Wenyu Li
Princeton University
8 Papers
Wenyu Li is an academic researcher from Princeton University. The author has contributed to research in topics: Biology & Apoptosis. The author has an hindex of 7, co-authored 7 publications.
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Papers
Crystal Structure of a UBP-Family Deubiquitinating Enzyme in Isolation and in Complex with Ubiquitin Aldehyde
Min Hu,Pingwei Li,Muyang Li,Wenyu Li,Tingting Yao,Jia-Wei Wu,Wei Gu,Robert E. Cohen,Yigong Shi +8 more
TL;DR: In this paper, the crystal structures of the 40 kDa catalytic core domain of HAUSP in isolation and in complex with ubiquitin aldehyde were reported, showing that the UBP deubiquitinating enzymes exhibit a conserved three-domain architecture, comprising Fingers, Palm and Thumb.
607
Structure of the apoptotic protease-activating factor 1 bound to ADP
TL;DR: The 2.2-Å crystal structure of an ADP-bound, WD40-deleted Apaf-1 is reported, which reveals the molecular mechanism by which Apf-1 exists in an inactive state before ATP binding, and drives conformational changes that are essential for the formation of the apoptosome and the activation of caspase-9.
375
Structural insights into the pro-apoptotic function of mitochondrial serine protease HtrA2/Omi
Wenyu Li,Srinivasa M. Srinivasula,Jijie Chai,Pingwei Li,Jia-Wei Wu,ZhiJia Zhang,Emad S. Alnemri,Yigong Shi +7 more
TL;DR: Structural and biochemical observations provide an important framework for deciphering the mechanisms of HtrA2/Omi-mediated apoptosis and reveal a pyramid-shaped homotrimer mediated exclusively by the serine protease domains.
302
Structural mechanism of Smad4 recognition by the nuclear oncoprotein Ski: insights on Ski-mediated repression of TGF-beta signaling.
TL;DR: The Ski family of nuclear oncoproteins represses TGF-beta signaling through interactions with the Smad proteins, and the structure of the Ski fragment, stabilized by a bound zinc atom, resembles the SAND domain, in which the corresponding I loop is responsible for DNA binding.
225
Molecular mechanism of Reaper-Grim-Hid-mediated suppression of DIAP1-dependent Dronc ubiquitination.
TL;DR: The structural basis of Dronc recognition by DIAP1 is reported as well as a novel mechanism by which the RHG proteins removeDIAP1-mediated downregulation of Dronsc.
155