메뉴 건너뛰기




Volumn 24, Issue 10, 2003, Pages 528-533

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

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; LEUCINE; LIGAND; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 7; TOLL LIKE RECEPTOR 8; TOLL LIKE RECEPTOR 9; UNCLASSIFIED DRUG;

EID: 0141559415     PISSN: 14714906     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1471-4906(03)00242-4     Document Type: Article
Times cited : (643)

References (35)
  • 1
    • 0036453247 scopus 로고    scopus 로고
    • Plant disease resistance: Commonality and novelty in multicellular innate immunity
    • Fluhr R., Kaplan-Levy R.N. Plant disease resistance: commonality and novelty in multicellular innate immunity. Curr. Top. Microbiol. Immunol. 270:2002;23-46.
    • (2002) Curr. Top. Microbiol. Immunol. , vol.270 , pp. 23-46
    • Fluhr, R.1    Kaplan-Levy, R.N.2
  • 2
    • 0012929728 scopus 로고    scopus 로고
    • Toll-like receptors
    • Takeda K., et al. Toll-like receptors. Annu. Rev. Immunol. 21:2003;335-376.
    • (2003) Annu. Rev. Immunol. , vol.21 , pp. 335-376
    • Takeda, K.1
  • 3
    • 0036839577 scopus 로고    scopus 로고
    • Endogenous ligands of Toll-like receptors: Implications for regulating inflammatory and immune responses
    • Beg A.A. Endogenous ligands of Toll-like receptors: implications for regulating inflammatory and immune responses. Trends Immunol. 23:2002;509-512.
    • (2002) Trends Immunol. , vol.23 , pp. 509-512
    • Beg, A.A.1
  • 4
    • 0037317763 scopus 로고    scopus 로고
    • Innate immune sensing and its roots: The story of endotoxin
    • Beutler B., Rietschel E.T. Innate immune sensing and its roots: the story of endotoxin. Nat. Rev. Immunol. 3:2003;169-176.
    • (2003) Nat. Rev. Immunol. , vol.3 , pp. 169-176
    • Beutler, B.1    Rietschel, E.T.2
  • 6
    • 0037033073 scopus 로고    scopus 로고
    • Lipopolysaccharide rapidly traffics to and from the Golgi apparatus with the Toll-like receptor 4-MD-2-CD14 complex in a process that is distinct from the initiation of signal transduction
    • Latz E., et al. Lipopolysaccharide rapidly traffics to and from the Golgi apparatus with the Toll-like receptor 4-MD-2-CD14 complex in a process that is distinct from the initiation of signal transduction. J. Biol. Chem. 277:2002;47834-47843.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47834-47843
    • Latz, E.1
  • 7
    • 0037604765 scopus 로고    scopus 로고
    • Induction of macrophage nitric oxide production by gram-negative flagellin involves signaling via heteromeric Toll-like receptor 5/Toll-like receptor 4 complexes
    • Mizel S.B., et al. Induction of macrophage nitric oxide production by gram-negative flagellin involves signaling via heteromeric Toll-like receptor 5/Toll-like receptor 4 complexes. J. Immunol. 170:2003;6217-6223.
    • (2003) J. Immunol. , vol.170 , pp. 6217-6223
    • Mizel, S.B.1
  • 8
    • 0036232737 scopus 로고    scopus 로고
    • Toll-like receptor 1 inhibits Toll-like receptor 4 signaling in endothelial cells
    • Spitzer J.H., et al. Toll-like receptor 1 inhibits Toll-like receptor 4 signaling in endothelial cells. Eur. J. Immunol. 32:2002;1182-1187.
    • (2002) Eur. J. Immunol. , vol.32 , pp. 1182-1187
    • Spitzer, J.H.1
  • 9
    • 0037505362 scopus 로고    scopus 로고
    • The Toll-IL-1 receptor adaptor family grows to five members
    • O'Neill L.A., et al. The Toll-IL-1 receptor adaptor family grows to five members. Trends Immunol. 24:2003;286-289.
    • (2003) Trends Immunol. , vol.24 , pp. 286-289
    • O'Neill, L.A.1
  • 10
    • 0035692811 scopus 로고    scopus 로고
    • The leucine-rich repeat as a protein recognition motif
    • Kobe B., Kajava A.V. The leucine-rich repeat as a protein recognition motif. Curr. Opin. Struct. Biol. 11:2001;725-732.
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 725-732
    • Kobe, B.1    Kajava, A.V.2
  • 11
    • 0037119003 scopus 로고    scopus 로고
    • Structures of glycoprotein Ibα and its complex with von Willebrand factor A1 domain
    • Huizinga E.G., et al. Structures of glycoprotein Ibα and its complex with von Willebrand factor A1 domain. Science. 297:2002;1176-1179.
    • (2002) Science , vol.297 , pp. 1176-1179
    • Huizinga, E.G.1
  • 12
    • 0035965120 scopus 로고    scopus 로고
    • Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain
    • Schubert W.D., et al. Internalins from the human pathogen Listeria monocytogenes combine three distinct folds into a contiguous internalin domain. J. Mol. Biol. 312:2001;783-794.
    • (2001) J. Mol. Biol. , vol.312 , pp. 783-794
    • Schubert, W.D.1
  • 13
    • 0037074015 scopus 로고    scopus 로고
    • Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin
    • Schubert W.D., et al. Structure of internalin, a major invasion protein of Listeria monocytogenes, in complex with its human receptor E-cadherin. Cell. 111:2002;825-836.
    • (2002) Cell , vol.111 , pp. 825-836
    • Schubert, W.D.1
  • 14
    • 0038325765 scopus 로고    scopus 로고
    • Structure of the Nogo receptor ectodomain: A recognition module implicated in myelin inhibition
    • He X.L., et al. Structure of the Nogo receptor ectodomain: a recognition module implicated in myelin inhibition. Neuron. 38:2003;177-185.
    • (2003) Neuron , vol.38 , pp. 177-185
    • He, X.L.1
  • 15
    • 0036232188 scopus 로고    scopus 로고
    • Assessment of the ability to model proteins with leucine-rich repeats in light of the latest structural information
    • Kajava A.V., Kobe B. Assessment of the ability to model proteins with leucine-rich repeats in light of the latest structural information. Protein Sci. 11:2002;1082-1090.
    • (2002) Protein Sci. , vol.11 , pp. 1082-1090
    • Kajava, A.V.1    Kobe, B.2
  • 16
    • 0013655342 scopus 로고
    • Periodicity of leucine and tandem repetition of a 24-amino acid segment in the primary structure of leucine-rich α2-glycoprotein of human serum
    • Takahashi N., et al. Periodicity of leucine and tandem repetition of a 24-amino acid segment in the primary structure of leucine-rich α2-glycoprotein of human serum. Proc. Natl. Acad. Sci. U. S. A. 82:1985;1906-1910.
    • (1985) Proc. Natl. Acad. Sci. U. S. A. , vol.82 , pp. 1906-1910
    • Takahashi, N.1
  • 17
    • 0030437795 scopus 로고    scopus 로고
    • Structural and functional diversity in the leucine-rich repeat family of proteins
    • Buchanan S.G., Gay N.J. Structural and functional diversity in the leucine-rich repeat family of proteins. Prog. Biophys. Mol. Biol. 65:1996;1-44.
    • (1996) Prog. Biophys. Mol. Biol. , vol.65 , pp. 1-44
    • Buchanan, S.G.1    Gay, N.J.2
  • 18
    • 0027718173 scopus 로고
    • Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats
    • Kobe B., Deisenhofer J. Crystal structure of porcine ribonuclease inhibitor, a protein with leucine-rich repeats. Nature. 366:1993;751-756.
    • (1993) Nature , vol.366 , pp. 751-756
    • Kobe, B.1    Deisenhofer, J.2
  • 19
    • 0037144544 scopus 로고    scopus 로고
    • Crystal structure of the platelet glycoprotein Ib(α) N-terminal domain reveals an unmasking mechanism for receptor activation
    • Uff S., et al. Crystal structure of the platelet glycoprotein Ib(α) N-terminal domain reveals an unmasking mechanism for receptor activation. J. Biol. Chem. 277:2002;35657-35663.
    • (2002) J. Biol. Chem. , vol.277 , pp. 35657-35663
    • Uff, S.1
  • 20
    • 0030596012 scopus 로고    scopus 로고
    • Mechanism of ribonuclease inhibition by ribonuclease inhibitor protein based on the crystal structure of its complex with ribonuclease A
    • Kobe B., Deisenhofer J. Mechanism of ribonuclease inhibition by ribonuclease inhibitor protein based on the crystal structure of its complex with ribonuclease A. J. Mol. Biol. 264:1996;1028-1043.
    • (1996) J. Mol. Biol. , vol.264 , pp. 1028-1043
    • Kobe, B.1    Deisenhofer, J.2
  • 21
    • 0030864496 scopus 로고    scopus 로고
    • Molecular recognition of human angiogenin by placental ribonuclease inhibitor - an X-ray crystallographic study at 2.0 Å resolution
    • Papageorgiou A.C., et al. Molecular recognition of human angiogenin by placental ribonuclease inhibitor - an X-ray crystallographic study at 2.0 Å resolution. EMBO J. 16:1997;5162-5177.
    • (1997) EMBO J. , vol.16 , pp. 5162-5177
    • Papageorgiou, A.C.1
  • 22
    • 0037033983 scopus 로고    scopus 로고
    • RanGAP mediates GTP hydrolysis without an arginine finger
    • Seewald M.J., et al. RanGAP mediates GTP hydrolysis without an arginine finger. Nature. 415:2002;662-666.
    • (2002) Nature , vol.415 , pp. 662-666
    • Seewald, M.J.1
  • 23
    • 0035976968 scopus 로고    scopus 로고
    • Identification and characterization of the DNA binding domain of CpG-binding protein
    • Lee J.H., et al. Identification and characterization of the DNA binding domain of CpG-binding protein. J. Biol. Chem. 276:2001;44669-44676.
    • (2001) J. Biol. Chem. , vol.276 , pp. 44669-44676
    • Lee, J.H.1
  • 24
    • 0037289001 scopus 로고    scopus 로고
    • Single-nucleotide polymorphisms in the Toll-like receptor 9 gene (TLR9): Frequencies, pairwise linkage disequilibrium, and haplotypes in three U.S. ethnic groups and exploratory case-control disease association studies
    • Lazarus R., et al. Single-nucleotide polymorphisms in the Toll-like receptor 9 gene (TLR9): frequencies, pairwise linkage disequilibrium, and haplotypes in three U.S. ethnic groups and exploratory case-control disease association studies. Genomics. 81:2003;85-91.
    • (2003) Genomics , vol.81 , pp. 85-91
    • Lazarus, R.1
  • 25
    • 0038607406 scopus 로고    scopus 로고
    • Identification of a sequence in human Toll-like receptor 5 required for the binding of gram-negative flagellin
    • Mizel S.B., et al. Identification of a sequence in human Toll-like receptor 5 required for the binding of gram-negative flagellin. J. Biol. Chem. 278:2003;23624-23629.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23624-23629
    • Mizel, S.B.1
  • 26
    • 0036245203 scopus 로고    scopus 로고
    • Innate immune recognition of lipopolysaccharide by endothelial cells
    • Henneke P., Golenbock D.T. Innate immune recognition of lipopolysaccharide by endothelial cells. Crit. Care Med. 30:2002;S207-S213.
    • (2002) Crit. Care Med. , vol.30
    • Henneke, P.1    Golenbock, D.T.2
  • 27
    • 0034306119 scopus 로고    scopus 로고
    • When protein folding is simplified to protein coiling: The continuum of solenoid protein structures
    • Kobe B., Kajava A.V. When protein folding is simplified to protein coiling: the continuum of solenoid protein structures. Trends Biochem. Sci. 25:2000;509-515.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 509-515
    • Kobe, B.1    Kajava, A.V.2
  • 28
    • 0034084438 scopus 로고    scopus 로고
    • TLR4 mutations are associated with endotoxin hyporesponsiveness in humans
    • Arbour N.C., et al. TLR4 mutations are associated with endotoxin hyporesponsiveness in humans. Nat. Genet. 25:2000;187-191.
    • (2000) Nat. Genet. , vol.25 , pp. 187-191
    • Arbour, N.C.1
  • 29
    • 0037866985 scopus 로고    scopus 로고
    • Monocytes heterozygous for the Asp299Gly and Thr399Ile mutations in the Toll-like receptor 4 gene show no deficit in lipopolysaccharide signalling
    • Erridge C., et al. Monocytes heterozygous for the Asp299Gly and Thr399Ile mutations in the Toll-like receptor 4 gene show no deficit in lipopolysaccharide signalling. J. Exp. Med. 197:2003;1787-1791.
    • (2003) J. Exp. Med. , vol.197 , pp. 1787-1791
    • Erridge, C.1
  • 30
    • 0036222620 scopus 로고    scopus 로고
    • Human Toll-like receptor 4 recognizes host-specific LPS modifications
    • Hajjar A.M., et al. Human Toll-like receptor 4 recognizes host-specific LPS modifications. Nat. Immunol. 3:2002;354-359.
    • (2002) Nat. Immunol. , vol.3 , pp. 354-359
    • Hajjar, A.M.1
  • 31
    • 0032983238 scopus 로고    scopus 로고
    • Lipopolysaccharide (LPS)-binding synthetic peptides derived from serum amyloid P component neutralize LPS
    • de Haas C.J., et al. Lipopolysaccharide (LPS)-binding synthetic peptides derived from serum amyloid P component neutralize LPS. Infect. Immun. 67:1999;2790-2796.
    • (1999) Infect. Immun. , vol.67 , pp. 2790-2796
    • De Haas, C.J.1
  • 32
    • 0025804653 scopus 로고
    • Dominant and recessive mutations define functional domains of Toll, a transmembrane protein required for dorsal-ventral polarity in the Drosophila embryo
    • Schneider D.S., et al. Dominant and recessive mutations define functional domains of Toll, a transmembrane protein required for dorsal-ventral polarity in the Drosophila embryo. Genes Dev. 5:1991;797-807.
    • (1991) Genes Dev. , vol.5 , pp. 797-807
    • Schneider, D.S.1
  • 33
    • 0028080261 scopus 로고
    • The leucine-rich repeat: A versatile binding motif
    • Kobe B., Deisenhofer J. The leucine-rich repeat: a versatile binding motif. Trends Biochem. Sci. 19:1994;415-421.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 415-421
    • Kobe, B.1    Deisenhofer, J.2
  • 35
    • 0034597766 scopus 로고    scopus 로고
    • Structural basis for signal transduction by Toll/interleukin-1 receptor domains
    • Xu Y., et al. Structural basis for signal transduction by Toll/interleukin-1 receptor domains. Nature. 408:2000;111-115.
    • (2000) Nature , vol.408 , pp. 111-115
    • Xu, Y.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.