메뉴 건너뛰기




Volumn 337, Issue 3, 2005, Pages 998-1005

Visualization of the trimeric P2X2 receptor with a crown-capped extracellular domain

Author keywords

ATP; Electron microscopy; Ion channel; Negative staining; P2X receptor; Purinergic; Single particle analysis

Indexed keywords

PURINE P2X2 RECEPTOR; MULTIPROTEIN COMPLEX; PROTEIN SUBUNIT; PURINE P2 RECEPTOR;

EID: 26844438833     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.09.141     Document Type: Article
Times cited : (40)

References (42)
  • 1
    • 0036788971 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors
    • R.A. North Molecular physiology of P2X receptors Physiol. Rev. 82 2002 1013 1067
    • (2002) Physiol. Rev. , vol.82 , pp. 1013-1067
    • North, R.A.1
  • 2
    • 0026648857 scopus 로고
    • ATP receptor-mediated synaptic currents in the central nervous system
    • F.A. Edwards, A.J. Gibb, and D. Colquhoun ATP receptor-mediated synaptic currents in the central nervous system Nature 359 1992 144 147
    • (1992) Nature , vol.359 , pp. 144-147
    • Edwards, F.A.1    Gibb, A.J.2    Colquhoun, D.3
  • 3
    • 0026771094 scopus 로고
    • ATP mediates fast synaptic transmission in mammalian neurons
    • R.J. Evans, V. Derkach, and A. Surprenant ATP mediates fast synaptic transmission in mammalian neurons Nature 357 1992 503 505
    • (1992) Nature , vol.357 , pp. 503-505
    • Evans, R.J.1    Derkach, V.2    Surprenant, A.3
  • 4
    • 0030671405 scopus 로고    scopus 로고
    • Activation of ATP P2X receptors elicits glutamate release from sensory neuron synapses
    • J.G. Gu, and A.B. MacDermott Activation of ATP P2X receptors elicits glutamate release from sensory neuron synapses Nature 389 1997 749 753
    • (1997) Nature , vol.389 , pp. 749-753
    • Gu, J.G.1    MacDermott, A.B.2
  • 5
    • 0031848216 scopus 로고    scopus 로고
    • ATP receptor-mediated enhancement of fast excitatory neurotransmitter release in the brain
    • B.S. Khakh, and G. Henderson ATP receptor-mediated enhancement of fast excitatory neurotransmitter release in the brain Mol. Pharmacol. 54 1998 372 378
    • (1998) Mol. Pharmacol. , vol.54 , pp. 372-378
    • Khakh, B.S.1    Henderson, G.2
  • 6
    • 0035253034 scopus 로고    scopus 로고
    • Distinct modulation of evoked and spontaneous EPSCs by purinoceptors in the nucleus tractus solitarii of the rat
    • F. Kato, and E. Shigetomi Distinct modulation of evoked and spontaneous EPSCs by purinoceptors in the nucleus tractus solitarii of the rat J. Physiol. 530 2001 469 486
    • (2001) J. Physiol. , vol.530 , pp. 469-486
    • Kato, F.1    Shigetomi, E.2
  • 7
    • 0028025001 scopus 로고
    • New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor
    • A.J. Brake, M.J. Wagenbach, and D. Julius New structural motif for ligand-gated ion channels defined by an ionotropic ATP receptor Nature 371 1994 519 523
    • (1994) Nature , vol.371 , pp. 519-523
    • Brake, A.J.1    Wagenbach, M.J.2    Julius, D.3
  • 8
    • 0028030797 scopus 로고
    • A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP
    • S. Valera, N. Hussy, R.J. Evans, N. Adami, R.A. North, A. Surprenant, and G. Buell A new class of ligand-gated ion channel defined by P2x receptor for extracellular ATP Nature 371 1994 516 519
    • (1994) Nature , vol.371 , pp. 516-519
    • Valera, S.1    Hussy, N.2    Evans, R.J.3    Adami, N.4    North, R.A.5    Surprenant, A.6    Buell, G.7
  • 9
    • 0035107660 scopus 로고    scopus 로고
    • International union of pharmacology. XXIV. Current status of the nomenclature and properties of P2X receptors and their subunits
    • B.S. Khakh, G. Burnstock, C. Kennedy, B.F. King, R.A. North, P. Seguela, M. Voigt, and P.P. Humphrey International union of pharmacology. XXIV. Current status of the nomenclature and properties of P2X receptors and their subunits Pharmacol. Rev. 53 2001 107 118
    • (2001) Pharmacol. Rev. , vol.53 , pp. 107-118
    • Khakh, B.S.1    Burnstock, G.2    Kennedy, C.3    King, B.F.4    North, R.A.5    Seguela, P.6    Voigt, M.7    Humphrey, P.P.8
  • 10
    • 0035287474 scopus 로고    scopus 로고
    • Molecular physiology of P2X receptors and ATP signalling at synapses
    • B.S. Khakh Molecular physiology of P2X receptors and ATP signalling at synapses Nat. Rev. Neurosci. 2 2001 165 174
    • (2001) Nat. Rev. Neurosci. , vol.2 , pp. 165-174
    • Khakh, B.S.1
  • 11
    • 0034602169 scopus 로고    scopus 로고
    • Identification of amino acid residues contributing to the ATP-binding site of a purinergic P2X receptor
    • L.H. Jiang, F. Rassendren, A. Surprenant, and R.A. North Identification of amino acid residues contributing to the ATP-binding site of a purinergic P2X receptor J. Biol. Chem. 275 2000 34190 34196
    • (2000) J. Biol. Chem. , vol.275 , pp. 34190-34196
    • Jiang, L.H.1    Rassendren, F.2    Surprenant, A.3    North, R.A.4
  • 17
    • 0038112088 scopus 로고    scopus 로고
    • Structure and gating mechanism of the acetylcholine receptor pore
    • A. Miyazawa, Y. Fujiyoshi, and N. Unwin Structure and gating mechanism of the acetylcholine receptor pore Nature 423 2003 949 955
    • (2003) Nature , vol.423 , pp. 949-955
    • Miyazawa, A.1    Fujiyoshi, Y.2    Unwin, N.3
  • 18
    • 13444271681 scopus 로고    scopus 로고
    • Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution
    • N. Unwin Refined structure of the nicotinic acetylcholine receptor at 4 Å resolution J. Mol. Biol. 346 2005 967 989
    • (2005) J. Mol. Biol. , vol.346 , pp. 967-989
    • Unwin, N.1
  • 19
    • 7444240214 scopus 로고    scopus 로고
    • The three-dimensional structure of an ionotropic glutamate receptor reveals a dimer-of-dimers assembly
    • W. Tichelaar, M. Safferling, K. Keinanen, H. Stark, and D.R. Madden The three-dimensional structure of an ionotropic glutamate receptor reveals a dimer-of-dimers assembly J. Mol. Biol. 344 2004 435 442
    • (2004) J. Mol. Biol. , vol.344 , pp. 435-442
    • Tichelaar, W.1    Safferling, M.2    Keinanen, K.3    Stark, H.4    Madden, D.R.5
  • 20
    • 13444302564 scopus 로고    scopus 로고
    • Structure and different conformational states of native AMPA receptor complexes
    • T. Nakagawa, Y. Cheng, E. Ramm, M. Sheng, and T. Walz Structure and different conformational states of native AMPA receptor complexes Nature 433 2005 545 549
    • (2005) Nature , vol.433 , pp. 545-549
    • Nakagawa, T.1    Cheng, Y.2    Ramm, E.3    Sheng, M.4    Walz, T.5
  • 21
    • 0442279279 scopus 로고    scopus 로고
    • Structure and function of AMPA receptors
    • E. Gouaux Structure and function of AMPA receptors J. Physiol. 554 2004 249 253
    • (2004) J. Physiol. , vol.554 , pp. 249-253
    • Gouaux, E.1
  • 25
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 26
    • 1942456920 scopus 로고    scopus 로고
    • Auto-accumulation method using simulated annealing enables fully automatic particle pickup completely free from a matching template or learning data
    • T. Ogura, and C. Sato Auto-accumulation method using simulated annealing enables fully automatic particle pickup completely free from a matching template or learning data J. Struct. Biol. 146 2004 344 358
    • (2004) J. Struct. Biol. , vol.146 , pp. 344-358
    • Ogura, T.1    Sato, C.2
  • 27
    • 0035782895 scopus 로고    scopus 로고
    • An automatic particle pickup method using a neural network applicable to low-contrast electron micrographs
    • T. Ogura, and C. Sato An automatic particle pickup method using a neural network applicable to low-contrast electron micrographs J. Struct. Biol. 136 2001 227 238
    • (2001) J. Struct. Biol. , vol.136 , pp. 227-238
    • Ogura, T.1    Sato, C.2
  • 28
    • 0347447277 scopus 로고    scopus 로고
    • Automatic particle pickup method using a neural network has high accuracy by applying an initial weight derived from eigenimages: A new reference free method for single-particle analysis
    • T. Ogura, and C. Sato Automatic particle pickup method using a neural network has high accuracy by applying an initial weight derived from eigenimages: a new reference free method for single-particle analysis J. Struct. Biol. 145 2004 63 75
    • (2004) J. Struct. Biol. , vol.145 , pp. 63-75
    • Ogura, T.1    Sato, C.2
  • 29
    • 0142059303 scopus 로고    scopus 로고
    • Topology representing network enables highly accurate classification of protein images taken by cryo electron-microscope without masking
    • T. Ogura, K. Iwasaki, and C. Sato Topology representing network enables highly accurate classification of protein images taken by cryo electron-microscope without masking J. Struct. Biol. 143 2003 185 200
    • (2003) J. Struct. Biol. , vol.143 , pp. 185-200
    • Ogura, T.1    Iwasaki, K.2    Sato, C.3
  • 31
    • 0019987933 scopus 로고
    • The correlation averaging of a regularly arranged bacterial cell envelope protein
    • W.O. Saxton, and W. Baumeister The correlation averaging of a regularly arranged bacterial cell envelope protein J. Microsc. 127 1982 127 138
    • (1982) J. Microsc. , vol.127 , pp. 127-138
    • Saxton, W.O.1    Baumeister, W.2
  • 34
    • 0031902319 scopus 로고    scopus 로고
    • The sodium channel has four domains surrounding a central pore
    • C. Sato, M. Sato, A. Iwasaki, T. Doi, and A. Engel The sodium channel has four domains surrounding a central pore J. Struct. Biol. 121 1998 314 325
    • (1998) J. Struct. Biol. , vol.121 , pp. 314-325
    • Sato, C.1    Sato, M.2    Iwasaki, A.3    Doi, T.4    Engel, A.5
  • 35
    • 20744449020 scopus 로고    scopus 로고
    • The non-selective cation-permeable channel TRPC3 is a tetrahedron with a cap on the large cytoplasmic end
    • K. Mio, T. Ogura, Y. Hara, Y. Mori, and C. Sato The non-selective cation-permeable channel TRPC3 is a tetrahedron with a cap on the large cytoplasmic end Biochem. Biophys. Res. Commun. 333 2005 768 777
    • (2005) Biochem. Biophys. Res. Commun. , vol.333 , pp. 768-777
    • Mio, K.1    Ogura, T.2    Hara, Y.3    Mori, Y.4    Sato, C.5
  • 36
    • 0035931906 scopus 로고    scopus 로고
    • The voltage-sensitive sodium channel is a bell-shaped molecule with several cavities
    • C. Sato, Y. Ueno, K. Asai, K. Takahashi, M. Sato, A. Engel, and Y. Fujiyoshi The voltage-sensitive sodium channel is a bell-shaped molecule with several cavities Nature 409 2001 1047 1051
    • (2001) Nature , vol.409 , pp. 1047-1051
    • Sato, C.1    Ueno, Y.2    Asai, K.3    Takahashi, K.4    Sato, M.5    Engel, A.6    Fujiyoshi, Y.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.