Leucine-rich repeats and pathogen recognition in Toll-like receptors.

By J. Bell, G. Mullen, C. Leifer, A. Mazzoni, D. Davies, D. Segal. Trends in immunology, 2003

795 citations recorded by the source corpus.

Subfields: Epidemiology, Immunology, Microbiology

View Paper: https://www.semanticscholar.org/paper/a5df4847af137c0ca26cd29d408ac4f374a8c063

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In Epidemiology

1. Shizuo Akira
2. K. Takeda
3. S. Dinesh-Kumar
4. P. Murray
5. Michael Schiff
6. W. Strober
7. R. Medzhitov
8. Taro Kawai

In Immunology

1. Shizuo Akira
2. K. Takeda
3. Misako Matsumoto
4. Tsukasa Seya
5. W. Strober
6. P. Murray
7. A. Kitani
8. David Mackey

In Microbiology

1. Shizuo Akira
2. K. Takeda
3. David Mackey
4. A. Bent
5. R. Medzhitov

Citations in the corpus

• Signalling pathways and molecular interactions of NOD1 and NOD2 (2006, background): “However, it should be noted that, as is the case for activation of most TLRs by their respective ligand”
• TLR3: interferon induction by double-stranded RNA including poly(I:C). (2008, background): “Human TLR3 consists of an extracellular domain containing 23 leucine rich repeats (LRRs) and N- and C-terminal flanking regions, the transmembrane domain, and the intracellular TIR domain [20].”
• The Structural Biology of Toll-Like Receptors (2011, background): “However, their amino acid sequences suggest that the structures of TLRs 7–9 ECDs are markedly different from TLR3 (Bell et al., 2003).”
• Somatic diversification of variable lymphocyte receptors in the agnathan sea lamprey (2004, background): “1f ), resembling the model predicted for Toll-like receptor (TLR) ectodomain”
• Elicitors, effectors, and R genes: the new paradigm and a lifetime supply of questions. (2007, background): “LRR domains are also found in many other proteins in the biological kingdom, and often control ligand binding or protein-protein interaction (17, 96).”
• Plant NBS-LRR proteins: adaptable guards (2006, background): “different types of dimers have been observed, involving interactions of either their concave surfaces [35] or their convex surfaces [36,37], or by concatenation involving an antiparallel -sheet at the interface [38].”
• Hydrophobicity: an ancient damage-associated molecular pattern that initiates innate immune responses (2004, background): “1 ), and this promiscuity has puzzled those who work on the”
• Toll-like receptor signalling (2004, background): “Each repeat consists of 24–29 amino acids and contains the leucine-rich sequence XLXXLXLXX, and another conserved sequence XOXXOX 4 FXXLX (Ref”
• A Novel Role for the TIR Domain in Association with Pathogen-Derived Elicitors (2007, background): “]. Thus, data suggest that some R proteins may indirectly recognize Avr proteins through other host proteins. This mode of activation is in contrast to mammalian TLR function in which TLRs directly recognize pathogen-associated molecular patterns (PAMPs) through their extracellular LRR domains [”