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Yasuhiro Nishiyama, Ph.D. 1995, Kobe Gakuin University UT-Houston Medical School |
Research Interests: Artificial immunogens to promote peptidolytic antibody production; selective inhigibors of pathogenic antibodies; peptide and protein chemistry
Our research, in close collaboration with Dr. Sudhir Paul's group,
is directed towards development of (1) artificial immunogens (chemically modified
peptides, proteins, viruses, etc.) that promote elicitation of antibodies with
peptidase activity specific to pathogens and (2) selective inhibitors of pathogenic
antibodies. Our current targets include catalytic antibodies that hydrolyze
envelope proteins of HIV and HCV and selective inhibitors of VIP-hydrolyzing
antibodies. A tutorial in my laboratory would provide experience in one or more
of the following areas: peptide and protein chemistry, synthetic chemistry using
solid-phase methods, structure determination using mass spectrometry, antibody
catalysis and inhibition kinetics, epitope analysis.
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Nishiyama Y, Bhatia G, Bangale Y, Planque S, Mmitsuda Y, Taguchi H, Karle S, Paul S (2004) Toward selective covalent inactivation of pathogenic antibodies: a phosphate diester analog of vasoactive intestinal peptide that inactivates catalytic autoantibodies. J Biol Chem 279:7877-7883.
Paul S, Planque S, Zhou YX, Taguchi H, Bhatia G, Karle S, Hanson C, Nishiyama Y (2003) Specific HIV gp120-cleaving antibodies induced by covalently reactive analog of gp120. J Biol Chem 278:20429-20435.
Taguchi H, Burr G, Karle S, Planque S, Zhou YX, Paul S, Nishiyama Y (2002) A mechanism-based probe for gp120-hydrolyzing antibodies. Bioorg Med Chem Lett 12:3167-3170.
Nishiyama Y, Taguchi H, Luo JQ, Zhou YX, Burr G, Karle S, Paul S (2002) Covalent reactivity of phosphonate menophenyl esters with serine proteinases: an overlooked feature of presumed transition state analogs. Arch Biochem Biophys 402:281-288.