You Feng

发表

Synthesis and evaluation of carbocyanine dyes as PRMT inhibitors and imaging agents.

Eric A. Owens, M. Henary, Y. Zheng, 2012, European journal of medicinal chemistry.

Pharmacophore-based virtual screening and biological evaluation of small molecule inhibitors for protein arginine methylation.

Hualiang Jiang, Y. Chou, Chao Yang, 2012, Journal of medicinal chemistry.

Kinetic mechanism and inhibitory study of protein arginine methyltransferase 1

You Feng, 2012 .

Discovery and mechanistic study of a class of protein arginine methylation inhibitors.

B. Wang, Y. Zheng, You Feng, 2010, Journal of medicinal chemistry.

Inhibitory study of protein arginine methyltransferase 1 using a fluorescent approach.

Yujun George Zheng, Chao Yang, Chao Yang, 2009, Biochemical and biophysical research communications.

A transient kinetic analysis of PRMT1 catalysis.

M. Stahley, J. Stivers, Y. Zheng, 2011, Biochemistry.

Histone H4 Acetylation Differentially Modulates Arginine Methylation by an in Cis Mechanism*

Y. G. Zheng, I. Ivanov, You Feng, 2011, The Journal of Biological Chemistry.

Substrate Specificity of Human Protein Arginine Methyltransferase 7 (PRMT7)

S. Clarke, You Feng, Andrea Hadjikyriacou, 2014, The Journal of Biological Chemistry.

Probing the general time scale question of boronic acid binding with sugars in aqueous solution at physiological pH.

B. Wang, Y. Zheng, You Feng, 2012, Bioorganic & medicinal chemistry.

Mammalian Protein Arginine Methyltransferase 7 (PRMT7) Specifically Targets RXR Sites in Lysine- and Arginine-rich Regions*

S. Clarke, A. Clark, J. Masson, 2013, The Journal of Biological Chemistry.

Scintillation Proximity Assay of Arginine Methylation

Y. G. Zheng, Jiang Wu, You Feng, 2012, Journal of biomolecular screening.

A glutamate/aspartate switch controls product specificity in a protein arginine methyltransferase

G. Blobel, E. Debler, S. Clarke, 2016, Proceedings of the National Academy of Sciences.

Labeling lysine acetyltransferase substrates with engineered enzymes and functionalized cofactor surrogates.

Leilei Yan, Y. Zheng, You Feng, 2013, Journal of the American Chemical Society.

t‐Darpp is an elongated monomer that binds calcium and is phosphorylated by cyclin‐dependent kinases 1 and 5

Dianlu Jiang, Feimeng Zhou, S. Kane, 2017, FEBS open bio.

t-Darpp is an elongated monomer that binds to calcium and is phosphorylated by cyclin-dependent kinases 1 and 5

S. Kane, Xiaoying Wang, J. Momand, 2017, bioRxiv.

Overexpression of t-Darpp in cultured cells leads to increased protein kinase A activity and increased phosphorylation of AKT (protein kinase B). In HER2+ breast cancer cells t-Darpp

S. Kane, Xiaoying Wang, J. Momand, 2017 .