메뉴 건너뛰기




Volumn 107, Issue 39, 2010, Pages 16863-16868

Protein-induced photophysical changes to the amyloid indicator dye thioflavin T

Author keywords

Alzheimer's; Beta 2 microglobulin; Parkinson; Photophysics; TICT

Indexed keywords

BETA 2 MICROGLOBULIN; THIOFLAVINE; AMYLOID; FLUORESCENT DYE; THIAZOLE DERIVATIVE;

EID: 78049308448     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1002867107     Document Type: Article
Times cited : (273)

References (39)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • DOI 10.1146/annurev.biochem.75.101304.123901
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333-366. (Pubitemid 44118036)
    • (2006) Annual Review of Biochemistry , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: Insights from solid-state NMR
    • DOI 10.1017/S0033583506004173, PII S0033583506004173
    • Tycko R (2006) Molecular structure of amyloid fibrils: Insights from solid-state NMR. Q Rev Biophys 39(1):1-55. (Pubitemid 44566373)
    • (2006) Quarterly Reviews of Biophysics , vol.39 , Issue.1 , pp. 1-55
    • Tycko, R.1
  • 3
    • 33646375442 scopus 로고    scopus 로고
    • Deposition diseases and 3D domain swapping
    • Bennett MJ, Sawaya MR, Eisenberg D (2006) Deposition diseases and 3D domain swapping. Structure 14(5):811-824.
    • (2006) Structure , vol.14 , Issue.5 , pp. 811-824
    • Bennett, M.J.1    Sawaya, M.R.2    Eisenberg, D.3
  • 4
    • 73649140576 scopus 로고    scopus 로고
    • The common architecture of cross-beta amyloid
    • Jahn TR, et al. (2010) The common architecture of cross-beta amyloid. J Mol Biol 395(4):717-727.
    • (2010) J Mol Biol , vol.395 , Issue.4 , pp. 717-727
    • Jahn, T.R.1
  • 6
    • 76649098825 scopus 로고    scopus 로고
    • Binding modeof Thioflavin T and other molecular probes in the context of amyloid fibrils-current status
    • Groenning M (2009) Binding modeof Thioflavin T and other molecular probes in the context of amyloid fibrils-current status. J Chem Biol.
    • (2009) J Chem Biol
    • Groenning, M.1
  • 7
    • 58149326746 scopus 로고    scopus 로고
    • Molecular mechanism of thioflavin-T binding to the surface of beta-rich peptide self-assemblies
    • Biancalana M, Makabe K, Koide A, Koide S (2009) Molecular mechanism of thioflavin-T binding to the surface of beta-rich peptide self-assemblies. J Mol Biol 385(4):1052-1063.
    • (2009) J Mol Biol , vol.385 , Issue.4 , pp. 1052-1063
    • Biancalana, M.1    Makabe, K.2    Koide, A.3    Koide, S.4
  • 8
    • 0000464103 scopus 로고
    • Fluorescent stains, with special reference to amyloid and connective tissues
    • Vassar PS, Culling CF (1959) Fluorescent stains, with special reference to amyloid and connective tissues. Arch Pathol 68:487-498.
    • (1959) Arch Pathol , vol.68 , pp. 487-498
    • Vassar, P.S.1    Culling, C.F.2
  • 9
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H, III (1993) Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci 2(3):404-410.
    • (1993) Protein Sci , vol.2 , Issue.3 , pp. 404-410
    • LeVine III, H.1
  • 10
    • 77952320068 scopus 로고    scopus 로고
    • Molecular mechanism of Thioflavin-T binding to amyloid fibrils
    • Biancalana M, Koide S Molecular mechanism of Thioflavin-T binding to amyloid fibrils.. Biochim Biophys Acta 1804(7):1405-1412.
    • Biochim Biophys Acta , vol.1804 , Issue.7 , pp. 1405-1412
    • Biancalana, M.1    Koide, S.2
  • 11
    • 51349128031 scopus 로고    scopus 로고
    • A regulatable switch mediates self-association in an immunoglobulin fold
    • CalabreseMF, Eakin CM, Wang JM,Miranker AD (2008) A regulatable switch mediates self-association in an immunoglobulin fold. Nat Struct Mol Biol 15(9):965-971.
    • (2008) Nat Struct Mol Biol , vol.15 , Issue.9 , pp. 965-971
    • Calabrese, M.F.1    Eakin, C.M.2    Wang, J.M.3    Miranker, A.D.4
  • 12
    • 55849088319 scopus 로고    scopus 로고
    • Regulation of MHC class I assembly and peptide binding
    • Peaper DR, Cresswell P (2008) Regulation of MHC class I assembly and peptide binding. Annu Rev Cell Dev Biol 24:343-368.
    • (2008) Annu Rev Cell Dev Biol , vol.24 , pp. 343-368
    • Peaper, D.R.1    Cresswell, P.2
  • 13
    • 2942748436 scopus 로고    scopus 로고
    • Oligomeric assembly of native-like precursors precedes amyloid formation by beta-2 microglobulin
    • Eakin CM, Attenello FJ, Morgan CJ, Miranker AD (2004) Oligomeric assembly of native-like precursors precedes amyloid formation by beta-2 microglobulin. Biochemistry 43(24):7808-7815.
    • (2004) Biochemistry , vol.43 , Issue.24 , pp. 7808-7815
    • Eakin, C.M.1    Attenello, F.J.2    Morgan, C.J.3    Miranker, A.D.4
  • 14
    • 0035367287 scopus 로고    scopus 로고
    • Kidney dialysis-associated amyloidosis: A molecular role for copper in fiber formation
    • DOI 10.1006/jmbi.2001.4661
    • Morgan CJ, Gelfand M, Atreya C, Miranker AD (2001) Kidney dialysis-associated amyloidosis: A molecular role for copper in fiber formation. J Mol Biol 309(2):339-345. (Pubitemid 32553492)
    • (2001) Journal of Molecular Biology , vol.309 , Issue.2 , pp. 339-345
    • Morgan, C.J.1    Gelfand, M.2    Atreya, C.3    Miranker, A.D.4
  • 15
    • 67650325176 scopus 로고    scopus 로고
    • The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: Insights from type II diabetes
    • Hebda JA, Miranker AD (2009) The interplay of catalysis and toxicity by amyloid intermediates on lipid bilayers: insights from type II diabetes. Ann Rev Biophys 38:125-152.
    • (2009) Ann Rev Biophys , vol.38 , pp. 125-152
    • Hebda, J.A.1    Miranker, A.D.2
  • 16
    • 33644813233 scopus 로고    scopus 로고
    • A native to amyloidogenic transition regulated by a backbone trigger
    • Eakin CM, Berman AJ, Miranker AD (2006) A native to amyloidogenic transition regulated by a backbone trigger. Nat Struct Mol Biol 13(3):202-208.
    • (2006) Nat Struct Mol Biol , vol.13 , Issue.3 , pp. 202-208
    • Eakin, C.M.1    Berman, A.J.2    Miranker, A.D.3
  • 17
    • 0028150789 scopus 로고
    • Three-dimensional structure of a peptide extending from one end of a class I MHC binding site
    • Collins EJ, Garboczi DN, Wiley DC (1994) Three-dimensional structure of a peptide extending from one end of a class I MHC binding site. Nature 371(6498):626-629.
    • (1994) Nature , vol.371 , Issue.6498 , pp. 626-629
    • Collins, E.J.1    Garboczi, D.N.2    Wiley, D.C.3
  • 21
    • 58149175632 scopus 로고    scopus 로고
    • Thioflavin T as a molecular rotor: Fluorescent properties of thioflavin T in solvents with different viscosity
    • Stsiapura VI, et al. (2008) Thioflavin T as a molecular rotor: Fluorescent properties of thioflavin T in solvents with different viscosity. J Phys Chem B 112(49):15893-15902.
    • (2008) J Phys Chem B , vol.112 , Issue.49 , pp. 15893-15902
    • Stsiapura, V.I.1
  • 22
    • 45749094206 scopus 로고    scopus 로고
    • Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin T acts as a sensitive fluorescent reporter of ligand binding to the acylation site
    • DOI 10.1021/ja7109822
    • Harel M, Sonoda LK, Silman I, Sussman JL, Rosenberry TL (2008) Crystal structure of thioflavin T bound to the peripheral site of Torpedo californica acetylcholinesterase reveals how thioflavin Tacts as a sensitive fluorescent reporter of ligand binding to the acylation site. J Am Chem Soc 130(25):7856-7861. (Pubitemid 351875060)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.25 , pp. 7856-7861
    • Harel, M.1    Sonoda, L.K.2    Silman, I.3    Sussman, J.L.4    Rosenberry, T.L.5
  • 23
    • 77649247193 scopus 로고    scopus 로고
    • Minimalist design of water-soluble cross-{beta} architecture
    • Biancalana M, Makabe K, Koide S (2010) Minimalist design of water-soluble cross-{beta} architecture. Proc Natl Acad Sci USA 107(8):3469-3474.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.8 , pp. 3469-3474
    • Biancalana, M.1    Makabe, K.2    Koide, S.3
  • 24
    • 84954358136 scopus 로고    scopus 로고
    • The binding of thioflavin T and its neutral analog BTA-1 to protofibrils of the Alzheimer's disease Abeta(16-22) peptide probed by molecular dynamics simulations
    • Wu C, et al. (2008) The binding of thioflavin T and its neutral analog BTA-1 to protofibrils of the Alzheimer's disease Abeta(16-22) peptide probed by molecular dynamics simulations. J Mol Biol 384(3):718-729.
    • (2008) J Mol Biol , vol.384 , Issue.3 , pp. 718-729
    • Wu, C.1
  • 26
    • 77649265357 scopus 로고    scopus 로고
    • Exploring the sequence determinants of amyloid structure using position-specific scoring matrices
    • Maurer-Stroh S, et al. (2010) Exploring the sequence determinants of amyloid structure using position-specific scoring matrices. Nat Methods 7:237-242.
    • (2010) Nat Methods , vol.7 , pp. 237-242
    • Maurer-Stroh, S.1
  • 27
    • 0142231517 scopus 로고    scopus 로고
    • Structural changes accompanying intramolecular electron transfer: Focus on twisted intramolecular charge-transfer states and structures
    • Grabowski ZR, Rotkiewicz K, Rettig W (2003) Structural changes accompanying intramolecular electron transfer: Focus on twisted intramolecular charge-transfer states and structures. Chem Rev 103(10):3899-4031.
    • (2003) Chem Rev , vol.103 , Issue.10 , pp. 3899-4031
    • Grabowski, Z.R.1    Rotkiewicz, K.2    Rettig, W.3
  • 28
    • 27944455577 scopus 로고    scopus 로고
    • Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: An induced circular dichroism/DFT study
    • DOI 10.1016/j.febslet.2005.10.048, PII S0014579305013177
    • Dzwolak W, Pecul M (2005) Chiral bias of amyloid fibrils revealed by the twisted conformation of Thioflavin T: An induced circular dichroism/DFT study. FEBS Lett 579(29):6601-6603. (Pubitemid 41682446)
    • (2005) FEBS Letters , vol.579 , Issue.29 , pp. 6601-6603
    • Dzwolak, W.1    Pecul, M.2
  • 29
    • 42749089759 scopus 로고    scopus 로고
    • Chiral bifurcation in aggregating insulin: An induced circular dichroism study
    • Loksztejn A, Dzwolak W (2008) Chiral bifurcation in aggregating insulin: An induced circular dichroism study. J Mol Biol 379(1):9-16.
    • (2008) J Mol Biol , vol.379 , Issue.1 , pp. 9-16
    • Loksztejn, A.1    Dzwolak, W.2
  • 30
    • 44549084117 scopus 로고    scopus 로고
    • On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2
    • Sabate R, Lascu I, Saupe SJ (2008) On the binding of Thioflavin-T to HET-s amyloid fibrils assembled at pH 2. J Struct Biol 162(3):387-396.
    • (2008) J Struct Biol , vol.162 , Issue.3 , pp. 387-396
    • Sabate, R.1    Lascu, I.2    Saupe, S.J.3
  • 32
    • 11144222595 scopus 로고    scopus 로고
    • The binding of thioflavin-T to amyloid fibrils: Localisation and implications
    • Krebs MR, Bromley EH, Donald AM (2005) The binding of thioflavin-T to amyloid fibrils: Localisation and implications. J Struct Biol 149(1):30-37.
    • (2005) J Struct Biol , vol.149 , Issue.1 , pp. 30-37
    • Krebs, M.R.1    Bromley, E.H.2    Donald, A.M.3
  • 33
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes by molecular replacement with Phaser
    • McCoy AJ (2007) Solving structures of protein complexes by molecular replacement with Phaser. Acta Crystallogr D 63(Pt 1):32-41.
    • (2007) Acta Crystallogr D , vol.63 , Issue.PART 1 , pp. 32-41
    • McCoy, A.J.1
  • 34
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov GN, Vagin AA, Dodson EJ (1997) Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D 53(Pt 3):240-255.
    • (1997) Acta Crystallogr D , vol.53 , Issue.PART 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 36
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: Programs for protein crystallography. Acta Crystallogr D 50(Pt 5):760-763.
    • (1994) Acta Crystallogr D , vol.50 , Issue.PART 5 , pp. 760-763
  • 37
    • 14244272868 scopus 로고    scopus 로고
    • PHENIX: Building new software for automated crystallographic structure determination
    • Adams PD, et al. (2002) PHENIX: Building new software for automated crystallographic structure determination. Acta Crystallogr D 58(Pt 11):1948-1954.
    • (2002) Acta Crystallogr D , vol.58 , Issue.PART 11 , pp. 1948-1954
    • Adams, P.D.1
  • 38
    • 84893169025 scopus 로고
    • General atomic and molecular electronic-structure system
    • Schmidt MW, et al. (1993) General atomic and molecular electronic-structure system. J Comput Chem 14(11):1347-1363.
    • (1993) J Comput Chem , vol.14 , Issue.11 , pp. 1347-1363
    • Schmidt, M.W.1
  • 39
    • 16444378435 scopus 로고
    • On the non-orthogonality problem connected with the use of atomic wave functions in the theory of molecules and crystals
    • Lowdin PO (1950) On the non-orthogonality problem connected with the use of atomic wave functions in the theory of molecules and crystals. J Chem Phys 18(3):365-375.
    • (1950) J Chem Phys , vol.18 , Issue.3 , pp. 365-375
    • Lowdin, P.O.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.