Dr. Yang joined the College in September 2003.
Undergraduate teaching in the areas of Medicinal Chemistry and Structural Biochemistry.
Dr. Yang’s research laboratory is interested in understanding the structural basis for important biological functions using protein crystallography as a tool. Currently, the laboratory is working on two major research projects.
1. The PCP biodegradation pathway: This pathway contains three enzymes, PCP hydroxylase, TCHQ dehalogenase and DCHQ dioxygenase. PCP hydroxylase catalyzes the conversion of PCP to TCHQ, which is the rate-limiting step in the pathway. TCHQ dehalogenase catalyzes the two successive steps of reduction reactions, converting TCHQ to TriCHQ and then to DCHQ. DCHQ is a common metabolic intermediate of PCP and several other chloroaromatic compounds. DCHQ dioxygenase is so far the only reported enzyme that degrades DCHQ. The end product of the ring cleavage of DCHQ is 2-chloromaleylacetate.
2. The Toll receptor signaling pathway: This pathway was first identified in Drosophila in the study of early embryonic development. Subsequent studies reveal that the Toll receptor signaling pathway is one of the major signaling pathways for Drosophila innate immunity. The Toll signaling pathway is activated by Gram-positive bacteria and fungi, whereas the immune deficiency (Imd)/Relish pathway is responsible for defense against Gram-negative pathogens. The Toll receptor itself does not recognize microbial patterns. Its activation requires a dimeric extracellular protein, Spätzle. The activation of the Toll receptor by Spätzle initiates the cytoplasmic-nuclear translocation of a family of transcription factors in the NF-KB family and produces the antimicrobial peptide drosomycin.
(see more in Scopus)
Sultan, A., Ling, B., Zhang, H., Ma, B., Michel, D., Alcorn, J., Yang, J. Synergistic effect between sphingosine-1-phosphate and chemotherapy drugs against human brainmetastasized breast cancer MDA-MB-361 cells (2013) Journal of Cancer, 4 (4), pp. 315-319.
Ling, B., Dong, Q., Sun, W., Michel, D., Jiao, R., Sammynaiken, R., Zhou, Y., Yang, J. Evaluating the anticancer activity of Hedyotis diffusa water extract against human breast cancer MCF7 cells (2013) Open Natural Products Journal, 6 (1), pp. 1-4.
Maley, J., Schatte, G., Yang, J., Sammynaiken, R. Spontaneous Ag-nanoparticle growth at single-walled carbon nanotube defect sites: A tool for in situ generation of SERS substrate (2011) Journal of Nanotechnology, art. no. 408151.
Ling, B., Chen, L., Alcorn, J., Ma, B., Yang, J. Sphingosine-1-phosphate: A potential therapeutic agent against human breast cancer (2011) Investigational New Drugs, 29 (2), pp. 396-399.
Sun, W., Qiao, L., Liu, Q., Chen, L., Ling, B., Sammynaiken, R., Yang, J. Anticancer activity of the PR domain of tumor suppressor RIZ1 (2011) International Journal of Medical Sciences, 8 (2), pp. 161-167.
Sun, W., Yang, J. Functional mechanisms for human tumor suppressors (2010) Journal of Cancer, 1 (1), pp. 136-140.
Chen, L., Ling, B., Alcorn, J., Yang, J. Quantitative analysis of the expression of human n-myristoyltransferase 1 (hNMT-1) in cancers (2009) Open Biomarkers Journal, 2 (1), pp. 6-10.
Chen, L., Maloney, K., Krol, E., Zhu, B., Yang, J. Cloning, overexpression, purification, and characterization of the maleylacetate reductase from Sphingobium chlorophenolicum strain ATCC 53874 (2009) Current Microbiology, 58 (6), pp. 599-603.
Senanayake, V., Juurlink, B.H., Zhang, C., Zhan, E., Wilson, L.D., Kwon, J., Yang, J., Lim, Z.L., Brunet, S.M.K., Schatte, G., Maley, J.M., Hoffmeyer, R.E., Sammynaiken, R. Do surface defects and modification determine the observed toxicity of carbon nanotubes? (2008) Journal of Biomedical Nanotechnology, 4 (4), pp. 515-523.
Sun, W., Geyer, C.R., Yang, J. Cloning, expression, purification and crystallization of the PR domain of human retinoblastoma protein-binding zinc finger protein 1 (RIZ1) (2008) International Journal of Molecular Sciences, 9 (6), pp. 943-950.
Chen, L., Yang, J. Biochemical characterization of the tetrachlorobenzoquinone reductase involved in the biodegradation of pentachlorophenol (2008) International Journal of Molecular Sciences, 9 (3), pp. 198-212.