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Volumn 16, Issue 5, 2006, Pages 585-592

Manipulating proteins for neuroscience

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CATION CHANNEL; CHANNELRHODOPSIN 2; GLUCOSE; GLUTAMIC ACID; PROTEIN; UNCLASSIFIED DRUG;

EID: 33749187361     PISSN: 09594388     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.conb.2006.08.004     Document Type: Review
Times cited : (9)

References (58)
  • 1
    • 15944398014 scopus 로고    scopus 로고
    • A molecular and genetic arsenal for systems neuroscience
    • Callaway E.M. A molecular and genetic arsenal for systems neuroscience. Trends Neurosci 28 (2005) 196-201
    • (2005) Trends Neurosci , vol.28 , pp. 196-201
    • Callaway, E.M.1
  • 2
    • 0030610646 scopus 로고    scopus 로고
    • Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin
    • Miyawaki A., Llopis J., Heim R., McCaffery J.M., Adams J.A., Ikura M., and Tsien R.Y. Fluorescent indicators for Ca2+ based on green fluorescent proteins and calmodulin. Nature 388 (1997) 882-887
    • (1997) Nature , vol.388 , pp. 882-887
    • Miyawaki, A.1    Llopis, J.2    Heim, R.3    McCaffery, J.M.4    Adams, J.A.5    Ikura, M.6    Tsien, R.Y.7
  • 3
    • 0033514515 scopus 로고    scopus 로고
    • Dynamic and quantitative Ca2+ measurements using improved cameleons
    • Miyawaki A., Griesbeck O., Heim R., and Tsien R.Y. Dynamic and quantitative Ca2+ measurements using improved cameleons. Proc Natl Acad Sci USA 96 (1999) 2135-2140
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 2135-2140
    • Miyawaki, A.1    Griesbeck, O.2    Heim, R.3    Tsien, R.Y.4
  • 4
    • 33646145526 scopus 로고    scopus 로고
    • A FRET-based calcium biosensor with fast signal kinetics and high fluorescence change
    • Mank M., Reiff D.F., Heim N., Friedrich M.W., Borst A., and Griesbeck O. A FRET-based calcium biosensor with fast signal kinetics and high fluorescence change. Biophys J 90 (2006) 1790-1796
    • (2006) Biophys J , vol.90 , pp. 1790-1796
    • Mank, M.1    Reiff, D.F.2    Heim, N.3    Friedrich, M.W.4    Borst, A.5    Griesbeck, O.6
  • 5
    • 20844449080 scopus 로고    scopus 로고
    • Detection of glutamate release from neurons by genetically encoded surface-displayed FRET nanosensors
    • Okumoto S., Looger L.L., Micheva K.D., Reimer R.J., Smith S.J., and Frommer W.B. Detection of glutamate release from neurons by genetically encoded surface-displayed FRET nanosensors. Proc Natl Acad Sci USA 102 (2005) 8740-8745
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 8740-8745
    • Okumoto, S.1    Looger, L.L.2    Micheva, K.D.3    Reimer, R.J.4    Smith, S.J.5    Frommer, W.B.6
  • 6
    • 24344451972 scopus 로고    scopus 로고
    • Construction and optimization of a family of genetically encoded metabolite sensors by semirational protein engineering
    • Deuschle K., Okumoto S., Fehr M., Looger L.L., Kozhukh L., and Frommer W.B. Construction and optimization of a family of genetically encoded metabolite sensors by semirational protein engineering. Protein Sci 14 (2005) 2304-2314
    • (2005) Protein Sci , vol.14 , pp. 2304-2314
    • Deuschle, K.1    Okumoto, S.2    Fehr, M.3    Looger, L.L.4    Kozhukh, L.5    Frommer, W.B.6
  • 7
    • 0032500053 scopus 로고    scopus 로고
    • Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins
    • Miesenbock G., De Angelis D.A., and Rothman J.E. Visualizing secretion and synaptic transmission with pH-sensitive green fluorescent proteins. Nature 394 (1998) 192-195
    • (1998) Nature , vol.394 , pp. 192-195
    • Miesenbock, G.1    De Angelis, D.A.2    Rothman, J.E.3
  • 8
    • 0036221893 scopus 로고    scopus 로고
    • A genetically targetable fluorescent probe of channel gating with rapid kinetics
    • Ataka K., and Pieribone V.A. A genetically targetable fluorescent probe of channel gating with rapid kinetics. Biophys J 82 (2002) 509-516
    • (2002) Biophys J , vol.82 , pp. 509-516
    • Ataka, K.1    Pieribone, V.A.2
  • 9
    • 27644592613 scopus 로고    scopus 로고
    • A hybrid approach to measuring electrical activity in genetically specified neurons
    • To improve in vivo voltage detection, a hybrid approach is used by the authors to impart the speed of a dye with the specificity of a genetically encoded protein. More than most, this paper shows what can be achieved with well-known reagents used in an innovative way to solve a common problem.
    • Chanda B., Blunck R., Faria L.C., Schweizer F.E., Mody I., and Bezanilla F. A hybrid approach to measuring electrical activity in genetically specified neurons. Nat Neurosci 8 (2005) 1619-1626. To improve in vivo voltage detection, a hybrid approach is used by the authors to impart the speed of a dye with the specificity of a genetically encoded protein. More than most, this paper shows what can be achieved with well-known reagents used in an innovative way to solve a common problem.
    • (2005) Nat Neurosci , vol.8 , pp. 1619-1626
    • Chanda, B.1    Blunck, R.2    Faria, L.C.3    Schweizer, F.E.4    Mody, I.5    Bezanilla, F.6
  • 10
    • 0034912282 scopus 로고    scopus 로고
    • Design and characterization of a DNA-encoded, voltage-sensitive fluorescent protein
    • Sakai R., Repunte-Canonigo V., Raj C.D., and Knopfel T. Design and characterization of a DNA-encoded, voltage-sensitive fluorescent protein. Eur J Neurosci 13 (2001) 2314-2318
    • (2001) Eur J Neurosci , vol.13 , pp. 2314-2318
    • Sakai, R.1    Repunte-Canonigo, V.2    Raj, C.D.3    Knopfel, T.4
  • 11
    • 0030834492 scopus 로고    scopus 로고
    • A genetically encoded optical probe of membrane voltage
    • Siegel M.S., and Isacoff E.Y. A genetically encoded optical probe of membrane voltage. Neuron 19 (1997) 735-741
    • (1997) Neuron , vol.19 , pp. 735-741
    • Siegel, M.S.1    Isacoff, E.Y.2
  • 13
    • 14644442259 scopus 로고    scopus 로고
    • Dopaminergic stimulation of local protein synthesis enhances surface expression of GluR1 and synaptic transmission in hippocampal neurons
    • The authors used both a GFP translation reporter and a localized application of a fluorescent puromycin analog to visualize localized protein synthesis in response to a dopamine agonist. This synthesis is dependent on protein kinase A signaling and can affect the levels of an AMPA receptor subunit, and is one of the first comprehensive observations of local protein synthesis in neuronal processes.
    • Smith W.B., Starck S.R., Roberts R.W., and Schuman E.M. Dopaminergic stimulation of local protein synthesis enhances surface expression of GluR1 and synaptic transmission in hippocampal neurons. Neuron 45 (2005) 765-779. The authors used both a GFP translation reporter and a localized application of a fluorescent puromycin analog to visualize localized protein synthesis in response to a dopamine agonist. This synthesis is dependent on protein kinase A signaling and can affect the levels of an AMPA receptor subunit, and is one of the first comprehensive observations of local protein synthesis in neuronal processes.
    • (2005) Neuron , vol.45 , pp. 765-779
    • Smith, W.B.1    Starck, S.R.2    Roberts, R.W.3    Schuman, E.M.4
  • 14
    • 3342935872 scopus 로고    scopus 로고
    • A general approach to detect protein expression in vivo using fluorescent puromycin conjugates
    • Starck S.R., Green H.M., Alberola-Ila J., and Roberts R.W. A general approach to detect protein expression in vivo using fluorescent puromycin conjugates. Chem Biol 11 (2004) 999-1008
    • (2004) Chem Biol , vol.11 , pp. 999-1008
    • Starck, S.R.1    Green, H.M.2    Alberola-Ila, J.3    Roberts, R.W.4
  • 15
    • 0034990497 scopus 로고    scopus 로고
    • Dynamic visualization of local protein synthesis in hippocampal neurons
    • Aakalu G., Smith W.B., Nguyen N., Jiang C., and Schuman E.M. Dynamic visualization of local protein synthesis in hippocampal neurons. Neuron 30 (2001) 489-502
    • (2001) Neuron , vol.30 , pp. 489-502
    • Aakalu, G.1    Smith, W.B.2    Nguyen, N.3    Jiang, C.4    Schuman, E.M.5
  • 17
    • 0037012096 scopus 로고    scopus 로고
    • Selective photostimulation of genetically chARGed neurons
    • Zemelman B.V., Lee G.A., Ng M., and Miesenbock G. Selective photostimulation of genetically chARGed neurons. Neuron 33 (2002) 15-22
    • (2002) Neuron , vol.33 , pp. 15-22
    • Zemelman, B.V.1    Lee, G.A.2    Ng, M.3    Miesenbock, G.4
  • 18
    • 12344309164 scopus 로고    scopus 로고
    • Light-activated ion channels for remote control of neuronal firing
    • Banghart M., Borges K., Isacoff E., Trauner D., and Kramer R.H. Light-activated ion channels for remote control of neuronal firing. Nat Neurosci 7 (2004) 1381-1386
    • (2004) Nat Neurosci , vol.7 , pp. 1381-1386
    • Banghart, M.1    Borges, K.2    Isacoff, E.3    Trauner, D.4    Kramer, R.H.5
  • 19
    • 26444501014 scopus 로고    scopus 로고
    • Long-term potentiation of exogenous glutamate responses at single dendritic spines
    • Bagal A.A., Kao J.P., Tang C.M., and Thompson S.M. Long-term potentiation of exogenous glutamate responses at single dendritic spines. Proc Natl Acad Sci USA 102 (2005) 14434-14439
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 14434-14439
    • Bagal, A.A.1    Kao, J.P.2    Tang, C.M.3    Thompson, S.M.4
  • 20
    • 21844479254 scopus 로고    scopus 로고
    • Detection of increased local excitatory circuits in the hippocampus during epileptogenesis using focal flash photolysis of caged glutamate
    • Shao L.R., and Dudek F.E. Detection of increased local excitatory circuits in the hippocampus during epileptogenesis using focal flash photolysis of caged glutamate. Epilepsia 46 Suppl 5 (2005) 100-106
    • (2005) Epilepsia , vol.46 , Issue.SUPPL. 5 , pp. 100-106
    • Shao, L.R.1    Dudek, F.E.2
  • 21
    • 14544308338 scopus 로고    scopus 로고
    • Excitatory cortical neurons form fine-scale functional networks
    • Yoshimura Y., Dantzker J.L., and Callaway E.M. Excitatory cortical neurons form fine-scale functional networks. Nature 433 (2005) 868-873
    • (2005) Nature , vol.433 , pp. 868-873
    • Yoshimura, Y.1    Dantzker, J.L.2    Callaway, E.M.3
  • 22
    • 17044431846 scopus 로고    scopus 로고
    • Remote control of behavior through genetically targeted photostimulation of neurons
    • The authors combined caged ATP and neuron-specific promoters to enable one of the first whole animal in vivo examinations of behavioral circuits by depolarizing groups of neurons. Merely depolarizing specific neurons, even in an animal without a central nervous system, recapitulates known behaviors and indicates that for some behavioral circuits specific neurons, rather than the brain, can control the behavioral response.
    • Lima S.Q., and Miesenbock G. Remote control of behavior through genetically targeted photostimulation of neurons. Cell 121 (2005) 141-152. The authors combined caged ATP and neuron-specific promoters to enable one of the first whole animal in vivo examinations of behavioral circuits by depolarizing groups of neurons. Merely depolarizing specific neurons, even in an animal without a central nervous system, recapitulates known behaviors and indicates that for some behavioral circuits specific neurons, rather than the brain, can control the behavioral response.
    • (2005) Cell , vol.121 , pp. 141-152
    • Lima, S.Q.1    Miesenbock, G.2
  • 23
    • 26444621497 scopus 로고    scopus 로고
    • Millisecond-timescale, genetically targeted optical control of neural activity
    • Boyden E.S., Zhang F., Bamberg E., Nagel G., and Deisseroth K. Millisecond-timescale, genetically targeted optical control of neural activity. Nat Neurosci 8 (2005) 1263-1268
    • (2005) Nat Neurosci , vol.8 , pp. 1263-1268
    • Boyden, E.S.1    Zhang, F.2    Bamberg, E.3    Nagel, G.4    Deisseroth, K.5
  • 24
    • 29044433616 scopus 로고    scopus 로고
    • Light activation of channelrhodopsin-2 in excitable cells of Caenorhabditis elegans triggers rapid behavioral responses
    • Nagel G., Brauner M., Liewald J.F., Adeishvili N., Bamberg E., and Gottschalk A. Light activation of channelrhodopsin-2 in excitable cells of Caenorhabditis elegans triggers rapid behavioral responses. Curr Biol 15 (2005) 2279-2284
    • (2005) Curr Biol , vol.15 , pp. 2279-2284
    • Nagel, G.1    Brauner, M.2    Liewald, J.F.3    Adeishvili, N.4    Bamberg, E.5    Gottschalk, A.6
  • 25
    • 33645974269 scopus 로고    scopus 로고
    • Ectopic expression of a microbial-type rhodopsin restores visual responses in mice with photoreceptor degeneration
    • The authors report that in a genetic mouse model of retinitis pigmentosa induced blindness, expression of ChR2 by viral injection enables the degenerated retinas to respond to a light stimulus and is stable for up to 6 months. The degenerated retinas, rendered sensitive to light again by ChR2, are able to send signals to the visual cortex.
    • Bi A., Cui J., Ma Y.P., Olshevskaya E., Pu M., Dizhoor A.M., and Pan Z.H. Ectopic expression of a microbial-type rhodopsin restores visual responses in mice with photoreceptor degeneration. Neuron 50 (2006) 23-33. The authors report that in a genetic mouse model of retinitis pigmentosa induced blindness, expression of ChR2 by viral injection enables the degenerated retinas to respond to a light stimulus and is stable for up to 6 months. The degenerated retinas, rendered sensitive to light again by ChR2, are able to send signals to the visual cortex.
    • (2006) Neuron , vol.50 , pp. 23-33
    • Bi, A.1    Cui, J.2    Ma, Y.P.3    Olshevskaya, E.4    Pu, M.5    Dizhoor, A.M.6    Pan, Z.H.7
  • 26
    • 29144480494 scopus 로고    scopus 로고
    • Fast noninvasive activation and inhibition of neural and network activity by vertebrate rhodopsin and green algae channelrhodopsin
    • The authors find that expression of two different light activated proteins, ChR2 and RO4, depolarize and hyperpolarize neurons, respectively, in response to specific wavelengths. In both cultured hippocampal neurons and embryonic chick spinal cords, these proteins can be used to control action potentials and their frequencies, setting the stage for functional examinations of polarization in learning and memory.
    • Li X., Gutierrez D.V., Hanson M.G., Han J., Mark M.D., Chiel H., Hegemann P., Landmesser L.T., and Herlitze S. Fast noninvasive activation and inhibition of neural and network activity by vertebrate rhodopsin and green algae channelrhodopsin. Proc Natl Acad Sci USA 102 (2005) 17816-17821. The authors find that expression of two different light activated proteins, ChR2 and RO4, depolarize and hyperpolarize neurons, respectively, in response to specific wavelengths. In both cultured hippocampal neurons and embryonic chick spinal cords, these proteins can be used to control action potentials and their frequencies, setting the stage for functional examinations of polarization in learning and memory.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 17816-17821
    • Li, X.1    Gutierrez, D.V.2    Hanson, M.G.3    Han, J.4    Mark, M.D.5    Chiel, H.6    Hegemann, P.7    Landmesser, L.T.8    Herlitze, S.9
  • 27
    • 31844446419 scopus 로고    scopus 로고
    • The mechanisms and functions of activity-dependent long-term potentiation of intrinsic excitability
    • Xu J., and Kang J. The mechanisms and functions of activity-dependent long-term potentiation of intrinsic excitability. Rev Neurosci 16 (2005) 311-323
    • (2005) Rev Neurosci , vol.16 , pp. 311-323
    • Xu, J.1    Kang, J.2
  • 28
    • 0024968835 scopus 로고
    • A general method for site-specific incorporation of unnatural amino acids into proteins
    • Noren C.J., Anthony-Cahill S.J., Griffith M.C., and Schultz P.G. A general method for site-specific incorporation of unnatural amino acids into proteins. Science 244 (1989) 182-188
    • (1989) Science , vol.244 , pp. 182-188
    • Noren, C.J.1    Anthony-Cahill, S.J.2    Griffith, M.C.3    Schultz, P.G.4
  • 30
    • 27744608733 scopus 로고    scopus 로고
    • Cis-trans isomerization at a proline opens the pore of a neurotransmitter-gated ion channel
    • 3A, the authors reveal that this proline is implicated as the connection between ligand binding and ungating of the channel. This elegant work shows how fine manipulation of amino acid structure can elucidate functional mechanisms of integral membrane receptors.
    • 3A, the authors reveal that this proline is implicated as the connection between ligand binding and ungating of the channel. This elegant work shows how fine manipulation of amino acid structure can elucidate functional mechanisms of integral membrane receptors.
    • (2005) Nature , vol.438 , pp. 248-252
    • Lummis, S.C.1    Beene, D.L.2    Lee, L.W.3    Lester, H.A.4    Broadhurst, R.W.5    Dougherty, D.A.6
  • 31
    • 25144465496 scopus 로고    scopus 로고
    • A cation-pi binding interaction with a tyrosine in the binding site of the GABAC receptor
    • Lummis S.C., D L.B., Harrison N.J., LesterF H.A., and Dougherty D.A. A cation-pi binding interaction with a tyrosine in the binding site of the GABAC receptor. Chem Biol 12 (2005) 993-997
    • (2005) Chem Biol , vol.12 , pp. 993-997
    • Lummis, S.C.1    Harrison, N.J.2    Lester, F.H.A.3    Dougherty, D.A.4
  • 32
    • 5644237713 scopus 로고    scopus 로고
    • Tyrosine residues that control binding and gating in the 5-hydroxytryptamine3 receptor revealed by unnatural amino acid mutagenesis
    • Beene D.L., Price K.L., Lester H.A., Dougherty D.A., and Lummis S.C. Tyrosine residues that control binding and gating in the 5-hydroxytryptamine3 receptor revealed by unnatural amino acid mutagenesis. J Neurosci 24 (2004) 9097-9104
    • (2004) J Neurosci , vol.24 , pp. 9097-9104
    • Beene, D.L.1    Price, K.L.2    Lester, H.A.3    Dougherty, D.A.4    Lummis, S.C.5
  • 33
    • 0038506126 scopus 로고    scopus 로고
    • Site-specific incorporation of unnatural amino acids into receptors expressed in Mammalian cells
    • Monahan S.L., Lester H.A., and Dougherty D.A. Site-specific incorporation of unnatural amino acids into receptors expressed in Mammalian cells. Chem Biol 10 (2003) 573-580
    • (2003) Chem Biol , vol.10 , pp. 573-580
    • Monahan, S.L.1    Lester, H.A.2    Dougherty, D.A.3
  • 34
    • 0035917812 scopus 로고    scopus 로고
    • Expanding the genetic code of Escherichia coli
    • Wang L., Brock A., Herberich B., and Schultz P.G. Expanding the genetic code of Escherichia coli. Science 292 (2001) 498-500
    • (2001) Science , vol.292 , pp. 498-500
    • Wang, L.1    Brock, A.2    Herberich, B.3    Schultz, P.G.4
  • 39
    • 0037422608 scopus 로고    scopus 로고
    • Addition of the keto functional group to the genetic code of Escherichia coli
    • Wang L., Zhang Z., Brock A., and Schultz P.G. Addition of the keto functional group to the genetic code of Escherichia coli. Proc Natl Acad Sci USA 100 (2003) 56-61
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 56-61
    • Wang, L.1    Zhang, Z.2    Brock, A.3    Schultz, P.G.4
  • 40
    • 31544456661 scopus 로고    scopus 로고
    • The incorporation of a photoisomerizable amino acid into proteins in E. coli
    • Bose M., Groff D., Xie J., Brustad E., and Schultz P.G. The incorporation of a photoisomerizable amino acid into proteins in E. coli. J Am Chem Soc 128 (2006) 388-389
    • (2006) J Am Chem Soc , vol.128 , pp. 388-389
    • Bose, M.1    Groff, D.2    Xie, J.3    Brustad, E.4    Schultz, P.G.5
  • 41
    • 18744396951 scopus 로고    scopus 로고
    • Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid
    • Hino N., Okazaki Y., Kobayashi T., Hayashi A., Sakamoto K., and Yokoyama S. Protein photo-cross-linking in mammalian cells by site-specific incorporation of a photoreactive amino acid. Nat Methods 2 (2005) 201-206
    • (2005) Nat Methods , vol.2 , pp. 201-206
    • Hino, N.1    Okazaki, Y.2    Kobayashi, T.3    Hayashi, A.4    Sakamoto, K.5    Yokoyama, S.6
  • 42
    • 33646038596 scopus 로고    scopus 로고
    • The genetic incorporation of a distance probe into proteins in Escherichia coli
    • Tsao M.L., Summerer D., Ryu Y., and Schultz P.G. The genetic incorporation of a distance probe into proteins in Escherichia coli. J Am Chem Soc 128 (2006) 4572-4573
    • (2006) J Am Chem Soc , vol.128 , pp. 4572-4573
    • Tsao, M.L.1    Summerer, D.2    Ryu, Y.3    Schultz, P.G.4
  • 45
    • 0033152865 scopus 로고    scopus 로고
    • Protein evolution by molecular breeding
    • Minshull J., and Stemmer W.P. Protein evolution by molecular breeding. Curr Opin Chem Biol 3 (1999) 284-290
    • (1999) Curr Opin Chem Biol , vol.3 , pp. 284-290
    • Minshull, J.1    Stemmer, W.P.2
  • 46
    • 10044227172 scopus 로고    scopus 로고
    • Evolution of new nonantibody proteins via iterative somatic hypermutation
    • Wang L., Jackson W.C., Steinbach P.A., and Tsien R.Y. Evolution of new nonantibody proteins via iterative somatic hypermutation. Proc Natl Acad Sci USA 101 (2004) 16745-16749
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16745-16749
    • Wang, L.1    Jackson, W.C.2    Steinbach, P.A.3    Tsien, R.Y.4
  • 47
    • 0036674618 scopus 로고    scopus 로고
    • AID and mismatch repair in antibody diversification
    • Martin A., and Scharff M.D. AID and mismatch repair in antibody diversification. Nat Rev Immunol 2 (2002) 605-614
    • (2002) Nat Rev Immunol , vol.2 , pp. 605-614
    • Martin, A.1    Scharff, M.D.2
  • 49
    • 33644636246 scopus 로고    scopus 로고
    • AID in somatic hypermutation and class switch recombination
    • Longerich S., Basu U., Alt F., and Storb U. AID in somatic hypermutation and class switch recombination. Curr Opin Immunol 18 (2006) 164-174
    • (2006) Curr Opin Immunol , vol.18 , pp. 164-174
    • Longerich, S.1    Basu, U.2    Alt, F.3    Storb, U.4
  • 51
    • 11144267737 scopus 로고    scopus 로고
    • Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein
    • Shaner N.C., Campbell R.E., Steinbach P.A., Giepmans B.N., Palmer A.E., and Tsien R.Y. Improved monomeric red, orange and yellow fluorescent proteins derived from Discosoma sp. red fluorescent protein. Nat Biotechnol 22 (2004) 1567-1572
    • (2004) Nat Biotechnol , vol.22 , pp. 1567-1572
    • Shaner, N.C.1    Campbell, R.E.2    Steinbach, P.A.3    Giepmans, B.N.4    Palmer, A.E.5    Tsien, R.Y.6
  • 52
    • 3242706582 scopus 로고    scopus 로고
    • Expanded dynamic range of fluorescent indicators for Ca(2+) by circularly permuted yellow fluorescent proteins
    • Nagai T., Yamada S., Tominaga T., Ichikawa M., and Miyawaki A. Expanded dynamic range of fluorescent indicators for Ca(2+) by circularly permuted yellow fluorescent proteins. Proc Natl Acad Sci USA 101 (2004) 10554-10559
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 10554-10559
    • Nagai, T.1    Yamada, S.2    Tominaga, T.3    Ichikawa, M.4    Miyawaki, A.5
  • 53
    • 1842424983 scopus 로고    scopus 로고
    • An improved cyan fluorescent protein variant useful for FRET
    • Rizzo M.A., Springer G.H., Granada B., and Piston D.W. An improved cyan fluorescent protein variant useful for FRET. Nat Biotechnol 22 (2004) 445-449
    • (2004) Nat Biotechnol , vol.22 , pp. 445-449
    • Rizzo, M.A.1    Springer, G.H.2    Granada, B.3    Piston, D.W.4
  • 55
    • 10644234677 scopus 로고    scopus 로고
    • Bcl-2-mediated alterations in endoplasmic reticulum Ca2+ analyzed with an improved genetically encoded fluorescent sensor
    • Palmer A.E., Jin C., Reed J.C., and Tsien R.Y. Bcl-2-mediated alterations in endoplasmic reticulum Ca2+ analyzed with an improved genetically encoded fluorescent sensor. Proc Natl Acad Sci USA 101 (2004) 17404-17409
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17404-17409
    • Palmer, A.E.1    Jin, C.2    Reed, J.C.3    Tsien, R.Y.4
  • 58
    • 33749076327 scopus 로고    scopus 로고
    • Chambers JJ, Banghart MR, Trauner D, Kramer RH: Light-induced depolarization of neurons using a modified Shaker K+ channel and a molecular photoswitch. J Neurophysiol 2006; DOI:10.1152/jn.00318.2006. By altering the cation specificity of the Shaker pore of the existing synthetic channel H-SPARK (hyperpolarizing SPARK), the authors create D-SPARK (depolarizing SPARK). D-SPARK allows all cations to flow, leading to depolarization rather than hyperpolarization upon light application. This pair of synthetic channels can be used simultaneously in different neurons, and can also be closed by application of specific wavelength light, unlike other light-controlled systems.


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