Yunfeng Li
University of Connecticut Health Center
22 Papers
18 Citations
Yunfeng Li is an academic researcher from University of Connecticut Health Center. The author has contributed to research in topics: Spore germination & Biology. The author has an hindex of 12, co-authored 16 publications. Previous affiliations of Yunfeng Li include University of Connecticut.
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Papers
Role of a SpoVA protein in dipicolinic acid uptake into developing spores of Bacillus subtilis
Yunfeng Li,Andrew Davis,George Korza,Pengfei Zhang,Yong-qing Li,Barbara Setlow,Peter Setlow,Bing Hao +7 more
TL;DR: These results provide direct evidence that SpoVA proteins, in particular SpoVAD, are directly involved in DPA(2,6) movement into developing B. subtilis spores.
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Functional coupling of TRPM2 and extrasynaptic NMDARs exacerbates excitotoxicity in ischemic brain injury
Pengyu Zong,Jianlin Feng,Zhichao Yue,Yunfeng Li,Gongxiong Wu,Baonan Sun,Yanlin He,Barbara A. Miller,Albert S. Yu,Zhongping Su,Jia Xie,Yasuo Mori,Bing Hao,Lixia Yue +13 more
TL;DR: Zhang et al. as discussed by the authors showed that NMDAR-induced excitotoxicity is enhanced by physical and functional coupling of NMDA receptor to an ion channel TRPM2 upon ischemic insults.
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Activity and regulation of various forms of CwlJ, SleB, and YpeB proteins in degrading cortex peptidoglycan of spores of Bacillus species in vitro and during spore germination.
Yunfeng Li,Xuan Yi Butzin,Andrew Davis,Barbara Setlow,George Korza,Fatma Işık Üstok,Graham Christie,Peter Setlow,Bing Hao +8 more
TL;DR: In this study, in vitro and in vivo analyses have been used to clarify the roles of individual SleB and YpeB domains in PG degradation and support the role of this invariant glutamate as the key catalytic residue insleB and CwlJ.
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Crystal Structure of the Catalytic Domain of the Bacillus cereus SleB Protein, Important in Cortex Peptidoglycan Degradation during Spore Germination
TL;DR: SleB bearing a Glu157-to-Gln mutation lost its cortex degradative activity completely, and CwlJ in Bacillus species likely has a three-dimensional structure similar to that of SleB, including the invariant putative catalytic Glu residue.
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Function of the SpoVAEa and SpoVAF Proteins of Bacillus subtilis Spores
Abigail Perez-Valdespino,Yunfeng Li,Barbara Setlow,Sonali Ghosh,David Pan,George Korza,Florence E. Feeherry,Christopher J. Doona,Yong-qing Li,Bing Hao,Peter Setlow +10 more
TL;DR: The Bacillus subtilis spoVAEa and spoVAF genes are expressed in developing spores as members of the spoVA operon, which encodes proteins essential for the uptake and release of dipicolinic acid during spore formation and germination.
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