Ph. D., Washington State University

   

 

Office:     325B Life Sciences Building

Phone:   1-419-372-8923

Email:     johnsg@bgsu.edu

   

 

Research:

Plant molecular biology and biochemistry

   

 

   

Research Interests:

Molecular biology and biochemistry of extracellular plant proteinases; folate metabolism and seed coat physiology.

Selected Publications:

ALiu, C.Y., H. Xu and J.S. Graham. 1998. Cloning and characterization of an Arabidopsis cDNA (Gen Bank AF062640) homologous to the matrix metalloproteinases. Plant Physiol. 117:1127.

Rickle, S.A., H. Xu, C.Y. Liu, P.F. Morris and J.S. Graham. 1998. Cloning of a gamma-glutamyl hydrolase cDNA (Gen Bank AF067141) from Arabidopsis. Plant Physiol. 117:1526.

Pak, J.H., C.Y. Liu, J. Huangpu and J.S. Graham. 1997. Characterization and development analysis of the soybean leaf metalloproteinase cDNA. FEBS Lett. 404:283-288.

Huangpu, J., J.H. Pak, W. Burkhart, M.C. Graham, S. Rickle, C.Y. Liu and J.S. Graham. 1996. Cloning of a soybean leaf cDNA (Gen Bank U63726) homologous to gamma glutamyl hydrolase. Plant Physiol. 112:862.

Huangpu, J., J.H. Pak, M.C. Graham, S.A. Rickle and J.S. Graham. 1996. Purification and molecular analysis of an extracellular ?-glutamyl hydrolase present in young tissues of the soybean plant. Biochem. Biophys. Res. Comm. 228:1-6.

Huangpu, J., M.C. Graham, and J.S. Graham. 1996. Cloning of a soybean cDNA (Accession No. U41657) encoding the abundant anionic seed coat peroxidase. Plant Physiol. 110:714.

Huangpu, J., and J.S. Graham. 1995. Purification and developmental analysis of an extracellular proteinase from young leaves of Glycine max. Plant Physiol. 108:969-974.

Diehn, S.H., W. Burkhart and J.S. Graham. 1994. Purfication and partial amino acid sequence of a wound-inducible, developmentally regulated anionic peroxidase from soybean leaves. Biochemical and Biophysical Research Communications 195(2):928-934.

McGeehan, J.W., W. Burkhart, J. Anderegg, J.D. Becherer, J.W. Gillikin and J.S. Graham. 1992. Sequencing and characterization of the soybean leaf metalloproteinase: Structural and functional similarity to the matrix metalloproteinase family. Plant Physiol. 99:1179-1183.

Graham, J.S., J. Xiong and J.W. Gillikin. 1991. Purification and developmental analysis of a metalloendoproteinase from the leaves of Glycine max. Plant Physiol. 97:786-792.

Gillikin, J.W., W. Burkhart and J.S. Graham. 1991. Complete amino acid sequence of a polypeptide from Zeamays similar to the pathogenesis-related-1 family. Plant Physiol. 96:1372.

Gillikin, J.W., and J.S. Graham. 1991. Purification and developmental analysis of the major anionic peroxidase from the seed coat of Glycine max. Plant Physiol. 96:214-220.

Graham, J.S., G. Pearce and C.A. Ryan. 1986. Regulation of Inhibitor I and II mRNA biosynthesis in tomato leaves during the wound response. Planta 169:399-405.

Lee, J.S., W.E. Brown, J.S. Graham, G. Pearce, E. Fox, T.W. Dreher, K.G. Ahern, G.D. Pearson and C.A. Ryan. 1986. Molecular characterization and phylogenetic studies of a wound-inducible proteinase inhibitor I gene in Lycopersicon species. Proc. Natl. Acad. Sci. USA 83:7277-7281.

Graham, J.S., G. Pearce, J. Merryweather, K. Titani, L. Erickson and C.A. Ryan. 1985. Wound-induced proteinase inhibitor from tomato leaves: II. The cDNA-deduced primary structure of pre-inhibitor II. J. Biol. Chem. 260:6561-6564.

Graham, J.S., G. Pearce, J. Merryweather, K. Titani, L. Erickson and C.A. Ryan. 1985. Wound-induced proteinase inhibitors from tomato leaves: I. The cDNA-deduced primary structure of preinhibitor I and its post-translational processing. J. Biol. Chem. 260:6555-6560.