Gang Yao, Ph.D.

Affiliations: 
2006 University of New Hampshire, Durham, NH, United States 
Area:
Molecular Biology, Biochemistry
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"Gang Yao"
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Parents

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Clyde L. Denis grad student 2006 UNH
 (Analysis of the role of poly(A) -binding protein (PAB1) in the mRNA degradation process in yeast.)
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Publications

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Yao G, Luo C, Harvey M, et al. (2015) Disruption of Polycystin-L causes Hippocampal Hyperexcitability. Human Molecular Genetics
Su X, Driscoll K, Yao G, et al. (2014) Bardet-Biedl syndrome proteins 1 and 3 regulate the ciliary trafficking of polycystic kidney disease 1 protein. Human Molecular Genetics. 23: 5441-51
Wang S, Wu M, Yao G, et al. (2014) The cytoplasmic tail of FPC antagonizes the full-length protein in the regulation of mTOR pathway. Plos One. 9: e95630
Yao G, Su X, Nguyen V, et al. (2014) Polycystin-1 regulates actin cytoskeleton organization and directional cell migration through a novel PC1-Pacsin 2-N-Wasp complex. Human Molecular Genetics. 23: 2769-79
Richardson R, Denis CL, Zhang C, et al. (2012) Mass spectrometric identification of proteins that interact through specific domains of the poly(A) binding protein. Molecular Genetics and Genomics : Mgg. 287: 711-30
Lee D, Ohn T, Chiang YC, et al. (2010) PUF3 acceleration of deadenylation in vivo can operate independently of CCR4 activity, possibly involving effects on the PAB1-mRNP structure. Journal of Molecular Biology. 399: 562-75
Yao G, Chiang YC, Zhang C, et al. (2007) PAB1 self-association precludes its binding to poly(A), thereby accelerating CCR4 deadenylation in vivo. Molecular and Cellular Biology. 27: 6243-53
Ohn T, Chiang YC, Lee DJ, et al. (2007) CAF1 plays an important role in mRNA deadenylation separate from its contact to CCR4. Nucleic Acids Research. 35: 3002-15
Clark LB, Viswanathan P, Quigley G, et al. (2004) Systematic mutagenesis of the leucine-rich repeat (LRR) domain of CCR4 reveals specific sites for binding to CAF1 and a separate critical role for the LRR in CCR4 deadenylase activity. The Journal of Biological Chemistry. 279: 13616-23
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