메뉴 건너뛰기




Volumn 1783, Issue 10, 2008, Pages 1681-1699

FRET with multiply labeled HERG K+ channels as a reporter of the in vivo coarse architecture of the cytoplasmic domains

Author keywords

Cytoplasmic domain architecture; FRET; HERG; Potassium channel

Indexed keywords

AMMONIA; DYE; FLUOROPHORE; HYBRID PROTEIN; POTASSIUM CHANNEL HERG; UNCLASSIFIED DRUG;

EID: 51049115964     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2008.06.009     Document Type: Article
Times cited : (22)

References (67)
  • 1
    • 33645300737 scopus 로고    scopus 로고
    • From molecule to malady
    • Ashcroft F.M. From molecule to malady. Nature 440 (2006) 440-447
    • (2006) Nature , vol.440 , pp. 440-447
    • Ashcroft, F.M.1
  • 2
    • 0037026489 scopus 로고    scopus 로고
    • The voltage-gated potassium channels and their relatives
    • Yellen G. The voltage-gated potassium channels and their relatives. Nature 419 (2002) 35-42
    • (2002) Nature , vol.419 , pp. 35-42
    • Yellen, G.1
  • 3
    • 0037968706 scopus 로고    scopus 로고
    • The roles of N- and C-terminal determinants in the activation of the Kv1.2 potassium channel
    • Ju M., Stevens L., Leadbitter E., and Wray D. The roles of N- and C-terminal determinants in the activation of the Kv1.2 potassium channel. J. Biol. Chem. 278 (2003) 12769-12778
    • (2003) J. Biol. Chem. , vol.278 , pp. 12769-12778
    • Ju, M.1    Stevens, L.2    Leadbitter, E.3    Wray, D.4
  • 9
    • 34548383850 scopus 로고    scopus 로고
    • Cyclic nucleotide-regulated ion channels: spotlight on symmetry
    • Taraska J.W., and Zagotta W.N. Cyclic nucleotide-regulated ion channels: spotlight on symmetry. Structure 15 (2007) 1023-1024
    • (2007) Structure , vol.15 , pp. 1023-1024
    • Taraska, J.W.1    Zagotta, W.N.2
  • 10
    • 0141831003 scopus 로고    scopus 로고
    • Structural basis for modulation and agonist specificity of HCN pacemaker channels
    • Zagotta W.N., Olivier N.B., Black K.D., Young E.C., Olson R., and Gouaux E. Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature 425 (2003) 200-205
    • (2003) Nature , vol.425 , pp. 200-205
    • Zagotta, W.N.1    Olivier, N.B.2    Black, K.D.3    Young, E.C.4    Olson, R.5    Gouaux, E.6
  • 11
    • 9644290757 scopus 로고    scopus 로고
    • Defective assembly and trafficking of mutant HERG channels with C-terminal truncations in long QT syndrome
    • Gong Q., Keeney D.R., Robinson J.C., and Zhou Z. Defective assembly and trafficking of mutant HERG channels with C-terminal truncations in long QT syndrome. J. Mol. Cell. Cardiol. 37 (2004) 1225-1233
    • (2004) J. Mol. Cell. Cardiol. , vol.37 , pp. 1225-1233
    • Gong, Q.1    Keeney, D.R.2    Robinson, J.C.3    Zhou, Z.4
  • 12
    • 0037178862 scopus 로고    scopus 로고
    • Defective human ether-a-go-go-related gene trafficking linked to an endoplasmic reticulum retention signal in the C terminus
    • Kupershmidt S., Yang T., Chanthapahychith S., Wang Z., Towbin J.A., and Roden D.M. Defective human ether-a-go-go-related gene trafficking linked to an endoplasmic reticulum retention signal in the C terminus. J. Biol. Chem. 277 (2002) 27442-27448
    • (2002) J. Biol. Chem. , vol.277 , pp. 27442-27448
    • Kupershmidt, S.1    Yang, T.2    Chanthapahychith, S.3    Wang, Z.4    Towbin, J.A.5    Roden, D.M.6
  • 14
    • 23744494441 scopus 로고    scopus 로고
    • Identification of the cyclic-nucleotide-binding domain as a conserved determinant of ion-channel cell-surface localization
    • Akhavan A., Atanasiu R., Noguchi T., Han W., Holder N., and Shrier A. Identification of the cyclic-nucleotide-binding domain as a conserved determinant of ion-channel cell-surface localization. J. Cell. Sci. 118 (2005) 2803-2812
    • (2005) J. Cell. Sci. , vol.118 , pp. 2803-2812
    • Akhavan, A.1    Atanasiu, R.2    Noguchi, T.3    Han, W.4    Holder, N.5    Shrier, A.6
  • 16
    • 0030614462 scopus 로고    scopus 로고
    • The human Δ1261 mutation of the HERG potassium channel results in a truncated protein that contains a subunit interaction domain and decreases the channel expression
    • Li X., Xu J., and Li M. The human Δ1261 mutation of the HERG potassium channel results in a truncated protein that contains a subunit interaction domain and decreases the channel expression. J. Biol. Chem. 272 (1997) 705-708
    • (1997) J. Biol. Chem. , vol.272 , pp. 705-708
    • Li, X.1    Xu, J.2    Li, M.3
  • 17
    • 34248191435 scopus 로고    scopus 로고
    • Heteromeric assembly of HERG 1a/1b channels occurs cotranslationally via amino terminal interactions
    • Phartiyal P., Jones E.M.C., and Robertson G.A. Heteromeric assembly of HERG 1a/1b channels occurs cotranslationally via amino terminal interactions. J. Biol. Chem. 282 (2007) 9874-9882
    • (2007) J. Biol. Chem. , vol.282 , pp. 9874-9882
    • Phartiyal, P.1    Jones, E.M.C.2    Robertson, G.A.3
  • 18
    • 0032567106 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain
    • Morais-Cabral J.H., Lee A., Cohen S.L., Chait B.T., Li M., and MacKinnon R. Crystal structure and functional analysis of the HERG potassium channel N terminus: a eukaryotic PAS domain. Cell 95 (1998) 649-655
    • (1998) Cell , vol.95 , pp. 649-655
    • Morais-Cabral, J.H.1    Lee, A.2    Cohen, S.L.3    Chait, B.T.4    Li, M.5    MacKinnon, R.6
  • 19
    • 0030054878 scopus 로고    scopus 로고
    • Molecular determinants for activation and inactivation of HERG, a human inward rectifier potassium channel
    • Schönherr R., and Heinemann S.H. Molecular determinants for activation and inactivation of HERG, a human inward rectifier potassium channel. J. Physiol. (Lond.) 493 (1996) 635-642
    • (1996) J. Physiol. (Lond.) , vol.493 , pp. 635-642
    • Schönherr, R.1    Heinemann, S.H.2
  • 22
    • 0031742141 scopus 로고    scopus 로고
    • Regulation of deactivation by an amino terminal domain in Human ether-a-go-go-related gene potassium channels
    • Wang J., Trudeau M.C., Zappia A.M., and Robertson G.A. Regulation of deactivation by an amino terminal domain in Human ether-a-go-go-related gene potassium channels. J. Gen. Physiol. 112 (1998) 637-647
    • (1998) J. Gen. Physiol. , vol.112 , pp. 637-647
    • Wang, J.1    Trudeau, M.C.2    Zappia, A.M.3    Robertson, G.A.4
  • 23
    • 0035425497 scopus 로고    scopus 로고
    • Potassium channels: life in the post-structural world
    • Minor Jr. D.L. Potassium channels: life in the post-structural world. Curr.Op. Struct. Biol. 11 (2001) 408-414
    • (2001) Curr.Op. Struct. Biol. , vol.11 , pp. 408-414
    • Minor Jr., D.L.1
  • 25
    • 0028292927 scopus 로고
    • A family of potassium channel genes related to EAG in Drosophila and mammals
    • Warmke J.W., and Ganetzky B. A family of potassium channel genes related to EAG in Drosophila and mammals. Proc. Natl. Acad. Sci. U.S.A. 91 (1994) 3438-3442
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 3438-3442
    • Warmke, J.W.1    Ganetzky, B.2
  • 26
    • 33645317063 scopus 로고    scopus 로고
    • hERG potassium channels and cardiac arrhythmia
    • Sanguinetti M.C., and Tristani-Firouzi M. hERG potassium channels and cardiac arrhythmia. Nature 440 (2006) 463-469
    • (2006) Nature , vol.440 , pp. 463-469
    • Sanguinetti, M.C.1    Tristani-Firouzi, M.2
  • 27
    • 33846452126 scopus 로고    scopus 로고
    • Toxins interacting with ether-a-go-go-related gene voltage-dependent potassium channels
    • Wanke E., and Restano-Cassulini R. Toxins interacting with ether-a-go-go-related gene voltage-dependent potassium channels. Toxicon 49 (2006) 239-248
    • (2006) Toxicon , vol.49 , pp. 239-248
    • Wanke, E.1    Restano-Cassulini, R.2
  • 28
    • 41549099967 scopus 로고    scopus 로고
    • he hERG K+channel: target and antitarget strategies in drug development
    • Raschi E., Vasina V., Poluzzi E., and De Ponti F. he hERG K+channel: target and antitarget strategies in drug development. Pharmacol. Res. 57 (2008) 181-195
    • (2008) Pharmacol. Res. , vol.57 , pp. 181-195
    • Raschi, E.1    Vasina, V.2    Poluzzi, E.3    De Ponti, F.4
  • 29
    • 0033082093 scopus 로고    scopus 로고
    • Mutations of the S4-S5 linker alter activation properties of HERG potassium channels expressed in Xenopus oocytes
    • Sanguinetti M.C., and Xu Q.P. Mutations of the S4-S5 linker alter activation properties of HERG potassium channels expressed in Xenopus oocytes. J. Physiol. (Lond.) 514 (1999) 667-675
    • (1999) J. Physiol. (Lond.) , vol.514 , pp. 667-675
    • Sanguinetti, M.C.1    Xu, Q.P.2
  • 30
    • 0036097030 scopus 로고    scopus 로고
    • Fast and slow voltage sensor movements in HERG potassium channels
    • Smith P.L., and Yellen G. Fast and slow voltage sensor movements in HERG potassium channels. J. Gen. Physiol. 119 (2002) 275-293
    • (2002) J. Gen. Physiol. , vol.119 , pp. 275-293
    • Smith, P.L.1    Yellen, G.2
  • 31
    • 0038580641 scopus 로고    scopus 로고
    • Negative charges in the transmembrane domains of the HERG K channel are involved in the activation- and deactivation-gating processes
    • Liu J., Zhang M., Jiang M., and Tseng G.-N. Negative charges in the transmembrane domains of the HERG K channel are involved in the activation- and deactivation-gating processes. J. Gen. Physiol. 121 (2003) 599-614
    • (2003) J. Gen. Physiol. , vol.121 , pp. 599-614
    • Liu, J.1    Zhang, M.2    Jiang, M.3    Tseng, G.-N.4
  • 33
    • 10344246598 scopus 로고    scopus 로고
    • Gating charges in the activation and inactivation processes of the HERG channel
    • Zhang M., Liu J., and Tseng G.-N. Gating charges in the activation and inactivation processes of the HERG channel. J. Gen. Physiol. 124 (2004) 703-718
    • (2004) J. Gen. Physiol. , vol.124 , pp. 703-718
    • Zhang, M.1    Liu, J.2    Tseng, G.-N.3
  • 36
    • 0033537885 scopus 로고    scopus 로고
    • Long QT syndrome-associated mutations in the Per-Arnt-sim (PAS) domain of HERG potassium channels accelerate deactivation
    • Chen J., Zou A., Splawski I., Keating M.T., and Sanguinetti M.C. Long QT syndrome-associated mutations in the Per-Arnt-sim (PAS) domain of HERG potassium channels accelerate deactivation. J. Biol. Chem. 274 (1999) 10113-10118
    • (1999) J. Biol. Chem. , vol.274 , pp. 10113-10118
    • Chen, J.1    Zou, A.2    Splawski, I.3    Keating, M.T.4    Sanguinetti, M.C.5
  • 37
    • 33845383109 scopus 로고    scopus 로고
    • Modulation of HERG gating by a charge cluster in the N-terminal proximal domain
    • Saenen J.B., Labro A.J., Raes A., and Snyders D.J. Modulation of HERG gating by a charge cluster in the N-terminal proximal domain. Biophys. J. 91 (2006) 4381-4391
    • (2006) Biophys. J. , vol.91 , pp. 4381-4391
    • Saenen, J.B.1    Labro, A.J.2    Raes, A.3    Snyders, D.J.4
  • 38
    • 0037472735 scopus 로고    scopus 로고
    • Relevance of the proximal domain in the amino-terminus of HERG channels for regulation by a phospholipase C-coupled hormone receptor
    • Gómez-Varela D., Barros F., Viloria C.G., Giráldez T., Manso D.G., Dupuy S.G., Miranda P., and de la Peña P. Relevance of the proximal domain in the amino-terminus of HERG channels for regulation by a phospholipase C-coupled hormone receptor. FEBS Lett. 535 (2003) 125-130
    • (2003) FEBS Lett. , vol.535 , pp. 125-130
    • Gómez-Varela, D.1    Barros, F.2    Viloria, C.G.3    Giráldez, T.4    Manso, D.G.5    Dupuy, S.G.6    Miranda, P.7    de la Peña, P.8
  • 40
    • 0037134973 scopus 로고    scopus 로고
    • A new way to rapidly create functional, fluorescent fusion proteins: random insertion of GFP with an in vitro transposition reaction
    • Sheridan D.L., Berlot C.H., Robert A., Inglis F.M., Jakobsdottir K.B., Howe J.R., and Hughes T.E. A new way to rapidly create functional, fluorescent fusion proteins: random insertion of GFP with an in vitro transposition reaction. BMC Neurosci. 3 (2002) 7
    • (2002) BMC Neurosci. , vol.3 , pp. 7
    • Sheridan, D.L.1    Berlot, C.H.2    Robert, A.3    Inglis, F.M.4    Jakobsdottir, K.B.5    Howe, J.R.6    Hughes, T.E.7
  • 41
    • 27644451882 scopus 로고    scopus 로고
    • Generation of functional fluorescent BK channels by random insertion of GFP variants
    • Giráldez T., Hughes T.E., and Sigworth F.J. Generation of functional fluorescent BK channels by random insertion of GFP variants. J. Gen. Physiol. 126 (2005) 429-438
    • (2005) J. Gen. Physiol. , vol.126 , pp. 429-438
    • Giráldez, T.1    Hughes, T.E.2    Sigworth, F.J.3
  • 42
    • 0034581516 scopus 로고    scopus 로고
    • Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescence protein
    • Miyawaki A., and Tsien R.Y. Monitoring protein conformations and interactions by fluorescence resonance energy transfer between mutants of green fluorescence protein. Meth. Enzymol. 327 (2000) 472-500
    • (2000) Meth. Enzymol. , vol.327 , pp. 472-500
    • Miyawaki, A.1    Tsien, R.Y.2
  • 43
    • 0035959942 scopus 로고    scopus 로고
    • Preassociation of calmodulin with voltage-gated Ca2+ channels revealed by FRET in single living cells
    • Erickson M.G., Alseikhan B.A., Peterson B.Z., and Yue D.T. Preassociation of calmodulin with voltage-gated Ca2+ channels revealed by FRET in single living cells. Neuron 31 (2001) 973-985
    • (2001) Neuron , vol.31 , pp. 973-985
    • Erickson, M.G.1    Alseikhan, B.A.2    Peterson, B.Z.3    Yue, D.T.4
  • 44
    • 22444447736 scopus 로고    scopus 로고
    • Imaging molecular interactions in living cells
    • Day R.N., and Schaufele F. Imaging molecular interactions in living cells. Mol. Endocrinol. 19 (2005) 1675-1686
    • (2005) Mol. Endocrinol. , vol.19 , pp. 1675-1686
    • Day, R.N.1    Schaufele, F.2
  • 45
    • 20444383852 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) measurement by gradual acceptor photobleaching
    • Van Munster E.B., Kremers G.J., Adjobo-Hermans M.J.W., and Gadella Jr. T.W.J. Fluorescence resonance energy transfer (FRET) measurement by gradual acceptor photobleaching. J. Microsc. 218 (2005) 253-262
    • (2005) J. Microsc. , vol.218 , pp. 253-262
    • Van Munster, E.B.1    Kremers, G.J.2    Adjobo-Hermans, M.J.W.3    Gadella Jr., T.W.J.4
  • 48
    • 12744280975 scopus 로고    scopus 로고
    • Protein interaction quantified in vivo by spectrally resolved fluorescence resonance energy transfer
    • Raicu V., Jansma D.B., Miller R.J.D., and Friesen J.D. Protein interaction quantified in vivo by spectrally resolved fluorescence resonance energy transfer. Biochem. J. 385 (2005) 265-277
    • (2005) Biochem. J. , vol.385 , pp. 265-277
    • Raicu, V.1    Jansma, D.B.2    Miller, R.J.D.3    Friesen, J.D.4
  • 49
    • 2942640371 scopus 로고    scopus 로고
    • Photobleaching-corrected FRET efficiency imaging of live cells
    • Zal T., and Gascoigne N.R.J. Photobleaching-corrected FRET efficiency imaging of live cells. Biophys. J. 86 (2004) 3923-3939
    • (2004) Biophys. J. , vol.86 , pp. 3923-3939
    • Zal, T.1    Gascoigne, N.R.J.2
  • 50
    • 0038650819 scopus 로고    scopus 로고
    • FRET-based analysis of TRPC subunit stoichiometry
    • Amiri H., Schultz G., and Schaefer M. FRET-based analysis of TRPC subunit stoichiometry. Cell Calcium 33 (2003) 463-470
    • (2003) Cell Calcium , vol.33 , pp. 463-470
    • Amiri, H.1    Schultz, G.2    Schaefer, M.3
  • 51
    • 0034633010 scopus 로고    scopus 로고
    • Förster distances between green fluorescent protein pairs
    • Patterson G.H., Piston D.W., and Barisas B.G. Förster distances between green fluorescent protein pairs. Anal. Biochem. 284 (2000) 438-440
    • (2000) Anal. Biochem. , vol.284 , pp. 438-440
    • Patterson, G.H.1    Piston, D.W.2    Barisas, B.G.3
  • 52
    • 33748063281 scopus 로고    scopus 로고
    • Spatio-temporal kinetics of growth hormone receptor signalling in single cells using FRET microscopy
    • Biener-Ramajunan E., Ramajunan V.K., Herman B., and Gertler A. Spatio-temporal kinetics of growth hormone receptor signalling in single cells using FRET microscopy. Growth Horm. IGF Res. 16 (2006) 247-257
    • (2006) Growth Horm. IGF Res. , vol.16 , pp. 247-257
    • Biener-Ramajunan, E.1    Ramajunan, V.K.2    Herman, B.3    Gertler, A.4
  • 53
    • 28444437454 scopus 로고    scopus 로고
    • A flexible approach to the calculation of resonance energy transfer efficiency between multiple donors and acceptors in complex geometries
    • Corry B., Jayatilaka D., and Rigby P. A flexible approach to the calculation of resonance energy transfer efficiency between multiple donors and acceptors in complex geometries. Biophys. J. 89 (2005) 3822-3836
    • (2005) Biophys. J. , vol.89 , pp. 3822-3836
    • Corry, B.1    Jayatilaka, D.2    Rigby, P.3
  • 55
    • 44049102683 scopus 로고    scopus 로고
    • Single particle image reconstruction of the human recombinant Kv2.1 channel
    • Adair B., Nunn R., Lewis S., Dukes I., Philipson L., and Yeager M. Single particle image reconstruction of the human recombinant Kv2.1 channel. Biophys. J. 94 (2008) 2106-2114
    • (2008) Biophys. J. , vol.94 , pp. 2106-2114
    • Adair, B.1    Nunn, R.2    Lewis, S.3    Dukes, I.4    Philipson, L.5    Yeager, M.6
  • 59
    • 10344247673 scopus 로고    scopus 로고
    • Salt bridges and gating in the COOH-terminal region of HCN2 and CNGA1 channels
    • Craven K.V., and Zagotta W.N. Salt bridges and gating in the COOH-terminal region of HCN2 and CNGA1 channels. J. Gen. Physiol. 124 (2004) 663-677
    • (2004) J. Gen. Physiol. , vol.124 , pp. 663-677
    • Craven, K.V.1    Zagotta, W.N.2
  • 60
    • 0017795758 scopus 로고
    • Fluorescence energy transfer as a spectroscopic ruler
    • Stryer L. Fluorescence energy transfer as a spectroscopic ruler. Ann. Rev. Biochem. 47 (1978) 819-846
    • (1978) Ann. Rev. Biochem. , vol.47 , pp. 819-846
    • Stryer, L.1
  • 61
    • 0026687952 scopus 로고
    • Fluorescence resonance energy transfer and nucleic acids
    • Clegg R.M. Fluorescence resonance energy transfer and nucleic acids. Meth. Enzymol. 211 (1992) 353-388
    • (1992) Meth. Enzymol. , vol.211 , pp. 353-388
    • Clegg, R.M.1
  • 62
    • 0028913136 scopus 로고
    • Fluorescence resonance energy transfer
    • Selvin P.R. Fluorescence resonance energy transfer. Meth. Enzymol. 246 (1995) 300-334
    • (1995) Meth. Enzymol. , vol.246 , pp. 300-334
    • Selvin, P.R.1
  • 63
    • 0038664388 scopus 로고    scopus 로고
    • Conformational rearrangements associated with the gating of the G protein-coupled potassium channel revealed by FRET microscopy
    • Riven I., Kalmanzon E., Segev L., and Reuveny E. Conformational rearrangements associated with the gating of the G protein-coupled potassium channel revealed by FRET microscopy. Neuron 38 (2003) 225-235
    • (2003) Neuron , vol.38 , pp. 225-235
    • Riven, I.1    Kalmanzon, E.2    Segev, L.3    Reuveny, E.4
  • 64
    • 0042336988 scopus 로고    scopus 로고
    • Disruption of an intersubunit interaction underlies Ca2+ -calmodulin modulation of cyclic nucleotide-gated channels
    • Zheng J., Varnum M.D., and Zagotta W.N. Disruption of an intersubunit interaction underlies Ca2+ -calmodulin modulation of cyclic nucleotide-gated channels. J. Neurosci. 23 (2003) 8167-8175
    • (2003) J. Neurosci. , vol.23 , pp. 8167-8175
    • Zheng, J.1    Varnum, M.D.2    Zagotta, W.N.3
  • 65
    • 0036566026 scopus 로고    scopus 로고
    • Molecular architecture of a retinal cGMP-gated channel: the arrangement of the cytoplasmic domains
    • Higgins M.K., Weitz D., Warne T., Schertler G.F.X., and Kaupp U.B. Molecular architecture of a retinal cGMP-gated channel: the arrangement of the cytoplasmic domains. EMBO J. 21 (2002) 2087-2094
    • (2002) EMBO J. , vol.21 , pp. 2087-2094
    • Higgins, M.K.1    Weitz, D.2    Warne, T.3    Schertler, G.F.X.4    Kaupp, U.B.5
  • 66
    • 33750594842 scopus 로고    scopus 로고
    • Three-dimensional structure of the KchIP-Kv4.3 T1 complex reveals a cross-shaped octamer
    • Pioletti M., Findeisen F., Hura G.L., and Minor Jr. D.L. Three-dimensional structure of the KchIP-Kv4.3 T1 complex reveals a cross-shaped octamer. Nat. Struct. Mol. Biol. 13 (2006) 987-995
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 987-995
    • Pioletti, M.1    Findeisen, F.2    Hura, G.L.3    Minor Jr., D.L.4
  • 67
    • 27144448780 scopus 로고    scopus 로고
    • Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity
    • Martin B.R., Giepmans B.N.G., Adams S.R., and Tsien R.Y. Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity. Nat. Biotechnol. 23 (2005) 1308-1314
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1308-1314
    • Martin, B.R.1    Giepmans, B.N.G.2    Adams, S.R.3    Tsien, R.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.