Structural Basis of Toll-Like Receptor 3 Signaling with Double-Stranded RNA

By Lin Liu, I. Botos, Yan Wang, J. Leonard, J. Shiloach, D. Segal, D. Davies. Science, 2008

737 citations recorded by the source corpus.

View Paper: https://www.semanticscholar.org/paper/7e16b8f67fa0d3caa8ff4ff5cdf8d64cba4d1e63

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

In Microbiology

Citations in the corpus

DAMPening Inflammation by Modulating TLR Signalling (2010, background): “One structure shows that TLR3 interacts with hydrophilic double-stranded RNA (dsRNA) via surfaceexposed sites [50].”
Pattern recognition receptors in health and diseases (2021, background): “It also interacts with TLR1–TLR2 in the same binding pocket as typical lipopeptide ligand.64 Crystal structure analysis revealed that double-stranded RNA (dsRNA) binds to the LRR domains of the N-terminus and Cterminus of TLR3.”
Molecular Basis of NF-κB Signaling (2013, background): “To date, several structures of the extracellular domain of TLRs bound to a ligand have been solved and reveal a common overall structure (45, 49, 67, 90, 130).”
A cell biological view of Toll-like receptor function: regulation through compartmentalization (2009, background): “The molecular basis of such diverse ligand binding remains poorly understood, although the elucidation of several recent structures of ligand–receptor complexes suggest that not all TLRs use the same ligand-binding interfac”
The Structural Biology of Toll-Like Receptors (2011, background): “The TLR-ECDs also contain structures that cap the N and C-terminal ends known as the LRR-NT and LRR-CT motifs, respectively (Figure 2).”
The inflammasomes: guardians of the body. (2009, background): “Doublestranded RNA and lipopeptides have recently been shown to bind TLR3 and TLR1/TLR2 complexes, respectively, whereas LPS-induced TLR4 activation is presumed to be indirect and to involve binding of LPS to MD2 (22, 23).”
Pathogen Recognition and Inflammatory Signaling in Innate Immune Defenses (2009, background): “directly bind to triacetylated lipopeptides, double-stranded RNA (dsRNA), and CpG DNA, respectively (159, 202, 216),”
Pathogen Recognition by the Innate Immune System (2011, background): “Furthermore, co-crystallization of TLR3 with dsRNA shows that the recognition domain of TLR3 has a horseshoe-shaped solenoid structure and that dsRNA binds to the lateral convex surface of the TLR3 ectodomain [15].”
Co-operation of TLR4 and raft proteins in LPS-induced pro-inflammatory signaling (2014, background): “It is a single-spanning transmembrane protein with an extracellular domain composed of 22 leucine-rich repeats conferring a horseshoe-like shape on the protein, found typical for TLRs by crystallography studies [6–8].”
Structural insights into RNA recognition by RIG-I (2011, neutral): “TLR3 is crescent-shaped molecule consisting of rigid leucine-rich repeats that bind to RNA and form obligate dimers (Liu et al., 2008).”
The interleukin‐1 receptor/Toll‐like receptor superfamily: 10 years of progress (2008, background): “Finally, a structure for the TLR3 dimer in complex with double-stranded RNA has been solved (65).”