TLR4/MD-2 activation by a synthetic agonist with no similarity to LPS

Structurally disparate molecules reportedly engage and activate Toll-like receptor (TLR) 4 and other TLRs, yet the interactions that mediate binding and activation by dissimilar ligands remain unknown. We describe Neoseptins, chemically synthesized peptidomimetics that bear no structural similarity...

Full description

Saved in:

Bibliographic Details
Published in:	Proceedings of the National Academy of Sciences - PNAS Vol. 113; no. 7; pp. E884 - E893
Main Authors:	Wang, Ying, Su, Lijing, Morin, Matthew D, Jones, Brian T, Whitby, Landon R, Surakattula, Murali M R P, Huang, Hua, Shi, Hexin, Choi, Jin Huk, Wang, Kuan-wen, Moresco, Eva Marie Y, Berger, Michael, Zhan, Xiaoming, Zhang, Hong, Boger, Dale L, Beutler, Bruce
Format:	Journal Article
Language:	English
Published:	United States 16.02.2016
Subjects:	Animals Lipopolysaccharides - pharmacology Lymphocyte Antigen 96 - agonists Mice Mice, Inbred C57BL Mice, Transgenic Mitogen-Activated Protein Kinases - metabolism NF-kappa B - metabolism Peptidomimetics - pharmacology Protein-Serine-Threonine Kinases - metabolism Signal Transduction Toll-Like Receptor 4 - agonists crystal structure proinflammatory response innate immunity peptidomimetic compounds neoseptins
ISSN:	1091-6490
Online Access:	Get more information
Tags:	Add Tag No Tags, Be the first to tag this record!

Be the first to leave a comment!