메뉴 건너뛰기




Volumn 21, Issue 8, 1996, Pages 963-968

Ultraviolet radiation, thiol reagents, and solubilization enhance AMPA receptor binding affinity via a common mechanism

Author keywords

Glutamate receptor; PCMBS; solubilization; thiol; ultraviolet; UV

Indexed keywords

ALPHA AMINO 3 HYDROXY 5 METHYL 4 ISOXAZOLEPROPIONIC ACID; AMPA RECEPTOR; CHLOROMERCURIBENZENESULFONIC ACID; GLUTAMATE RECEPTOR; THIOL DERIVATIVE;

EID: 0029902466     PISSN: 03643190     EISSN: None     Source Type: Journal    
DOI: 10.1007/BF02532347     Document Type: Article
Times cited : (10)

References (30)
  • 1
    • 0026043897 scopus 로고
    • Modulation of the time course of fast EPSCs and glutamate channel kinetics by aniracetam
    • Tang, C.-M., Shi, Q.-Y., Katchman, A., and Lynch, G. 1991. Modulation of the time course of fast EPSCs and glutamate channel kinetics by aniracetam. Science 254:288-290.
    • (1991) Science , vol.254 , pp. 288-290
    • Tang, C.-M.1    Shi, Q.-Y.2    Katchman, A.3    Lynch, G.4
  • 2
    • 0026351573 scopus 로고
    • Modulation of excitatory synaptic transmission by drugs that reduce desensitization
    • Vyklicky, L., Patneau, D. K., and Mayer, M. L. 1991. Modulation of excitatory synaptic transmission by drugs that reduce desensitization. Neuron 7:971-984.
    • (1991) Neuron , vol.7 , pp. 971-984
    • Vyklicky, L.1    Patneau, D.K.2    Mayer, M.L.3
  • 3
    • 0025786139 scopus 로고
    • Aniracetam reduces glutamate receptor desensitization and slows the decay of fast excitatory synaptic currents in the hippocampus
    • Isaacson, J. S., and Nicoll, R. 1991. Aniracetam reduces glutamate receptor desensitization and slows the decay of fast excitatory synaptic currents in the hippocampus. Proc. Natl. Acad. Sci. 88: 10936-10940.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 10936-10940
    • Isaacson, J.S.1    Nicoll, R.2
  • 4
    • 0023160595 scopus 로고
    • 3H]AMPA binding to glutamate receptor subpopulations in rat brain
    • 3H]AMPA binding to glutamate receptor subpopulations in rat brain. Brain. Res. 402:243-254.
    • (1987) Brain. Res. , vol.402 , pp. 243-254
    • Olsen, R.W.1    Szamraj, O.2    Houser, C.R.3
  • 5
    • 0023220868 scopus 로고
    • 3H]-alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) and a filtration assay
    • 3H]-alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid (AMPA) and a filtration assay. Neurochem. Res. 12:775-782.
    • (1987) Neurochem. Res. , vol.12 , pp. 775-782
    • Murphy, D.E.1    Snowhill, E.W.2    Williams, M.3
  • 6
    • 0023705643 scopus 로고
    • 3H]alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid binding to rat telencephalic membranes
    • 3H]alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid binding to rat telencephalic membranes. Molec. Pharmacol. 34:117-123.
    • (1988) Molec. Pharmacol. , vol.34 , pp. 117-123
    • Terramani, T.1    Kessler, M.2    Lynch, G.3    Baudry, M.4
  • 7
    • 0023679750 scopus 로고
    • Chaotropic ions affect the conformation of quisqualate receptors-in rat cortical membranes
    • Honore, T., and Drejer, J. 1988. Chaotropic ions affect the conformation of quisqualate receptors-in rat cortical membranes. J. Neurochem. 51:457-461.
    • (1988) J. Neurochem. , vol.51 , pp. 457-461
    • Honore, T.1    Drejer, J.2
  • 8
    • 0026566892 scopus 로고
    • Evidence that high-and low-affinity AMPA binding sites reflect membrane-dependent states of a single receptor
    • Hall, R. A., Kessler, M., and Lynch, G. 1992. Evidence that high-and low-affinity AMPA binding sites reflect membrane-dependent states of a single receptor. J. Neurochem. 59:1997-2004.
    • (1992) J. Neurochem. , vol.59 , pp. 1997-2004
    • Hall, R.A.1    Kessler, M.2    Lynch, G.3
  • 9
    • 0027332679 scopus 로고
    • 3H]AMPA binding to rat brain membranes: Evidence that receptor desensitization increases agonist affinity
    • 3H]AMPA binding to rat brain membranes: Evidence that receptor desensitization increases agonist affinity. Brain Res. 628:345-348.
    • (1993) Brain Res. , vol.628 , pp. 345-348
    • Hall, R.A.1    Kessler, M.2    Quan, A.3    Ambros-Ingerson, J.4    Lynch, G.5
  • 10
    • 0027930763 scopus 로고
    • Differential subcellular localization of two populations of glutamate/AMPA receptors in the rat telencephalon
    • Standley, S., Irvin, N., and Baudry, M. 1994. Differential subcellular localization of two populations of glutamate/AMPA receptors in the rat telencephalon. Neurochem. Int. 25:287-293.
    • (1994) Neurochem. Int. , vol.25 , pp. 287-293
    • Standley, S.1    Irvin, N.2    Baudry, M.3
  • 11
    • 0027970352 scopus 로고
    • 3H]AMPA binding and western blot studies
    • 3H]AMPA binding and western blot studies. J. Neurochem. 63:1658-1665.
    • (1994) J. Neurochem. , vol.63 , pp. 1658-1665
    • Hall, R.A.1    Bahr, B.A.2
  • 12
    • 0027234701 scopus 로고
    • The molecular biology of mammalian glutamate receptor channels
    • Seeburg, P. 1993. The molecular biology of mammalian glutamate receptor channels. Trends Neurosci. 16:359-365.
    • (1993) Trends Neurosci. , vol.16 , pp. 359-365
    • Seeburg, P.1
  • 15
    • 0026572771 scopus 로고
    • Solubilization and purification of an alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid binding protein from bovine brain
    • Hunter, C., and Wenthold, R. J. 1992. Solubilization and purification of an alpha-amino-3-hydroxy-5-methylisoxazole-4-propionic acid binding protein from bovine brain. J. Neurochem. 58: 1379-1385.
    • (1992) J. Neurochem. , vol.58 , pp. 1379-1385
    • Hunter, C.1    Wenthold, R.J.2
  • 16
    • 0021991131 scopus 로고
    • Complex structure of quisqualate-sensitive glutamate receptors in rat cortex
    • Honore, T., and Nielsen, M. 1985. Complex structure of quisqualate-sensitive glutamate receptors in rat cortex. Neurosci. Lett. 54:27-32.
    • (1985) Neurosci. Lett. , vol.54 , pp. 27-32
    • Honore, T.1    Nielsen, M.2
  • 17
    • 0026636057 scopus 로고
    • 3H]-amino-3-hydroxy-5-methylisoxazole-4-propionate binding sites in chick telencephalon: Effects of high-energy radiation and detergent solubilisation
    • 3H]-amino-3-hydroxy-5-methylisoxazole-4-propionate binding sites in chick telencephalon: Effects of high-energy radiation and detergent solubilisation. J. Neurochem. 58:2030-2036.
    • (1992) J. Neurochem. , vol.58 , pp. 2030-2036
    • Henley, J.M.1    Nielsen, M.2    Barnard, E.A.3
  • 18
    • 0026730133 scopus 로고
    • Functional reconstitution of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptors from rat brain
    • Bahr, B. A., Vodyanoy, V., Hall, R. A., Suppiramaniam, V., Kessler, M., Sumikawa, K., and Lynch, G. 1992. Functional reconstitution of alpha-amino-3-hydroxy-5-methylisoxazole-4-propionate (AMPA) receptors from rat brain. J. Neurochem. 59:1979-1982.
    • (1992) J. Neurochem. , vol.59 , pp. 1979-1982
    • Bahr, B.A.1    Vodyanoy, V.2    Hall, R.A.3    Suppiramaniam, V.4    Kessler, M.5    Sumikawa, K.6    Lynch, G.7
  • 19
    • 0006339343 scopus 로고
    • The chemical modification of proteins by group-specific and site-specific reagents
    • Neurath, Hill, Boeder (eds.)
    • Glazer, A. N. 1976. The chemical modification of proteins by group-specific and site-specific reagents. Pages 1-103 in Neurath, Hill, Boeder (eds.) The Proteins.
    • (1976) The Proteins , pp. 1-103
    • Glazer, A.N.1
  • 20
    • 33845620381 scopus 로고
    • The photochemistry of native proteins
    • London
    • Rideal, E. K., and Roberts, R. 1951. The photochemistry of native proteins. Proc. Royal Soc. (London) 205A:391-408.
    • (1951) Proc. Royal Soc. , vol.205 A , pp. 391-408
    • Rideal, E.K.1    Roberts, R.2
  • 21
    • 0025740935 scopus 로고
    • Crosslinking proteins to nucleic acids by ultraviolet laser irradiation
    • Pashev, I. G., Dimitrov, S. I., and Angelov, D. 1991. Crosslinking proteins to nucleic acids by ultraviolet laser irradiation. Trends Biochem. Sci. 16:323-326.
    • (1991) Trends Biochem. Sci. , vol.16 , pp. 323-326
    • Pashev, I.G.1    Dimitrov, S.I.2    Angelov, D.3
  • 22
    • 0022981653 scopus 로고
    • Specific cleavage of dynein heavy chains by ultraviolet irradiation in the presence of ATP and vanadate
    • Lee-Eiford, A., Ow, R., and Gibbons, L. R. 1986. Specific cleavage of dynein heavy chains by ultraviolet irradiation in the presence of ATP and vanadate. J. Biol. Chem. 261:2337-2342.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2337-2342
    • Lee-Eiford, A.1    Ow, R.2    Gibbons, L.R.3
  • 23
    • 0023490518 scopus 로고
    • Environmental wavelengths of ultraviolet light induce cytoskeletal damage
    • Zamansky, G. B., and Chou, I. N. 1987. Environmental wavelengths of ultraviolet light induce cytoskeletal damage. J. Invest. Dermatol. 89:603-606.
    • (1987) J. Invest. Dermatol. , vol.89 , pp. 603-606
    • Zamansky, G.B.1    Chou, I.N.2
  • 24
    • 0024402680 scopus 로고
    • Ultraviolet irradiation selectively disrupts the gamma-aminobutyric acid/benzodiazepine receptor-linked chloride ionophore
    • Evoniuk, G., Moody, E. J., and Skolnick, P. 1989. Ultraviolet irradiation selectively disrupts the gamma-aminobutyric acid/benzodiazepine receptor-linked chloride ionophore. Mol. Pharmacol. 35:695-700.
    • (1989) Mol. Pharmacol. , vol.35 , pp. 695-700
    • Evoniuk, G.1    Moody, E.J.2    Skolnick, P.3
  • 25
    • 0006549637 scopus 로고
    • Influence of coordinating ligands on structure and spectra of hemerythrin
    • Kerestzes-Nagy, S., and Klotz, I. M. 1965. Influence of coordinating ligands on structure and spectra of hemerythrin. Biochemistry 4:919-931.
    • (1965) Biochemistry , vol.4 , pp. 919-931
    • Kerestzes-Nagy, S.1    Klotz, I.M.2
  • 26
    • 0014253008 scopus 로고
    • Allosteric interactions in aspartate transcarbamylase. II. Evidence for different conformational states of the protein in the presence and absence of specific ligands
    • Gerhart, J. C., and Schachman, H. K. 1968. Allosteric interactions in aspartate transcarbamylase. II. Evidence for different conformational states of the protein in the presence and absence of specific ligands. Biochemistry 7:538-552.
    • (1968) Biochemistry , vol.7 , pp. 538-552
    • Gerhart, J.C.1    Schachman, H.K.2
  • 27
    • 0023483332 scopus 로고
    • p-Chloromercuribenzoate-induced dissociation of cytoskeletal proteins in red blood cells of rats
    • Kunimoto, M., Shibata, K., and Miura, T. 1987. p-Chloromercuribenzoate-induced dissociation of cytoskeletal proteins in red blood cells of rats. Biochim. Biophys. Acta 905:257-267.
    • (1987) Biochim. Biophys. Acta , vol.905 , pp. 257-267
    • Kunimoto, M.1    Shibata, K.2    Miura, T.3
  • 28
    • 0027169106 scopus 로고
    • Effect of sulfhydryl reagents on spectrin states on the erythrocyte membrane
    • Yang, M. 1993. Effect of sulfhydryl reagents on spectrin states on the erythrocyte membrane. Biochem. Biophys. Res. Comm. 192:918-925.
    • (1993) Biochem. Biophys. Res. Comm. , vol.192 , pp. 918-925
    • Yang, M.1
  • 29
    • 0018353288 scopus 로고
    • Ligand-induced interconversion of affinity states in membrane-bound acetylcholine receptor from Torpedo californica. Effects of sulfhydryl and disulfide reagents
    • Moore, H.-P. H., and Raftery, M. A. 1979. Ligand-induced interconversion of affinity states in membrane-bound acetylcholine receptor from Torpedo californica. Effects of sulfhydryl and disulfide reagents. Biochemistry 18:1907-1911.
    • (1979) Biochemistry , vol.18 , pp. 1907-1911
    • Moore, H.-P.H.1    Raftery, M.A.2
  • 30
    • 0027517972 scopus 로고
    • Further evidence for multiple forms of an N-methyl-D-aspartate recognition domain in rat brain using membrane binding techniques
    • Zuo, P., Ogita, K. Suzuki, T., Han, D., and Yoneda, Y. 1993. Further evidence for multiple forms of an N-methyl-D-aspartate recognition domain in rat brain using membrane binding techniques. J. Neurochem. 61:1865-1873.
    • (1993) J. Neurochem. , vol.61 , pp. 1865-1873
    • Zuo, P.1    Ogita, K.2    Suzuki, T.3    Han, D.4    Yoneda, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.