메뉴 건너뛰기




Volumn 2, Issue 1, 2006, Pages 47-52

Allosteric control of an ionotropic glutamate receptor with an optical switch

Author keywords

[No Author keywords available]

Indexed keywords

AZOBENZENE; ION CHANNEL; IONOTROPIC RECEPTOR; MOLECULAR MOTOR; AZO COMPOUND; CYSTEINE; GLUTAMATE RECEPTOR; LIGAND; LIGLUR RECEPTOR; UBIQUITIN;

EID: 33645218213     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio756     Document Type: Article
Times cited : (504)

References (30)
  • 1
    • 0004240038 scopus 로고    scopus 로고
    • Feringa, B.L. Ed. Wiley-VCH, Weinheim, Germany
    • Feringa, B.L. Ed. Molecular Switches. (Wiley-VCH, Weinheim, Germany, 2001).
    • (2001) Molecular Switches
  • 3
    • 0018860646 scopus 로고
    • Covalently bound photoisomerizable agonist - Comparison with reversibly bound agonists at electrophorus electroplaques
    • Lester, H.A., Krouse, M.E., Nass, M.M., Wassermann, N.H. & Erlanger, B.F. Covalently bound photoisomerizable agonist - Comparison with reversibly bound agonists at electrophorus electroplaques. J. Gen. Physiol. 75, 207-232 (1980).
    • (1980) J. Gen. Physiol. , vol.75 , pp. 207-232
    • Lester, H.A.1    Krouse, M.E.2    Nass, M.M.3    Wassermann, N.H.4    Erlanger, B.F.5
  • 4
    • 23044503853 scopus 로고    scopus 로고
    • A light-actuated nanovalve derived from a channel protein
    • Kocer, A., Walko, M., Meijberg, W. & Feringa, B.L. A light-actuated nanovalve derived from a channel protein. Science 309, 755-758 (2005).
    • (2005) Science , vol.309 , pp. 755-758
    • Kocer, A.1    Walko, M.2    Meijberg, W.3    Feringa, B.L.4
  • 5
    • 12344309164 scopus 로고    scopus 로고
    • Light-activated ion channels for remote control of neuronal firing
    • Banghart, M., Borges, K., Isacoff, E., Trauner, D. & Kramer, R.H. Light-activated ion channels for remote control of neuronal firing. Nat. Neurosci. 7, 1381-1386 (2004).
    • (2004) Nat. Neurosci. , vol.7 , pp. 1381-1386
    • Banghart, M.1    Borges, K.2    Isacoff, E.3    Trauner, D.4    Kramer, R.H.5
  • 6
    • 0032032919 scopus 로고    scopus 로고
    • The macro- And microarchitectures of the ligand-binding domain of glutamate receptors
    • Paas, Y. The macro- and microarchitectures of the ligand-binding domain of glutamate receptors. Trends Neurosci. 21, 117-125 (1998).
    • (1998) Trends Neurosci. , vol.21 , pp. 117-125
    • Paas, Y.1
  • 8
    • 0038662595 scopus 로고    scopus 로고
    • Evolution, structure, and activation mechanism of family 3/C G-protein-coupled receptors
    • Pin, J.P., Galvez, T. & Prezeau, L. Evolution, structure, and activation mechanism of family 3/C G-protein-coupled receptors. Pharmacol. Ther. 98, 325-354 (2003).
    • (2003) Pharmacol. Ther. , vol.98 , pp. 325-354
    • Pin, J.P.1    Galvez, T.2    Prezeau, L.3
  • 9
    • 33646521228 scopus 로고    scopus 로고
    • Kandel, E.R., Schwartz, J.H. & Jessell, T.M. Eds. McGraw-Hill, New York
    • Kandel, E.R., Schwartz, J.H. & Jessell, T.M. Eds. Principles of Neural Science Ed. 4. (McGraw-Hill, New York, 2000).
    • (2000) Principles of Neural Science Ed. 4.
  • 11
    • 0033636314 scopus 로고    scopus 로고
    • Mechanisms for activation and antagonism of an AMPA-Sensitive glutamate receptor: Crystal structures of the GluR2 ligand binding core
    • Armstrong, N. & Gouaux, E. Mechanisms for activation and antagonism of an AMPA-Sensitive glutamate receptor: Crystal structures of the GluR2 ligand binding core. Neuron 28, 165-181 (2000).
    • (2000) Neuron , vol.28 , pp. 165-181
    • Armstrong, N.1    Gouaux, E.2
  • 12
    • 13844266202 scopus 로고    scopus 로고
    • Crystal structures of the GluR5 and GluR6 ligand binding cores: Molecular mechanisms underlying kainate receptor selectivity
    • Mayer, M.L. Crystal structures of the GluR5 and GluR6 ligand binding cores: Molecular mechanisms underlying kainate receptor selectivity. Neuron 45, 539-552 (2005).
    • (2005) Neuron , vol.45 , pp. 539-552
    • Mayer, M.L.1
  • 13
    • 13444281913 scopus 로고    scopus 로고
    • Structure of the kainate receptor subunit GluR6 agonist-binding domain complexed with domoic acid
    • Nanao, M.H., Green, T., Stern-Bach, Y., Heinemann, S.F. & Choe, S. Structure of the kainate receptor subunit GluR6 agonist-binding domain complexed with domoic acid. Proc. Natl. Acad. Sci. USA 102, 1708-1713 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 1708-1713
    • Nanao, M.H.1    Green, T.2    Stern-Bach, Y.3    Heinemann, S.F.4    Choe, S.5
  • 14
    • 0037261506 scopus 로고    scopus 로고
    • Stereostructure-activity studies on agonists, at the AMPA and kainate subtypes of ionotropic glutamate receptors
    • Johansen, T.N., Greenwood, J.R., Frydenvang, K., Madsen, U. & Krogsgaard-Larsen, P. Stereostructure-activity studies on agonists, at the AMPA and kainate subtypes of ionotropic glutamate receptors. Chirality 15, 167-179 (2003).
    • (2003) Chirality , vol.15 , pp. 167-179
    • Johansen, T.N.1    Greenwood, J.R.2    Frydenvang, K.3    Madsen, U.4    Krogsgaard-Larsen, P.5
  • 15
    • 18344416965 scopus 로고    scopus 로고
    • 4-alkyl- And 4-cinnamylglutamic acid analogues are potent GluR5 kainate receptor agonists
    • Pedregal, C. et al. 4-alkyl- and 4-cinnamylglutamic acid analogues are potent GluR5 kainate receptor agonists. J. Med. Chem. 43, 1958-1968 (2000).
    • (2000) J. Med. Chem. , vol.43 , pp. 1958-1968
    • Pedregal, C.1
  • 16
    • 0027339892 scopus 로고
    • Determinants of Ca2+ permeability in both TM1 and TM2 of high-affinity kainate receptor channels - Diversity by RNA editing
    • Kohler, M., Burnashev, N., Sakmann, B. & Seeburg, P.H. Determinants of Ca2+ permeability in both TM1 and TM2 of high-affinity kainate receptor channels - diversity by RNA editing. Neuron 10, 491-500 (1993).
    • (1993) Neuron , vol.10 , pp. 491-500
    • Kohler, M.1    Burnashev, N.2    Sakmann, B.3    Seeburg, P.H.4
  • 17
    • 0021895138 scopus 로고
    • A new generation of Ca-2+ indicators with greatly improved fluorescence properties
    • Grynkiewicz, G., Poenie, M. & Tsien, R.Y. A new generation of Ca-2+ indicators with greatly improved fluorescence properties. J. Biol. Chem. 260, 3440-3450 (1985).
    • (1985) J. Biol. Chem. , vol.260 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 19
    • 0043033172 scopus 로고    scopus 로고
    • Structural basis for partial agonist action at ionotropic glutamate receptors
    • Jin, R.S., Banke, T.G., Mayer, M.L., Traynelis, S.F. & Gouaux, E. Structural basis for partial agonist action at ionotropic glutamate receptors. Nat. Neurosci. 6, 803-810 (2003).
    • (2003) Nat. Neurosci. , vol.6 , pp. 803-810
    • Jin, R.S.1    Banke, T.G.2    Mayer, M.L.3    Traynelis, S.F.4    Gouaux, E.5
  • 21
    • 0034718925 scopus 로고    scopus 로고
    • Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor
    • Kunishima, N. et al. Structural basis of glutamate recognition by a dimeric metabotropic glutamate receptor. Nature 407, 971-977 (2000).
    • (2000) Nature , vol.407 , pp. 971-977
    • Kunishima, N.1
  • 22
    • 0038037859 scopus 로고    scopus 로고
    • Mechanisms of activation, inhibition and specificity: Crystal structures of the NMDA receptor NR1 ligand-binding core
    • Furukawa, H. & Gouaux, E. Mechanisms of activation, inhibition and specificity: crystal structures of the NMDA receptor NR1 ligand-binding core. EMBO J. 22, 2873-2885 (2003).
    • (2003) EMBO J. , vol.22 , pp. 2873-2885
    • Furukawa, H.1    Gouaux, E.2
  • 23
    • 0037203773 scopus 로고    scopus 로고
    • Structural identification of a bacterial quorum-sensing signal containing boron
    • Chen, X. et al. Structural identification of a bacterial quorum-sensing signal containing boron. Nature 415, 545-549 (2002).
    • (2002) Nature , vol.415 , pp. 545-549
    • Chen, X.1
  • 24
    • 4444247468 scopus 로고    scopus 로고
    • Functional engineered channels and pores
    • Bayley, H. & Jayasinghe, L. Functional engineered channels and pores. Mol. Membr. Biol. 21, 209-220 (2004).
    • (2004) Mol. Membr. Biol. , vol.21 , pp. 209-220
    • Bayley, H.1    Jayasinghe, L.2
  • 25
    • 4143115810 scopus 로고    scopus 로고
    • Periplasmic binding proteins: A versatile superfamily for protein engineering
    • Dwyer, M.A. & Hellinga, H.W. Periplasmic binding proteins: a versatile superfamily for protein engineering. Curr. Opin. Struct. Biol. 14, 495-504 (2004).
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 495-504
    • Dwyer, M.A.1    Hellinga, H.W.2
  • 26
    • 0035743527 scopus 로고    scopus 로고
    • Molecular and biomolecular optoelectronics
    • Willner, I. & Willner, B. Molecular and biomolecular optoelectronics. Pure Appl. Chem. 73, 535-542 (2001).
    • (2001) Pure Appl. Chem. , vol.73 , pp. 535-542
    • Willner, I.1    Willner, B.2
  • 28
    • 0030959560 scopus 로고    scopus 로고
    • Activation and desensitization of hippocampal kainate receptors
    • Wilding, T.J. & Huettner, J.E. Activation and desensitization of hippocampal kainate receptors. J. Neurosci. 17, 2713-2721 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 2713-2721
    • Wilding, T.J.1    Huettner, J.E.2
  • 29
    • 0027715150 scopus 로고
    • Selective modulation of desensitization at AMPA versus kainate receptors by cyclothiazide and concanavalin-A
    • Partin, K.M., Patneau, D.K., Winters, C.A., Mayer, M.L. & Buonanno, A. Selective modulation of desensitization at AMPA versus kainate receptors by cyclothiazide and concanavalin-A. Neuron 11, 1069-1082 (1993).
    • (1993) Neuron , vol.11 , pp. 1069-1082
    • Partin, K.M.1    Patneau, D.K.2    Winters, C.A.3    Mayer, M.L.4    Buonanno, A.5
  • 30
    • 0027301896 scopus 로고
    • Stereoselective reactions of lithium enolates derived from N-Boc protected pyroglutamic esters
    • Ezquerra, J. et al. Stereoselective reactions of lithium enolates derived from N-Boc protected pyroglutamic esters. Tetrahedron 49, 8665-8678 (1993).
    • (1993) Tetrahedron , vol.49 , pp. 8665-8678
    • Ezquerra, J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.