Pharmacology
background shadow background pic Zheng

Ning Zheng, Ph.D.,
Associate Professor

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  phcol510  phcol575

Email: nzheng@uw.edu
Box 357280
HSC D429

Office: 206.616.3990
Lab: 206.616.3887
Fax: 206.685.3822
 

 

 

 

 

 

 

The blueprint of life encoded by the genome is interpreted, executed, and maintained by hundreds of thousands of proteins. Their precisely coordinated functions are fundamental to all biological systems and to every aspect of human health. We are in general interested in understanding how proteins interact with each other and with other biological molecules to mediate biological functions.

Figure Our current research focuses on a superfamily of multi-component protein machines, known as cullin-RING ubiquitin ligases. By controlling protein turnover, these cellular machines regulate diverse biological processes, such as cell cycle progression, signal transduction, transcription, DNA repair, and metabolism. Dysregulation of these cellular protein complexes has been associated with multiple human disorders including cancer, neurological diseases, and viral infection.

An important technique used in our research is protein complex X-ray crystallography. It allows us to determine the atomic 3-D structures of the protein machines we are interested in. Seeing is believing. A close-up view of these nano-scale cellular components can tell us in details how they engage and work together to make life possible.

From our studies, we hope to derive fundamental principles of biology at molecular level. More importantly, we hope that the results of our research will have a direct impact in biomedicine by accelerating the discovery and development of novel therapeutic drugs.



 

Publications 

Hormone signaling through protein destruction: a lesson from plants. - ABSTRACT

A ubiquitin-like protein unleashes ubiquitin ligases. - ABSTRACT

Wilms tumor suppressor WTX negatively regulates WNT/beta-catenin signaling. - ABSTRACT

Mechanism of auxin perception by the TIR1 ubiquitin ligase. - ABSTRACT

Molecular architecture and assembly of the DDB1-CUL4A ubiquitin ligase machinery. - ABSTRACT

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