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Wenqing Xu
Researcher at University of Washington
Publications - 74
Citations - 9223
Wenqing Xu is an academic researcher from University of Washington. The author has contributed to research in topics: Wnt signaling pathway & Protein phosphatase 2. The author has an hindex of 38, co-authored 66 publications receiving 8329 citations. Previous affiliations of Wenqing Xu include Harvard University & Boston Children's Hospital.
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Journal ArticleDOI
Three-dimensional structure of the tyrosine kinase c-Src
TL;DR: The structure of a large fragment of the c-SRC tyrosine kinase, comprising the regulatory and kinase domains and the carboxy-terminal tail, has been determined and shows how appropriate cellular signals, or transforming mutations in v-Src, could break these interactions to produce an open, active kinase.
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Crystal structures of c-Src reveal features of its autoinhibitory mechanism.
TL;DR: Four additional c-Src structures in which this segment adopts an ordered but inhibitory conformation are reported, in which the ordered activation loop forms an alpha helix that stabilizes the inactive conformation of the kinase domain, blocks the peptide substrate-binding site, and prevents Tyr-416 phosphorylation.
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beta-catenin destruction complex: insights and questions from a structural perspective.
David Kimelman,Wenqing Xu +1 more
TL;DR: This work suggests a working model for the destruction complex based on the existing structural and experimental data, and focuses on the questions that this model and other studies have raised about the function of the complex in both the normal and Wnt-inhibited states.
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Recognition of Antimicrobial Peptides by a Bacterial Sensor Kinase
Martin Bader,Sarah Sanowar,Margaret E. Daley,Anna Schneider,Uhn-Soo Cho,Wenqing Xu,Rachel E. Klevit,Hervé Le Moual,Samuel I. Miller +8 more
TL;DR: It is shown that enzymatic activity of Salmonella typhimurium PhoQ is directly activated by antimicrobial peptides.
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Crystal structure of a protein phosphatase 2A heterotrimeric holoenzyme
Uhn-Soo Cho,Wenqing Xu +1 more
TL;DR: The crystal structure of an AB′C heterotrimeric PP2A holoenzyme reveals that the HEAT repeats of the scaffold A subunit form a horseshoe-shaped fold, holding the catalytic C and regulatory B′ subunits together on the same side.