown. R., Raab, R., Ma, P., Beck, S., Coffman, G., Hussaini, I., and Laurie, G. (2006) Restricted epithelial proliferation by lacritin via PKC-dependent NFAT and mTOR pathways. J. Cell Biol. 174: 889-700.
Ma, P., S.L. Beck, R.W. Raab, R.L. McKown, G.L. Coffman, A. Utani, W.J.Chirico, A.C. Rapraeger, and G.W. Laurie. (2006) Heparanase deglycanation of syndecan-1 is required for binding of epithelial-restricted prosecretory mitogen “lacritin”. J. Cell Biol. 174: 1097-1106.
J. L. Goodin, R. W. Raab, R. L. McKown, G. Coffman, B. S. Powell, J. T. Enama, J. A. Ligon, and G. P. Andrews. (2005) Yersinia pestis outer membrane type III secretion protein YscC: expression, purification, characterization, and induction of specific antiserum. Protein Expression. & Purification. 40, 152-163.
NIH/STTR R42 Phase II
Stimulation of Tear Secretion by a Novel Glycoprotein
Modeling Novel Treatments for Dry Eye
Commonwealth Health Research Board
Development of Novel Diagnostics and Treatments for Ocular Diseases
Structure and Function of Ocular Lacritin
NIH STTR Phase I R42
Proof of Concept for Antimicrobial Properties of Lacritin In Vitro
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