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Jasper Yik, Ph.D.

Jasper Yik

Clinical/Research Interests

Regulation of gene expression during chondrocyte differentiation from stem cells. Identification of novel transcription factors important for chondrogenesis and cartilage homeostatis.

Specialty:

Orthopaedic Surgery

Address:

Research I
4635 2nd Ave.
Sacramento, CA 95817

Education:

University of Oklahoma, Health Sciences Center
Oklahoma City, Oklahoma
Ph.D. 2002

Education:

University of Central Oklahoma
Edmond, Oklahoma
B.S. 1995

Select Recent Publications:

Barboric, M., Yik, J.H.N., Czudnochowski, N., Yang, Z., Chen, R., Contreras, X., Geyer, M., Matija, Peterlin B., Zhou, Q. Tat competes with HEXIM1 to increase the active pool of P-TEFb for HIV-1 transcription. Nucleic Acids Res. (2007) 35: 2003-2012 (co-first authors)

Zhou, Q., and Yik, J.H.N. The Yin and Yang of P-TEFb regulation: implications for HIV gene expression and the global control of cell growth and differentiation. Microbio. Mol. Bio. Review (2006) 70: 646-659

Yang, Z., Yik, J.H.N., Chen, R., He, N., Jang, M.K., Ozato, K., and Zhou, Q. Recruitment of P-TEFb for stimulation of transcriptional elongation by bromodomain protein Brd4. Mol. Cell (2005) 19: 535-545

Yik, J.H.N., Chen, R., Pezda, A.C., and Zhou, Q. Compensatory contributions of HEXIM1 and HEXIM2 in maintaining the balance of active and inactive P-TEFb complexes for control of transcription. J. Biol. Chem. (2005) 280: 16368-16376

Yik, J.H.N., Chen, R., Pezda, A.C., Samford, C.S., and Zhou, Q. A Human Immuno-deficiency Virus Type-1 Tat-like arginine-rich RNA-binding domain is essential for HEXIM1 to inhibit RNA polymerase II transcription through 7SK snRNA-mediated inactivation of P-TEFb. Mol. Cell. Biol. (2004) 24: 5094-5105

Yik, J.H.N., Chen, R., Nishimura, R., Jennings, J., Link, A.J., and Zhou, Q. Inhibition of P-TEFb (CDK9/cyclin T) kinase and RNA polymerase II transcription by the coordinated actions of HEXIM1 and 7SK snRNA. Mol. Cell (2003)12: 971-982

Yik, J.H.N., Saxena, A., and Weigel, P.H. The minor subunit splice variant, H2b and H2c, of the human asialoglycoprotein receptor are present with the major subunit H1 in different hetero-oligomeric receptor complexes. J. Biol. Chem. (2002) 277: 23076-23083

Yik, J.H.N., Saxena, A., Weigel, J.A., and Weigel, P.H. Nonpalmitoylated asialo-glycoprotein receptors recycle constitutively but are defective in coated pit-mediated endocytosis, dissociation, and delivery of ligand to lysosomes. J. Biol. Chem. (2002) 277: 40844-40852

Yik, J.H.N., and Weigel, P.H. The position of cysteine relative to the transmembrane domain is critical for palmitoylation of H1, the major subunit of the human asialoglyco-protein receptor. J. Biol. Chem. (2002) 277: 47305-47312

Yik, J.H.N., Saxena, A., Weigel, J.A., and Weigel, P.H. Palmitoylation-defective asialo-glycoprotein receptors are normal in their cellular distribution and ability to bind ligand, but are defective in ligand uptake and degradation. Biochem. Biophys. Res. Commun. (2002) 297: 980-986