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Volumn 117, Issue 13, 2013, Pages 3459-3468

Thioflavin T and its photoirradiative derivatives: Exploring their spectroscopic properties in the absence and presence of amyloid fibrils

Author keywords

[No Author keywords available]

Indexed keywords

GLYCOPROTEINS; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

EID: 84875795083     PISSN: 15206106     EISSN: 15205207     Source Type: Journal    
DOI: 10.1021/jp309331u     Document Type: Article
Times cited : (21)

References (66)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein Misfolding, Functional Amyloid, and Human Disease
    • Chiti, F.; Dobson, C. M. Protein Misfolding, Functional Amyloid, and Human Disease Annu. Rev. Biochem. 2006, 75, 333-366
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 36049020231 scopus 로고    scopus 로고
    • A General Model of Prion Strains and Their Pathogenicity
    • Collinge, J.; Clarke, A. R. A General Model of Prion Strains and Their Pathogenicity Science 2007, 318, 930-936
    • (2007) Science , vol.318 , pp. 930-936
    • Collinge, J.1    Clarke, A.R.2
  • 5
    • 32944457929 scopus 로고    scopus 로고
    • Amyloidosis
    • Pepys, M. B. Amyloidosis Annu. Rev. Med. 2006, 57, 223-241
    • (2006) Annu. Rev. Med. , vol.57 , pp. 223-241
    • Pepys, M.B.1
  • 6
    • 78649285837 scopus 로고    scopus 로고
    • Interactions between Amyloidophilic Dyes and Their Relevance to Studies of Amyloid Inhibitors
    • Buell, A. K.; Dobson, C. M.; Knowles, T. P. J.; Welland, M. E. Interactions between Amyloidophilic Dyes and Their Relevance to Studies of Amyloid Inhibitors Biophys. J. 2010, 99, 3492-3497
    • (2010) Biophys. J. , vol.99 , pp. 3492-3497
    • Buell, A.K.1    Dobson, C.M.2    Knowles, T.P.J.3    Welland, M.E.4
  • 7
    • 1442330474 scopus 로고    scopus 로고
    • From Conversion to Aggregation: Protofibril Formation of the Prion Protein
    • DeMarco, M. L.; Daggett, V. From Conversion to Aggregation: Protofibril Formation of the Prion Protein Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 2293-2298
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 2293-2298
    • Demarco, M.L.1    Daggett, V.2
  • 8
    • 84906367178 scopus 로고
    • On the Nature of the Waxy, Lardaceous, or Amyloid Deposit
    • Dickinson, W. H. On the Nature of the Waxy, Lardaceous, or Amyloid Deposit Med. Chir. Trans. 1867, 50, 39-56
    • (1867) Med. Chir. Trans. , vol.50 , pp. 39-56
    • Dickinson, W.H.1
  • 9
    • 0001781312 scopus 로고
    • Double-Refringence of the Amyloid-Congo-Red-Complex in Histological Sections
    • Ladewig, P. Double-Refringence of the Amyloid-Congo-Red-Complex in Histological Sections Nature 1945, 156, 81-82
    • (1945) Nature , vol.156 , pp. 81-82
    • Ladewig, P.1
  • 10
    • 0014191331 scopus 로고
    • Thioflavin S Fluorescent and Congo Red Anisotropic Stainings in the Histologic Demonstration of Amyloid
    • Kelenyi, G. Thioflavin S Fluorescent and Congo Red Anisotropic Stainings in the Histologic Demonstration of Amyloid Acta Neuropathol. 1967, 7, 336-348
    • (1967) Acta Neuropathol. , vol.7 , pp. 336-348
    • Kelenyi, G.1
  • 11
    • 58149333149 scopus 로고    scopus 로고
    • A New Amyloid-Like β-Aggregate with Most of the Amyloid Characteristics except Fibril Morphology
    • Chang, E. S.; Liao, T. Y.; Lim, T. S.; Fann, W.; Chen, R. P. A New Amyloid-Like β-Aggregate with Most of the Amyloid Characteristics except Fibril Morphology J. Mol. Biol. 2009, 385, 1257-1265
    • (2009) J. Mol. Biol. , vol.385 , pp. 1257-1265
    • Chang, E.S.1    Liao, T.Y.2    Lim, T.S.3    Fann, W.4    Chen, R.P.5
  • 13
    • 0036791002 scopus 로고    scopus 로고
    • One O-Linked Sugar Can Affect the Coil-to-Beta Structural Transition of the Prion Peptide
    • Chen, P. Y.; Lin, C. C.; Chang, Y. T.; Lin, S. C.; Chan, S. I. One O-Linked Sugar Can Affect the Coil-to-Beta Structural Transition of the Prion Peptide Proc. Natl. Acad. Sci. U.S.A. 2002, 99, 12633-12638
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 12633-12638
    • Chen, P.Y.1    Lin, C.C.2    Chang, Y.T.3    Lin, S.C.4    Chan, S.I.5
  • 15
    • 33846976187 scopus 로고    scopus 로고
    • Quantifying the Sequence-Dependent Species Barrier between Hamster and Mouse Prions
    • Lee, L. Y.; Chen, R. P. Quantifying the Sequence-Dependent Species Barrier between Hamster and Mouse Prions J. Am. Chem. Soc. 2007, 129, 1644-1652
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 1644-1652
    • Lee, L.Y.1    Chen, R.P.2
  • 16
    • 80255138067 scopus 로고    scopus 로고
    • Leu-138 in the Bovine Prion Peptide Fibrils Is Involved in the Seeding Discrimination Related to Codon-129 M/V Polymorphism in the Prion Peptide Seeding Experiment
    • Liao, T. Y.; Lee, L. Y.; Chen, R. P. Leu-138 in the Bovine Prion Peptide Fibrils Is Involved in the Seeding Discrimination Related to Codon-129 M/V Polymorphism in the Prion Peptide Seeding Experiment FEBS J. 2011, 278, 4351-4361
    • (2011) FEBS J. , vol.278 , pp. 4351-4361
    • Liao, T.Y.1    Lee, L.Y.2    Chen, R.P.3
  • 17
    • 84856344635 scopus 로고    scopus 로고
    • Exploring the Binding Mechanism of Thioflavin-T to the Beta-Amyloid Peptide by Blind Docking Method
    • Zhao, D. S.; Chen, Y. X.; Liu, Q.; Zhao, Y. F.; Li, Y. M. Exploring the Binding Mechanism of Thioflavin-T to the Beta-Amyloid Peptide by Blind Docking Method Sci. China: Chem. 2012, 55, 112-117
    • (2012) Sci. China: Chem. , vol.55 , pp. 112-117
    • Zhao, D.S.1    Chen, Y.X.2    Liu, Q.3    Zhao, Y.F.4    Li, Y.M.5
  • 18
    • 79953245314 scopus 로고    scopus 로고
    • Amyloid Structure: Conformational Diversity and Consequences
    • Toyama, B. H.; Weissman, J. S. Amyloid Structure: Conformational Diversity and Consequences Annu. Rev. Biochem. 2011, 80, 557-585
    • (2011) Annu. Rev. Biochem. , vol.80 , pp. 557-585
    • Toyama, B.H.1    Weissman, J.S.2
  • 19
    • 28244484729 scopus 로고    scopus 로고
    • Structures for Amyloid Fibrils
    • Makin, O. S.; Serpell, L. C. Structures for Amyloid Fibrils FEBS J. 2005, 272, 5950-5961
    • (2005) FEBS J. , vol.272 , pp. 5950-5961
    • Makin, O.S.1    Serpell, L.C.2
  • 20
    • 84864587117 scopus 로고    scopus 로고
    • Atomic Force Fluorescence Microscopy in the Characterization of Amyloid Fibril Assembly and Oligomeric Intermediates
    • Ostapchenko, V.; Gasset, M.; Baskakov, I. V. Atomic Force Fluorescence Microscopy in the Characterization of Amyloid Fibril Assembly and Oligomeric Intermediates Methods Mol. Biol. 2012, 849, 157-167
    • (2012) Methods Mol. Biol. , vol.849 , pp. 157-167
    • Ostapchenko, V.1    Gasset, M.2    Baskakov, I.V.3
  • 22
    • 0037592927 scopus 로고    scopus 로고
    • Direct Observation of Amyloid Fibril Growth Monitored by Thioflavin T Fluorescence
    • Ban, T.; Hamada, D.; Hasegawa, K.; Naiki, H.; Goto, Y. Direct Observation of Amyloid Fibril Growth Monitored by Thioflavin T Fluorescence J. Biol. Chem. 2003, 278, 16462-16465
    • (2003) J. Biol. Chem. , vol.278 , pp. 16462-16465
    • Ban, T.1    Hamada, D.2    Hasegawa, K.3    Naiki, H.4    Goto, Y.5
  • 23
    • 0024509805 scopus 로고
    • Fluorometric Determination of Amyloid Fibrils in Vitro Using the Fluorescent Dye, Thioflavin T1
    • Naiki, H.; Higuchi, K.; Hosokawa, M.; Takeda, T. Fluorometric Determination of Amyloid Fibrils in Vitro Using the Fluorescent Dye, Thioflavin T1 Anal. Biochem. 1989, 177, 244-249
    • (1989) Anal. Biochem. , vol.177 , pp. 244-249
    • Naiki, H.1    Higuchi, K.2    Hosokawa, M.3    Takeda, T.4
  • 24
    • 79957578506 scopus 로고    scopus 로고
    • Supramolecular Assemblies of Thioflavin T with Cucurbiturils: Prospects of Cooperative and Competitive Metal Ion Binding
    • Bhasikuttan, A. C.; Choudhury, S. D.; Pal, H.; Mohanty, J. Supramolecular Assemblies of Thioflavin T with Cucurbiturils: Prospects of Cooperative and Competitive Metal Ion Binding Isr. J. Chem. 2011, 51, 634-645
    • (2011) Isr. J. Chem. , vol.51 , pp. 634-645
    • Bhasikuttan, A.C.1    Choudhury, S.D.2    Pal, H.3    Mohanty, J.4
  • 25
    • 78149417674 scopus 로고    scopus 로고
    • Fluorescence Quantum Yield of Thioflavin T in Rigid Isotropic Solution and Incorporated into the Amyloid Fibrils
    • Sulatskaya, A. I.; Maskevich, A. A.; Kuznetsova, I. M.; Uversky, V. N.; Turoverov, K. K. Fluorescence Quantum Yield of Thioflavin T in Rigid Isotropic Solution and Incorporated into the Amyloid Fibrils PLoS One 2010, e15385
    • (2010) PLoS One , pp. 15385
    • Sulatskaya, A.I.1    Maskevich, A.A.2    Kuznetsova, I.M.3    Uversky, V.N.4    Turoverov, K.K.5
  • 26
    • 68849102984 scopus 로고    scopus 로고
    • Interactions of Thioflavin T with Serum Albumins: Spectroscopic Analyses
    • Sen, P.; Fatima, S.; Ahmad, B.; Khan, R. H. Interactions of Thioflavin T with Serum Albumins: Spectroscopic Analyses Spectrochim. Acta, Part A 2009, 74, 94-99
    • (2009) Spectrochim. Acta, Part A , vol.74 , pp. 94-99
    • Sen, P.1    Fatima, S.2    Ahmad, B.3    Khan, R.H.4
  • 28
    • 67349108090 scopus 로고    scopus 로고
    • Steady-State and Time-Resolved Emission Studies of Thioflavin-T
    • Naik, L. R.; Naik, A. B.; Pal, H. Steady-State and Time-Resolved Emission Studies of Thioflavin-T J. Photochem. Photobiol., A 2009, 204, 161-167
    • (2009) J. Photochem. Photobiol., A , vol.204 , pp. 161-167
    • Naik, L.R.1    Naik, A.B.2    Pal, H.3
  • 29
    • 0345874563 scopus 로고    scopus 로고
    • Emission of Thioflavin T and Its Control in the Presence of DNA
    • Ilanchelian, M.; Ramaraj, R. Emission of Thioflavin T and Its Control in the Presence of DNA J. Photochem. Photobiol., A 2004, 162, 129-137
    • (2004) J. Photochem. Photobiol., A , vol.162 , pp. 129-137
    • Ilanchelian, M.1    Ramaraj, R.2
  • 30
    • 0041705204 scopus 로고    scopus 로고
    • Influence of Cyclodextrin Complexation on the Emission of Thioflavin T and Its Off-On Control
    • Raj, C. R.; Ramaraj, R. Influence of Cyclodextrin Complexation on the Emission of Thioflavin T and Its Off-On Control J. Photochem. Photobiol., A 1999, 122, 39-46
    • (1999) J. Photochem. Photobiol., A , vol.122 , pp. 39-46
    • Raj, C.R.1    Ramaraj, R.2
  • 31
    • 0035790045 scopus 로고    scopus 로고
    • Emission of Thioflavin T and Its Off-On Control in Polymer Membranes
    • Raj, C. R.; Ramaraj, R. Emission of Thioflavin T and Its Off-On Control in Polymer Membranes Photochem. Photobiol. 2001, 74, 752-759
    • (2001) Photochem. Photobiol. , vol.74 , pp. 752-759
    • Raj, C.R.1    Ramaraj, R.2
  • 32
    • 0031577239 scopus 로고    scopus 로고
    • Gamma-Cyclodextrin Induced Intermolecular Excimer Formation of Thioflavin T
    • Raj, C. R.; Ramaraj, R. Gamma-Cyclodextrin Induced Intermolecular Excimer Formation of Thioflavin T Chem. Phys. Lett. 1997, 273, 285-290
    • (1997) Chem. Phys. Lett. , vol.273 , pp. 285-290
    • Raj, C.R.1    Ramaraj, R.2
  • 34
    • 77956531088 scopus 로고    scopus 로고
    • Highly Sensitive Amyloid Detection Enabled by Thioflavin T Dimers
    • Qin, L. H.; Vastl, J.; Gao, J. M. Highly Sensitive Amyloid Detection Enabled by Thioflavin T Dimers Mol. BioSyst. 2010, 6, 1791-1795
    • (2010) Mol. BioSyst. , vol.6 , pp. 1791-1795
    • Qin, L.H.1    Vastl, J.2    Gao, J.M.3
  • 36
    • 79956019256 scopus 로고    scopus 로고
    • Confined Ultrafast Torsional Dynamics of Thioflavin-T in a Nanocavity
    • Singh, P. K.; Kumbhakar, M.; Pal, H.; Nath, S. Confined Ultrafast Torsional Dynamics of Thioflavin-T in a Nanocavity Phys. Chem. Chem. Phys. 2011, 13, 8008-8014
    • (2011) Phys. Chem. Chem. Phys. , vol.13 , pp. 8008-8014
    • Singh, P.K.1    Kumbhakar, M.2    Pal, H.3    Nath, S.4
  • 37
    • 79959256663 scopus 로고    scopus 로고
    • Study of Thioflavin-T Immobilized in Porous Silicon and the Effect of Different Organic Vapors on the Fluorescence Lifetime
    • Hutter, T.; Amdursky, N.; Gepshtein, R.; Elliott, S. R.; Huppert, D. Study of Thioflavin-T Immobilized in Porous Silicon and the Effect of Different Organic Vapors on the Fluorescence Lifetime Langmuir 2011, 27, 7587-7594
    • (2011) Langmuir , vol.27 , pp. 7587-7594
    • Hutter, T.1    Amdursky, N.2    Gepshtein, R.3    Elliott, S.R.4    Huppert, D.5
  • 38
    • 67649197968 scopus 로고    scopus 로고
    • Ultrafast Torsional Dynamics of Protein Binding Dye Thioflavin-T in Nanoconfined Water Pool
    • Singh, P. K.; Kumbhakar, M.; Pal, H.; Nath, S. Ultrafast Torsional Dynamics of Protein Binding Dye Thioflavin-T in Nanoconfined Water Pool J. Phys. Chem. B 2009, 113, 8532-8538
    • (2009) J. Phys. Chem. B , vol.113 , pp. 8532-8538
    • Singh, P.K.1    Kumbhakar, M.2    Pal, H.3    Nath, S.4
  • 39
    • 56749096456 scopus 로고    scopus 로고
    • Thioflavin T Displays Enhanced Fluorescence Selectively inside Anionic Micelles and Mammalian Cells
    • Kumar, S.; Singh, A. K.; Krishnamoorthy, G.; Swaminathan, R. Thioflavin T Displays Enhanced Fluorescence Selectively inside Anionic Micelles and Mammalian Cells J. Fluoresc. 2008, 18, 1199-1205
    • (2008) J. Fluoresc. , vol.18 , pp. 1199-1205
    • Kumar, S.1    Singh, A.K.2    Krishnamoorthy, G.3    Swaminathan, R.4
  • 40
    • 58149175632 scopus 로고    scopus 로고
    • Thioflavin T as a Molecular Rotor: Fluorescent Properties of Thioflavin T in Solvents with Different Viscosity
    • Stsiapura, V. I.; Maskevich, A. A.; Kuzmitsky, V. A.; Uversky, V. N.; Kuznetsova, I. M.; Turoverov, K. K. Thioflavin T as a Molecular Rotor: Fluorescent Properties of Thioflavin T in Solvents with Different Viscosity J. Phys. Chem. B 2008, 112, 15893-15902
    • (2008) J. Phys. Chem. B , vol.112 , pp. 15893-15902
    • Stsiapura, V.I.1    Maskevich, A.A.2    Kuzmitsky, V.A.3    Uversky, V.N.4    Kuznetsova, I.M.5    Turoverov, K.K.6
  • 41
    • 84866388266 scopus 로고    scopus 로고
    • Molecular Rotors: What Lies behind the High Sensitivity of the Thioflavin-T Fluorescent Marker
    • Amdursky, N.; Erez, Y.; Huppert, D. Molecular Rotors: What Lies Behind the High Sensitivity of the Thioflavin-T Fluorescent Marker Acc. Chem. Res. 2012, 45, 1548-1557
    • (2012) Acc. Chem. Res. , vol.45 , pp. 1548-1557
    • Amdursky, N.1    Erez, Y.2    Huppert, D.3
  • 42
    • 84870980956 scopus 로고    scopus 로고
    • Temperature and Viscosity Dependence of the Nonradiative Decay Rates of Auramine-O and Thioflavin-T in Glass-Forming Solvents
    • Erez, Y.; Amdursky, N.; Gepshtein, R.; Huppert, D. Temperature and Viscosity Dependence of the Nonradiative Decay Rates of Auramine-O and Thioflavin-T in Glass-Forming Solvents J. Phys. Chem. A 2012, 116, 12056-12064
    • (2012) J. Phys. Chem. A , vol.116 , pp. 12056-12064
    • Erez, Y.1    Amdursky, N.2    Gepshtein, R.3    Huppert, D.4
  • 43
    • 79953035149 scopus 로고    scopus 로고
    • Temperature Dependence of the Fluorescence Properties of Thioflavin-T in Propanol, a Glass-Forming Liquid
    • Amdursky, N.; Gepshtein, R.; Erez, Y.; Huppert, D. Temperature Dependence of the Fluorescence Properties of Thioflavin-T in Propanol, a Glass-Forming Liquid J. Phys. Chem. A 2011, 115, 2540-2548
    • (2011) J. Phys. Chem. A , vol.115 , pp. 2540-2548
    • Amdursky, N.1    Gepshtein, R.2    Erez, Y.3    Huppert, D.4
  • 45
    • 77955616232 scopus 로고    scopus 로고
    • Charge Transfer Process Determines Ultrafast Excited State Deactivation of Thioflavin T in Low-Viscosity Solvents
    • Stsiapura, V. I.; Maskevich, A. A.; Tikhomirov, S. A.; Buganov, O. V. Charge Transfer Process Determines Ultrafast Excited State Deactivation of Thioflavin T in Low-Viscosity Solvents J. Phys. Chem. A 2010, 114, 8345-8350
    • (2010) J. Phys. Chem. A , vol.114 , pp. 8345-8350
    • Stsiapura, V.I.1    Maskevich, A.A.2    Tikhomirov, S.A.3    Buganov, O.V.4
  • 46
    • 69549101587 scopus 로고    scopus 로고
    • Near-Field Scanning Optical Microscopy Measurements of Fluorescent Molecular Probes Binding to Insulin Amyloid Fibrils
    • Kitts, C. C.; Bout, D. A. V. Near-Field Scanning Optical Microscopy Measurements of Fluorescent Molecular Probes Binding to Insulin Amyloid Fibrils J. Phys. Chem. B 2009, 113, 12090-12095
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12090-12095
    • Kitts, C.C.1    Bout, D.A.V.2
  • 47
    • 79953839293 scopus 로고    scopus 로고
    • On the Origin of the Stronger Binding of Pib over Thioflavin T to Protofibrils of the Alzheimer Amyloid-Beta Peptide: A Molecular Dynamics Study
    • Wu, C.; Bowers, M. T.; Shea, J. E. On the Origin of the Stronger Binding of Pib over Thioflavin T to Protofibrils of the Alzheimer Amyloid-Beta Peptide: A Molecular Dynamics Study Biophys. J. 2011, 100, 1316-1324
    • (2011) Biophys. J. , vol.100 , pp. 1316-1324
    • Wu, C.1    Bowers, M.T.2    Shea, J.E.3
  • 49
    • 43049164334 scopus 로고    scopus 로고
    • Secondary Nucleation and Accessible Surface in Insulin Amyloid Fibril Formation
    • Fodera, V.; Librizzi, F.; Groenning, M.; van de Weert, M.; Leone, M. Secondary Nucleation and Accessible Surface in Insulin Amyloid Fibril Formation J. Phys. Chem. B 2008, 112, 3853-3858
    • (2008) J. Phys. Chem. B , vol.112 , pp. 3853-3858
    • Fodera, V.1    Librizzi, F.2    Groenning, M.3    Van De Weert, M.4    Leone, M.5
  • 50
    • 76649138290 scopus 로고    scopus 로고
    • Binding Mode of Thioflavin T and Other Molecular Probes in the Context of Amyloid Fibrils-Current Status
    • Groenning, M. Binding Mode of Thioflavin T and Other Molecular Probes in the Context of Amyloid Fibrils-Current Status J. Chem. Biol. 2010, 3, 1-18
    • (2010) J. Chem. Biol. , vol.3 , pp. 1-18
    • Groenning, M.1
  • 51
    • 0035968202 scopus 로고    scopus 로고
    • Thioflavin T Is a Fluorescent Probe of the Acetylcholinesterase Peripheral Site That Reveals Conformational Interactions between the Peripheral and Acylation Sites
    • De Ferrari, G. V.; Mallender, W. D.; Inestrosa, N. C.; Rosenberry, T. L. Thioflavin T Is a Fluorescent Probe of the Acetylcholinesterase Peripheral Site That Reveals Conformational Interactions between the Peripheral and Acylation Sites J. Biol. Chem. 2001, 276, 23282-23287
    • (2001) J. Biol. Chem. , vol.276 , pp. 23282-23287
    • De Ferrari, G.V.1    Mallender, W.D.2    Inestrosa, N.C.3    Rosenberry, T.L.4
  • 52
    • 0000703066 scopus 로고
    • Toward a Systematic Molecular-Orbital Theory for Excited-States
    • Foresman, J. B.; Headgordon, M.; Pople, J. A.; Frisch, M. J. Toward a Systematic Molecular-Orbital Theory for Excited-States J. Phys. Chem. 1992, 96, 135-149
    • (1992) J. Phys. Chem. , vol.96 , pp. 135-149
    • Foresman, J.B.1    Headgordon, M.2    Pople, J.A.3    Frisch, M.J.4
  • 53
    • 1642335199 scopus 로고    scopus 로고
    • Failure of Time-Dependent Density Functional Theory for Long-Range Charge-Transfer Excited States: The Zincbacteriochlorin-Bacterlochlorin and Bacteriochlorophyll-Spheroidene Complexes
    • Dreuw, A.; Head-Gordon, M. Failure of Time-Dependent Density Functional Theory for Long-Range Charge-Transfer Excited States: The Zincbacteriochlorin- Bacterlochlorin and Bacteriochlorophyll-Spheroidene Complexes J. Am. Chem. Soc. 2004, 126, 4007-4016
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 4007-4016
    • Dreuw, A.1    Head-Gordon, M.2
  • 54
    • 0012753616 scopus 로고
    • A Comparison of Single Reference Methods for Characterizing Stationary-Points of Excited-State Potential-Energy Surfaces
    • Stanton, J. F.; Gauss, J.; Ishikawa, N.; Headgordon, M. A Comparison of Single Reference Methods for Characterizing Stationary-Points of Excited-State Potential-Energy Surfaces J. Chem. Phys. 1995, 103, 4160-4174
    • (1995) J. Chem. Phys. , vol.103 , pp. 4160-4174
    • Stanton, J.F.1    Gauss, J.2    Ishikawa, N.3    Headgordon, M.4
  • 55
    • 80052075541 scopus 로고    scopus 로고
    • Communication: Configuration Interaction Singles Has a Large Systematic Bias against Charge-Transfer States
    • Subotnik, J. E. Communication: Configuration Interaction Singles Has a Large Systematic Bias against Charge-Transfer States J. Chem. Phys. 2011, 135, 071104
    • (2011) J. Chem. Phys. , vol.135 , pp. 071104
    • Subotnik, J.E.1
  • 56
    • 33746868881 scopus 로고    scopus 로고
    • A State-Specific Polarizable Continuum Model Time Dependent Density Functional Theory Method for Excited State Calculations in Solution
    • Improta, R.; Barone, V.; Scalmani, G.; Frisch, M. J. A State-Specific Polarizable Continuum Model Time Dependent Density Functional Theory Method for Excited State Calculations in Solution J. Chem. Phys. 2006, 125, 054103
    • (2006) J. Chem. Phys. , vol.125 , pp. 054103
    • Improta, R.1    Barone, V.2    Scalmani, G.3    Frisch, M.J.4
  • 57
    • 0035918550 scopus 로고    scopus 로고
    • Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism
    • Nielsen, L.; Khurana, R.; Coats, A.; Frokjaer, S.; Brange, J.; Vyas, S.; Uversky, V. N.; Fink, A. L. Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism Biochemistry 2001, 40, 6036-6046
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 60
    • 33847088218 scopus 로고
    • Photocatalysis through Excitation of Adsorbates. 1. Highly Efficient N-Deethylation of Rhodamine B Adsorbed to Cadmium Sulfide
    • Watanabe, T.; Takizawa, T.; Honda, K. Photocatalysis through Excitation of Adsorbates. 1. Highly Efficient N-Deethylation of Rhodamine B Adsorbed to Cadmium Sulfide J. Phys. Chem. 1977, 81, 1845-1851
    • (1977) J. Phys. Chem. , vol.81 , pp. 1845-1851
    • Watanabe, T.1    Takizawa, T.2    Honda, K.3
  • 61
    • 30244524212 scopus 로고
    • Formation of Free Radicals in Water under High-Power Laser UV Irradiation
    • Nikogosyan, D.; Angelov, D. Formation of Free Radicals in Water under High-Power Laser UV Irradiation Chem. Phys. Lett. 1981, 77, 208-210
    • (1981) Chem. Phys. Lett. , vol.77 , pp. 208-210
    • Nikogosyan, D.1    Angelov, D.2
  • 63
    • 77951780294 scopus 로고    scopus 로고
    • Viscosity Effect on the Ultrafast Bond Twisting Dynamics in an Amyloid Fibril Sensor: Thioflavin-T
    • Singh, P. K.; Kumbhakar, M.; Pal, H.; Nath, S. Viscosity Effect on the Ultrafast Bond Twisting Dynamics in an Amyloid Fibril Sensor: Thioflavin-T J. Phys. Chem. B 2010, 114, 5920-5927
    • (2010) J. Phys. Chem. B , vol.114 , pp. 5920-5927
    • Singh, P.K.1    Kumbhakar, M.2    Pal, H.3    Nath, S.4
  • 66
    • 79960923653 scopus 로고    scopus 로고
    • Modeling the Nonradiative Decay Rate of Electronically Excited Thioflavin T
    • Huppert, D.; Erez, Y.; Liu, Y. H.; Amdursky, N. Modeling the Nonradiative Decay Rate of Electronically Excited Thioflavin T J. Phys. Chem. A 2011, 115, 8479-8487
    • (2011) J. Phys. Chem. A , vol.115 , pp. 8479-8487
    • Huppert, D.1    Erez, Y.2    Liu, Y.H.3    Amdursky, N.4


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