John has over 25 years experience as a research scientist and senior research executive in the biotechnology/pharmaceutical industry, specifically as Senior Director of Molecular Biology and Gene Expression at Genetics Institute and Wyeth Pharmaceuticals, as Vice President of Discovery Biology at Biogen Idec, and as Chief Scientific Officer at RenaMed Biologics. John's broad background includes expertise in protein and general biochemistry, recombinant protein expression and cell culture in both microbial and mammalian systems, molecular biology and genomics, and disease biology in the areas of immunology/inflammation, oncology, neurodegeneration / neurorepair, fibrosis, and renal and placental disorders. John is author of over 60 research articles.
He is also an inventor on 42 issued United States patents in the areas of recombinant gene expression technology, gene discovery technology, protein-protein interaction methods, novel genes, therapeutic proteins and modified therapeutic proteins.
John M McCoy PhD, selected publications
- Dunn R, McCoy J, Simsek M, Majumdar A, Chang SH, Rajbhandary UL, Khorana HG. The bacteriorhodopsin gene. Proc Natl Acad Sci U S A 1981, Nov;78(11):6744-8.
- McCoy JM, Khorana HG. Introduction and characterization of amber mutations in the bacteriorhodopsin gene. J Biol Chem 1983;258(13):8456-61.
- Gilles-Gonzalez MA, Hackett NR, Jones SJ, Khorana HG, Lee DS, Lo KM, McCoy JM. Methods for mutagenesis of the bacterioopsin gene. Methods Enzymol 1986;125:190-214.
- Dunn RJ, Hackett NR, McCoy JM, Chao BH, Kimura K, Khorana HG. Structure-Function studies on bacteriorhodopsin. I. Expression of the bacterio-opsin gene in escherichia coli. J Biol Chem 1987, Jul 5;262(19):9246-54.
- Huber HE, McCoy JM, Seehra JS, Richardson CC. Human immunodeficiency virus 1 reverse transcriptase. Template binding, processivity, strand displacement synthesis, and template switching. J Biol Chem 1989, Mar 15;264(8):4669-78.
- LaVallie ER, DiBlasio EA, Kovacic S, Grant KL, Schendel PF, McCoy JM. A thioredoxin gene fusion expression system that circumvents inclusion body formation in the E. Coli cytoplasm. Biotechnology (N Y) 1993, Feb;11(2):187-93.
- LaVallie ER, Rehemtulla A, Racie LA, DiBlasio EA, Ferenz C, Grant KL, et al. Cloning and functional expression of a cdna encoding the catalytic subunit of bovine enterokinase. J Biol Chem 1993, Nov 5;268(31):23311-7.
- Czupryn M, Bennett F, Dube J, Grant K, Scoble H, Sookdeo H, McCoy JM. Alanine-Scanning mutagenesis of human interleukin-11: Identification of regions important for biological activity. Ann N Y Acad Sci 1995, Jul 21;762:152-64.
- Lu Z, Murray KS, Van Cleave V, LaVallie ER, Stahl ML, McCoy JM. Expression of thioredoxin random peptide libraries on the escherichia coli cell surface as functional fusions to flagellin: A system designed for exploring protein-protein interactions. Biotechnology (N Y) 1995, Apr;13(4):366-72.
- Collins-Racie LA, McColgan JM, Grant KL, DiBlasio-Smith EA, McCoy JM, LaVallie ER. Production of recombinant bovine enterokinase catalytic subunit in escherichia coli using the novel secretory fusion partner dsba. Biotechnology (N Y) 1995, Sep;13(9):982-7.
- Czupryn MJ, McCoy JM, Scoble HA. Structure-Function relationships in human interleukin-11. Identification of regions involved in activity by chemical modification and site-directed mutagenesis. J Biol Chem 1995, Jan 13;270(2):978-85.
- Lu Z, DiBlasio-Smith EA, Grant KL, Warne NW, LaVallie ER, Collins-Racie LA, et al. Histidine patch thioredoxins. Mutant forms of thioredoxin with metal chelating affinity that provide for convenient purifications of thioredoxin fusion proteins. J Biol Chem 1996, Mar 1;271(9):5059-65.
- Colas P, Cohen B, Jessen T, Grishina I, McCoy J, Brent R. Genetic selection of peptide aptamers that recognize and inhibit cyclin-dependent kinase 2. Nature 1996, Apr;380(6574):548-50.
- Jacobs KA, Collins-Racie LA, Colbert M, Duckett M, Golden-Fleet M, Kelleher K, et al. A genetic selection for isolating cdnas encoding secreted proteins. Gene 1997, Oct 1;198(1-2):289-96.
- Lu Z, Tripp BC, McCoy JM. Displaying libraries of conformationally constrained peptides on the surface of escherichia coli as flagellin fusions. Methods Mol Biol 1998;87:265-80.
- Smith PA, Tripp BC, DiBlasio-Smith EA, Lu Z, LaVallie ER, McCoy JM. A plasmid expression system for quantitative in vivo biotinylation of thioredoxin fusion proteins in escherichia coli. Nucleic Acids Res 1998, Mar 15;26(6):1414-20.
- Sun BI, Bush SM, Collins-Racie LA, LaVallie ER, DiBlasio-Smith EA, Wolfman NM, et al. Derriere: A tgf-beta family member required for posterior development in xenopus. Development 1999, Apr;126(7):1467-82.
- Jacobs KA, Collins-Racie LA, Colbert M, Duckett M, Evans C, Golden-Fleet M, et al. A genetic selection for isolating cdna clones that encode signal peptides. Methods Enzymol 1999;303:468-79.
- LaVallie ER, Lu Z, Diblasio-Smith EA, Collins-Racie LA, McCoy JM. Thioredoxin as a fusion partner for production of soluble recombinant proteins in escherichia coli. Methods Enzymol 2000;326:322-40.
- Mi S, Lee X, Li X, Veldman GM, Finnerty H, Racie L, et al. Syncytin is a captive retroviral envelope protein involved in human placental morphogenesis. Nature 2000, Feb 17;403(6771):785-9.
- Lee X, Keith, C. J, Jr., Stumm N, Moutsatsos I, et al. Downregulation of placental syncytin expression and abnormal protein localization in pre-eclampsia. Placenta 2001, Nov;22(10):808-12.
- Mi S, Lee X, Shao Z, Thill G, Ji B, Relton J, et al. LINGO-1 is a component of the nogo-66 receptor/p75 signaling complex. Nat Neurosci 2004, Mar;7(3):221-8.
- Mi S, Miller RH, Lee X, Scott ML, Shulag-Morskaya S, Shao Z, et al. LINGO-1 negatively regulates myelination by oligodendrocytes. Nat Neurosci 2005, Jun;8(6):745-51.
- Shao Z, Browning JL, Lee X, Scott ML, Shulga-Morskaya S, Allaire N, et al. TAJ/TROY, an orphan TNF receptor family member, binds nogo-66 receptor 1 and regulates axonal regeneration. Neuron 2005, Feb 3;45(3):353-9.
- Ji B, Li M, Wu WT, Yick LW, Lee X, Shao Z, et al. LINGO-1 antagonist promotes functional recovery and axonal sprouting after spinal cord injury. Mol Cell Neurosci 2006, Sep 28;33(3):311-20.