메뉴 건너뛰기




Volumn 30, Issue 13, 2014, Pages 3775-3786

Complexation of amyloid fibrils with charged conjugated polymers

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; ATOMIC FORCE MICROSCOPY; DYES; FUNCTIONAL POLYMERS; GLYCOPROTEINS;

EID: 84897985686     PISSN: 07437463     EISSN: 15205827     Source Type: Journal    
DOI: 10.1021/la404739f     Document Type: Article
Times cited : (34)

References (60)
  • 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
  • 2
    • 68649086842 scopus 로고    scopus 로고
    • Structure-activity relationship of amyloid fibrils
    • Maji, S. K.; Wang, L.; Greenwald, J.; Riek, R. Structure-activity relationship of amyloid fibrils FEBS Lett. 2009, 583, 2610-2617
    • (2009) FEBS Lett. , vol.583 , pp. 2610-2617
    • Maji, S.K.1    Wang, L.2    Greenwald, J.3    Riek, R.4
  • 3
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • Jarrett, J. T.; Lansbury, P. T., Jr Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? Cell 1993, 73, 1055-1058
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury, Jr.P.T.2
  • 4
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper, J. D.; Lansbury, P. T., Jr. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins Annu. Rev. Biochem. 1997, 66, 385-407
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, Jr.P.T.2
  • 5
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • Uversky, V. N.; Fink, A. L. Conformational constraints for amyloid fibrillation: the importance of being unfolded Biochim. Biophys. Acta 2004, 1698, 131-153
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2
  • 6
    • 0035941305 scopus 로고    scopus 로고
    • Stabilization of partially folded conformation during α-synuclein oligomerization in both purified and cytosolic preparations
    • Uversky, V. N.; Lee, H. J.; Li, J.; Fink, A. L.; Lee, S. J. Stabilization of partially folded conformation during α-synuclein oligomerization in both purified and cytosolic preparations J. Biol. Chem. 2001, 276, 43495-43498
    • (2001) J. Biol. Chem. , vol.276 , pp. 43495-43498
    • Uversky, V.N.1    Lee, H.J.2    Li, J.3    Fink, A.L.4    Lee, S.J.5
  • 7
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • Dobson, C. M. The structural basis of protein folding and its links with human disease Philos. Trans. R. Soc. London, B: Biol. Sci. 2001, 356, 133-145
    • (2001) Philos. Trans. R. Soc. London, B: Biol. Sci. , vol.356 , pp. 133-145
    • Dobson, C.M.1
  • 10
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and X-ray diffraction
    • Sunde, M.; Blake, C. The structure of amyloid fibrils by electron microscopy and X-ray diffraction Adv. Protein Chem. 1997, 50, 123-159
    • (1997) Adv. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 11
    • 0032849874 scopus 로고    scopus 로고
    • Quantification of β-sheet amyloid fibril structures with thioflavin T
    • LeVine, H., 3rd. Quantification of β-sheet amyloid fibril structures with thioflavin T Methods Enzymol. 1999, 309, 274-284
    • (1999) Methods Enzymol. , vol.309 , pp. 274-284
    • Levine III, H.1
  • 12
    • 0032855483 scopus 로고    scopus 로고
    • Quantifying amyloid by Congo red spectral shift assay
    • Klunk, W. E.; Jacob, R. F.; Mason, R. P. Quantifying amyloid by Congo red spectral shift assay Methods Enzymol. 1999, 309, 285-305
    • (1999) Methods Enzymol. , vol.309 , pp. 285-305
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 13
    • 2542455537 scopus 로고    scopus 로고
    • Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer's disease
    • Klein, W. L.; Stine, W. B., Jr.; Teplow, D. B. Small assemblies of unmodified amyloid β-protein are the proximate neurotoxin in Alzheimer's disease Neurobiol. Aging 2004, 25, 569-580
    • (2004) Neurobiol. Aging , vol.25 , pp. 569-580
    • Klein, W.L.1    Stine, Jr.W.B.2    Teplow, D.B.3
  • 14
    • 33750365052 scopus 로고    scopus 로고
    • Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins?
    • Lashuel, H. A.; Lansbury, P. T., Jr. Are amyloid diseases caused by protein aggregates that mimic bacterial pore-forming toxins? Q. Rev. Biophys. 2006, 39, 167-201
    • (2006) Q. Rev. Biophys. , vol.39 , pp. 167-201
    • Lashuel, H.A.1    Lansbury, Jr.P.T.2
  • 16
    • 22244442489 scopus 로고    scopus 로고
    • The biochemistry of Parkinson's disease
    • Cookson, M. R. The biochemistry of Parkinson's disease Annu. Rev. Biochem. 2005, 74, 29-52
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 29-52
    • Cookson, M.R.1
  • 17
    • 0036775723 scopus 로고    scopus 로고
    • Genetics of Parkinson's disease and biochemical studies of implicated gene products - Commentary
    • Lansbury, P. T.; Brice, A. Genetics of Parkinson's disease and biochemical studies of implicated gene products-Commentary Curr. Opin. Cell Biol. 2002, 14, 653-660
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 653-660
    • Lansbury, P.T.1    Brice, A.2
  • 18
    • 0033782907 scopus 로고    scopus 로고
    • Studying human neurodegenerative diseases in flies and worms
    • Feany, M. B. Studying human neurodegenerative diseases in flies and worms J. Neuropath. Exp. Neurol. 2000, 59, 847-856
    • (2000) J. Neuropath. Exp. Neurol. , vol.59 , pp. 847-856
    • Feany, M.B.1
  • 19
    • 0028277520 scopus 로고
    • Identification of two distinct synucleins from human brain
    • Jakes, R.; Spillantini, M. G.; Goedert, M. Identification of two distinct synucleins from human brain FEBS Lett. 1994, 345, 27-32
    • (1994) FEBS Lett. , vol.345 , pp. 27-32
    • Jakes, R.1    Spillantini, M.G.2    Goedert, M.3
  • 20
    • 84884250340 scopus 로고    scopus 로고
    • The function of α-synuclein
    • Bendor, J. T.; Logan, T. P.; Edwards, R. H. The function of α-synuclein Neuron 2013, 79, 1044-1066
    • (2013) Neuron , vol.79 , pp. 1044-1066
    • Bendor, J.T.1    Logan, T.P.2    Edwards, R.H.3
  • 21
    • 84871414210 scopus 로고    scopus 로고
    • The many faces of α-synuclein: From structure and toxicity to therapeutic target
    • Lashuel, H. A.; Overk, C. R.; Oueslati, A.; Masliah, E. The many faces of α-synuclein: from structure and toxicity to therapeutic target Nat. Rev. Neurosci. 2013, 14, 38-48
    • (2013) Nat. Rev. Neurosci. , vol.14 , pp. 38-48
    • Lashuel, H.A.1    Overk, C.R.2    Oueslati, A.3    Masliah, E.4
  • 22
    • 34548620297 scopus 로고    scopus 로고
    • Neuropathology, biochemistry, and biophysics of α-synuclein aggregation
    • Uversky, V. N. Neuropathology, biochemistry, and biophysics of α-synuclein aggregation J. Neurochem. 2007, 103, 17-37
    • (2007) J. Neurochem. , vol.103 , pp. 17-37
    • Uversky, V.N.1
  • 23
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • Conway, K. A.; Lee, S. J.; Rochet, J. C.; Ding, T. T.; Williamson, R. E.; Lansbury, P. T. Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy Proc. Natl. Acad. Sci. U.S.A. 2000, 97, 571-576
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 24
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of α-synuclein secondary structure upon binding to synthetic membranes
    • Davidson, W. S.; Jonas, A.; Clayton, D. F.; George, J. M. Stabilization of α-synuclein secondary structure upon binding to synthetic membranes J. Biol. Chem. 1998, 273, 9443-9449
    • (1998) J. Biol. Chem. , vol.273 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 25
    • 2942555022 scopus 로고    scopus 로고
    • Structure of membrane-bound α-synuclein studied by site-directed spin labeling
    • Jao, C. C.; Der-Sarkissian, A.; Chen, J.; Langen, R. Structure of membrane-bound α-synuclein studied by site-directed spin labeling Proc. Natl. Acad. Sci. U.S.A. 2004, 101, 8331-8336
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 8331-8336
    • Jao, C.C.1    Der-Sarkissian, A.2    Chen, J.3    Langen, R.4
  • 27
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR
    • Heise, H. H. W.; Becker, S.; Andronesi, O. C.; Riedel, D.; Baldus, M. Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR Proc. Natl. Acad. Sci. U.S.A. 2005, 102, 15871-15876
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 15871-15876
    • Heise, H.H.W.1    Becker, S.2    Andronesi, O.C.3    Riedel, D.4    Baldus, M.5
  • 29
    • 0037022186 scopus 로고    scopus 로고
    • Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α-synuclein in vitro
    • Cohlberg, J. A.; Li, J.; Uversky, V. N.; Fink, A. L. Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from α-synuclein in vitro Biochemistry 2002, 41, 1502-1511
    • (2002) Biochemistry , vol.41 , pp. 1502-1511
    • Cohlberg, J.A.1    Li, J.2    Uversky, V.N.3    Fink, A.L.4
  • 31
    • 84890504484 scopus 로고    scopus 로고
    • Characterization of Amyloid Formation by Glucagon-Like Peptides: Role of Basic Residues in Heparin-Mediated Aggregation
    • Jha, N. N.; Anoop, A.; Ranganathan, S.; Mohite, G. M.; Padinhateeri, R.; Maji, S. K. Characterization of Amyloid Formation by Glucagon-Like Peptides: Role of Basic Residues in Heparin-Mediated Aggregation Biochemistry 2013, 52, 8800-8810
    • (2013) Biochemistry , vol.52 , pp. 8800-8810
    • Jha, N.N.1    Anoop, A.2    Ranganathan, S.3    Mohite, G.M.4    Padinhateeri, R.5    Maji, S.K.6
  • 35
    • 84864622893 scopus 로고    scopus 로고
    • A pentameric luminescent-conjugated oligothiophene for optical imaging of in vitro-formed amyloid fibrils and protein aggregates in tissue sections
    • Nilsson, K. P.; Lindgren, M.; Hammarstrom, P. A pentameric luminescent-conjugated oligothiophene for optical imaging of in vitro-formed amyloid fibrils and protein aggregates in tissue sections Methods Mol. Biol. 2012, 849, 425-434
    • (2012) Methods Mol. Biol. , vol.849 , pp. 425-434
    • Nilsson, K.P.1    Lindgren, M.2    Hammarstrom, P.3
  • 38
    • 0042838375 scopus 로고    scopus 로고
    • Self-assembly of synthetic peptides control conformation and optical properties of a zwitterionic polythiophene derivative
    • Nilsson, K. P.; Rydberg, J.; Baltzer, L.; Inganas, O. Self-assembly of synthetic peptides control conformation and optical properties of a zwitterionic polythiophene derivative Proc. Natl. Acad. Sci. U.S.A. 2003, 100, 10170-10174
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 10170-10174
    • Nilsson, K.P.1    Rydberg, J.2    Baltzer, L.3    Inganas, O.4
  • 39
    • 20644462783 scopus 로고    scopus 로고
    • Electroactive Luminescent Self-assembled Bio-Organic Nanowires: Integration of Semiconducting Oligoelectrolytes within Amyloidogenic Proteins
    • Herland, A.; Bjork, P.; Nilsson, K. P.; Olsson, J. D.; Asberg, P.; Konradsson, P.; Hammarstrom, P.; Inganas, O. Electroactive Luminescent Self-assembled Bio-Organic Nanowires:Integration of Semiconducting Oligoelectrolytes within Amyloidogenic Proteins Adv. Mater. 2005, 17, 1466-1471
    • (2005) Adv. Mater. , vol.17 , pp. 1466-1471
    • Herland, A.1    Bjork, P.2    Nilsson, K.P.3    Olsson, J.D.4    Asberg, P.5    Konradsson, P.6    Hammarstrom, P.7    Inganas, O.8
  • 40
    • 84887073423 scopus 로고    scopus 로고
    • Conjugated Polyfluorene-based Reversible Fluorescent Sensor for Cu(II) and Cyanide Ions in Aqueous Medium
    • Chakraborty, C.; Singh, P.; Maji, S. K.; Malik, S. Conjugated Polyfluorene-based Reversible Fluorescent Sensor for Cu(II) and Cyanide Ions in Aqueous Medium Chem. Lett. 2013, 42, 1355-1357
    • (2013) Chem. Lett. , vol.42 , pp. 1355-1357
    • Chakraborty, C.1    Singh, P.2    Maji, S.K.3    Malik, S.4
  • 41
    • 34248332079 scopus 로고    scopus 로고
    • Chemical sensors based on amplifying fluorescent conjugated polymers
    • Thomas, S. W., III; Joly, G. D.; Swager, T. M. Chemical sensors based on amplifying fluorescent conjugated polymers Chem. Rev. 2007, 107, 1339-1386
    • (2007) Chem. Rev. , vol.107 , pp. 1339-1386
    • Thomas III, S.W.1    Joly, G.D.2    Swager, T.M.3
  • 42
    • 84855847029 scopus 로고    scopus 로고
    • Immobilization of poly(fluorene) within clay nanocomposite: An easy way to control keto defect
    • Chakraborty, C.; Dana, K.; Malik, S. Immobilization of poly(fluorene) within clay nanocomposite: an easy way to control keto defect J. Colloid Interface Sci. 2012, 368, 172-180
    • (2012) J. Colloid Interface Sci. , vol.368 , pp. 172-180
    • Chakraborty, C.1    Dana, K.2    Malik, S.3
  • 43
    • 33846817163 scopus 로고    scopus 로고
    • Relationships between the Sequence of α-Synuclein and its Membrane Affinity, Fibrillization Propensity, and Yeast Toxicity
    • Volles, M. J.; Lansbury, P. T., Jr. Relationships between the Sequence of α-Synuclein and its Membrane Affinity, Fibrillization Propensity, and Yeast Toxicity J. Mol. Biol. 2007, 366, 1510-1522
    • (2007) J. Mol. Biol. , vol.366 , pp. 1510-1522
    • Volles, M.J.1    Lansbury, Jr.P.T.2
  • 48
    • 0041825430 scopus 로고    scopus 로고
    • Mixtures of wild-type and a pathogenic (E22G) form of Aβ40 in vitro accumulate protofibrils, including amyloid pores
    • Lashuel, H. A.; Hartley, D. M.; Petre, B. M.; Wall, J. S.; Simon, M. N.; Walz, T.; Lansbury, P. T. Mixtures of wild-type and a pathogenic (E22G) form of Aβ40 in vitro accumulate protofibrils, including amyloid pores J. Mol. Biol. 2003, 332, 795-808
    • (2003) J. Mol. Biol. , vol.332 , pp. 795-808
    • Lashuel, H.A.1    Hartley, D.M.2    Petre, B.M.3    Wall, J.S.4    Simon, M.N.5    Walz, T.6    Lansbury, P.T.7
  • 49
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • Whitmore, L.; Wallace, B. A. Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases Biopolymers 2008, 89, 392-400
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 51
    • 39749112546 scopus 로고    scopus 로고
    • Fitting neurological protein aggregation kinetic data via a 2-step, minimal/"Ockham's razor" model: The Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth
    • Morris, A. M.; Watzky, M. A.; Agar, J. N.; Finke, R. G. Fitting neurological protein aggregation kinetic data via a 2-step, minimal/ "Ockham's razor" model: the Finke-Watzky mechanism of nucleation followed by autocatalytic surface growth Biochemistry 2008, 47, 2413-2427
    • (2008) Biochemistry , vol.47 , pp. 2413-2427
    • Morris, A.M.1    Watzky, M.A.2    Agar, J.N.3    Finke, R.G.4
  • 52
    • 34548165708 scopus 로고    scopus 로고
    • Infrared spectroscopy of proteins
    • Barth, A. Infrared spectroscopy of proteins Biochim. Biophys. Acta 2007, 1767, 1073-1101
    • (2007) Biochim. Biophys. Acta , vol.1767 , pp. 1073-1101
    • Barth, A.1
  • 53
    • 27744577906 scopus 로고    scopus 로고
    • FT-IR approaches on amyloid fibril structure
    • Hiramatsu, H.; Kitagawa, T. FT-IR approaches on amyloid fibril structure Biochim. Biophys. Acta 2005, 1753, 100-107
    • (2005) Biochim. Biophys. Acta , vol.1753 , pp. 100-107
    • Hiramatsu, H.1    Kitagawa, T.2
  • 54
    • 84865560144 scopus 로고    scopus 로고
    • Amyloid-like fibril formation by tachykinin neuropeptides and its relevance to amyloid β-protein aggregation and toxicity
    • Singh, P. K.; Maji, S. K. Amyloid-like fibril formation by tachykinin neuropeptides and its relevance to amyloid β-protein aggregation and toxicity Cell Biochem. Biophys. 2012, 64, 29-44
    • (2012) Cell Biochem. Biophys. , vol.64 , pp. 29-44
    • Singh, P.K.1    Maji, S.K.2
  • 55
    • 0021061819 scopus 로고
    • Rapid colorimetric assay for cellular growth and survival: Application to proliferation and cytotoxicity assays
    • Mosmann, T. Rapid colorimetric assay for cellular growth and survival: application to proliferation and cytotoxicity assays J. Immunol. Methods 1983, 65, 55-63
    • (1983) J. Immunol. Methods , vol.65 , pp. 55-63
    • Mosmann, T.1
  • 57
    • 84890843811 scopus 로고    scopus 로고
    • Trypsin inhibitor complexes with human and bovine serum albumins: TEM and spectroscopic analysis
    • Hebia, C.; Bekale, L.; Chanphai, P.; Agbebavi, J.; Tajmir-Riahi, H. A. Trypsin inhibitor complexes with human and bovine serum albumins: TEM and spectroscopic analysis J. Photochem. Photobiol. B 2013, 130C, 254-259
    • (2013) J. Photochem. Photobiol. B , vol.130 , pp. 254-259
    • Hebia, C.1    Bekale, L.2    Chanphai, P.3    Agbebavi, J.4    Tajmir-Riahi, H.A.5
  • 59
    • 33750430630 scopus 로고    scopus 로고
    • Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Aβ42 peptide
    • Kim, W.; Hecht, M. H. Generic hydrophobic residues are sufficient to promote aggregation of the Alzheimer's Aβ42 peptide Proc. Natl. Acad. Sci. U.S.A. 2006, 103, 15824-15829
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 15824-15829
    • Kim, W.1    Hecht, M.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.