Xiaolong Li
Harvard University
12 Papers
21 Citations
Xiaolong Li is an academic researcher from Harvard University. The author has contributed to research in topics: Biology & Epitope. The author has an hindex of 6, co-authored 8 publications. Previous affiliations of Xiaolong Li include Huazhong Agricultural University & Peking University.
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Papers
Force-dependent transition in the T-cell receptor β-subunit allosterically regulates peptide discrimination and pMHC bond lifetime
Dibyendu Kumar Das,Yinnian Feng,Robert J. Mallis,Xiaolong Li,Derin B. Keskin,Rebecca E. Hussey,Sonia K. Brady,Jia-huai Wang,Jia-huai Wang,Gerhard Wagner,Ellis L. Reinherz,Matthew J. Lang +11 more
TL;DR: This work demonstrates a catch-and-release αβTCR structural conversion correlating with ligand potency wherein a strongly binding/compact state transitions to a weakly binding/extended state, supporting a model in which quaternary α βTCR subunit associations regulate TCR recognition under load.
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Terazosin activates Pgk1 and Hsp90 to promote stress resistance
Xinping Chen,Chunyue Zhao,Xiaolong Li,Tao Wang,Yizhou Li,Cheng Cao,Yue-He Ding,Meng-Qiu Dong,Lorenzo I. Finci,Jia-huai Wang,Xiaoyu Li,Lei Liu +11 more
TL;DR: Terazosin (TZ), a widely marketed α1-adrenergic receptor antagonist, alleviated organ damage and improved survival in rodent models of stroke and sepsis, and has a new protein target, Pgk1, and its corresponding biological effect is revealed.
Pre–T cell receptors topologically sample self-ligands during thymocyte β-selection
Xiaolong Li,Réka Mizsei,Kemin Tan,Robert J. Mallis,Jonathan S. Duke-Cohan,Aoi Akitsu,Paul W. Tetteh,Abhinav Dubey,Wonmuk Hwang,Gerhard Wagner,Matthew J. Lang,Haribabu Arthanari,Jia-huai Wang,Ellis L. Reinherz +13 more
TL;DR: X-ray crystallography is used to visualize how preTCRs recognize pMHCs and shows how a preTCR applies the concave β-sheet surface of its single variable domain (Vβ) to “horizontally” grab the protruding MHC α2-helix.
Crystal structure of HLA-B*5801 with a TW10 HIV Gag epitope reveals a novel mode of peptide presentation
TL;DR: Crystal structure of HLA-B*5801 with a TW10 HIV Gag epitope reveals a novel mode of peptide presentation.
The binding of DCC-P3 motif and FAK-FAT domain mediates the initial step of netrin-1/DCC signaling for axon attraction.
TL;DR: It is proposed that netrin-1/DCC engagement creates a small cluster of P3/FAT for FAK recruitment close to the cell membrane, which exerts a concerted effect with PIP2 forFAK signaling.
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