Y
Yang Li
Researcher at Harvard University
Publications - 19
Citations - 715
Yang Li is an academic researcher from Harvard University. The author has contributed to research in topics: Mitochondrion & Clime. The author has an hindex of 12, co-authored 19 publications receiving 546 citations. Previous affiliations of Yang Li include Boston Children's Hospital & Broad Institute.
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Journal ArticleDOI
Expansion of Biological Pathways Based on Evolutionary Inference
TL;DR: A computational algorithm, clustering by inferred models of evolution (CLIME), which inputs a eukaryotic species tree, homology matrix, and pathway (gene set) of interest, and reveals unanticipated evolutionary modularity and coevolving components.
Journal ArticleDOI
A Compendium of Genetic Modifiers of Mitochondrial Dysfunction Reveals Intra-organelle Buffering
Tsz-Leung To,Alejandro M. Cuadros,Hardik Shah,Hardik Shah,Wendy H. W. Hung,Yang Li,Yang Li,Sharon H. Kim,Sharon H. Kim,Daniel H. F. Rubin,Daniel H. F. Rubin,Ryan H. Boe,Sneha Rath,Sneha Rath,John K. Eaton,Federica Piccioni,Amy Goodale,Zohra Kalani,John G. Doench,David E. Root,Stuart L. Schreiber,Stuart L. Schreiber,Scott B. Vafai,Vamsi K. Mootha,Vamsi K. Mootha +24 more
TL;DR: Perhaps paradoxically, certain forms of mitochondrial dysfunction may best be buffered with "second site" inhibitors to the organelle, which benefits cells by rebalancing redox cofactors, increasing reductive carboxylation, and promoting glycolysis.
ComponentDOI
Cryo-EM structures of ASC and NLRC4 CARD filaments reveal a unified mechanism of nucleation and activation of caspase-1.
Yang Li,Yang Li,Tian-Min Fu,Tian-Min Fu,Alvin Lu,Alvin Lu,Kristen Witt,Kristen Witt,Jianbin Ruan,Jianbin Ruan,Chen Shen,Chen Shen,Hao Wu,Hao Wu +13 more
TL;DR: Cryo-electron microscopy structures of NLRC4 CARD and ASC CARD filaments mediated by conserved three types of asymmetric interactions are presented, which indicate a unified mechanism for downstream caspase-1 recruitment through CARD–CARD interactions by both adaptors.
Journal ArticleDOI
Cryo-EM structure of the DNA-PK holoenzyme.
Humayun Sharif,Yang Li,Yang Li,Yuanchen Dong,Liyi Dong,Liyi Dong,Wei Li Wang,Youdong Mao,Youdong Mao,Hao Wu +9 more
TL;DR: Cryo-electron microscopy structures of the DNA-PK complex lead to a partial model for the interactions between DNA- PKcs and the Ku70/80 complex, and reveal how theDNA- PK complex may bring free ends of damaged DNA for repair.
ComponentDOI
Assembly mechanism of the CARMA1-BCL10-MALT1-TRAF6 signalosome.
TL;DR: Cryo-electron microscopy data reveal biophysical mechanisms in the assembly of the CARMA1-BCL10-MALT1-TRAF6 complex for signal transduction and suggest immediate dimerization of MALT1 in the BCL10 filamentous scaffold.