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Volumn 124, Issue , 2016, Pages 1105-1120

Protein aggregation and neurodegenerative diseases: From theory to therapy

Author keywords

Cell toxicity; Drug target; Misfolding and aggregation; Neurodegenerative diseases; Therapeutic intervention

Indexed keywords

PROTEIN AGGREGATE;

EID: 84995581912     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1016/j.ejmech.2016.07.054     Document Type: Article
Times cited : (124)

References (279)
  • 1
    • 33746099650 scopus 로고    scopus 로고
    • Protein aggregation in crowded environments
    • [1] Ellis, R.J., Minton, A.P., Protein aggregation in crowded environments. Biol. Chem. 387 (2006), 485–497.
    • (2006) Biol. Chem. , vol.387 , pp. 485-497
    • Ellis, R.J.1    Minton, A.P.2
  • 2
    • 0034254189 scopus 로고    scopus 로고
    • Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell
    • [2] van den Berg, B., Wain, R., Dobson, C.M., Ellis, R.J., Macromolecular crowding perturbs protein refolding kinetics: implications for folding inside the cell. EMBO J. 19 (2000), 3870–3875.
    • (2000) EMBO J. , vol.19 , pp. 3870-3875
    • van den Berg, B.1    Wain, R.2    Dobson, C.M.3    Ellis, R.J.4
  • 3
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • [3] Hartl, F.U., Molecular chaperones in cellular protein folding. Nature 381 (1996), 571–579.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 4
    • 0037040541 scopus 로고    scopus 로고
    • Molecular chaperones in the cytosol: from nascent chain to folded protein
    • [4] Hartl, F.U., Hayer-Hartl, M., Molecular chaperones in the cytosol: from nascent chain to folded protein. Science 295 (2002), 1852–1858.
    • (2002) Science , vol.295 , pp. 1852-1858
    • Hartl, F.U.1    Hayer-Hartl, M.2
  • 5
    • 84863903065 scopus 로고    scopus 로고
    • Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis
    • [5] Lindquist, S.L., Kelly, J.W., Chemical and biological approaches for adapting proteostasis to ameliorate protein misfolding and aggregation diseases: progress and prognosis. Cold Spring Harb. Perspect. Biol., 3, 2011.
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3
    • Lindquist, S.L.1    Kelly, J.W.2
  • 7
    • 39349083915 scopus 로고    scopus 로고
    • Adapting proteostasis for disease intervention
    • [7] Balch, W.E., Morimoto, R.I., Dillin, A., Kelly, J.W., Adapting proteostasis for disease intervention. Science 319 (2008), 916–919.
    • (2008) Science , vol.319 , pp. 916-919
    • Balch, W.E.1    Morimoto, R.I.2    Dillin, A.3    Kelly, J.W.4
  • 8
    • 46749117136 scopus 로고    scopus 로고
    • Molecular and cellular aspects of protein misfolding and disease
    • [8] Herczenik, E., Gebbink, M.F., Molecular and cellular aspects of protein misfolding and disease. FASEB J. 22 (2008), 2115–2133.
    • (2008) FASEB J. , vol.22 , pp. 2115-2133
    • Herczenik, E.1    Gebbink, M.F.2
  • 9
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • [9] Chiti, F., Dobson, C.M., Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem. 75 (2006), 333–366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 10
    • 77953667076 scopus 로고    scopus 로고
    • Neurodegenerative diseases: lessons from genome-wide screens in small model organisms
    • [10] van Ham, T.J., Breitling, R., Swertz, M.A., Nollen, E.A., Neurodegenerative diseases: lessons from genome-wide screens in small model organisms. EMBO Mol. Med. 1 (2009), 360–370.
    • (2009) EMBO Mol. Med. , vol.1 , pp. 360-370
    • van Ham, T.J.1    Breitling, R.2    Swertz, M.A.3    Nollen, E.A.4
  • 11
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • [11] Soto, C., Unfolding the role of protein misfolding in neurodegenerative diseases. Nat. Rev. Neurosci. 4 (2003), 49–60.
    • (2003) Nat. Rev. Neurosci. , vol.4 , pp. 49-60
    • Soto, C.1
  • 12
    • 3142514201 scopus 로고    scopus 로고
    • Protein aggregation and neurodegenerative disease
    • [12] Ross, C.A., Poirier, M.A., Protein aggregation and neurodegenerative disease. Nat. Med. 10:Suppl. (2004), S10–S17.
    • (2004) Nat. Med. , vol.10 , pp. S10-S17
    • Ross, C.A.1    Poirier, M.A.2
  • 13
    • 33645728523 scopus 로고    scopus 로고
    • Neurodegenerative diseases: new concepts of pathogenesis and their therapeutic implications
    • [13] Skovronsky, D.M., Lee, V.M., Trojanowski, J.Q., Neurodegenerative diseases: new concepts of pathogenesis and their therapeutic implications. Annu. Rev. Pathol. 1 (2006), 151–170.
    • (2006) Annu. Rev. Pathol. , vol.1 , pp. 151-170
    • Skovronsky, D.M.1    Lee, V.M.2    Trojanowski, J.Q.3
  • 14
    • 7044238416 scopus 로고    scopus 로고
    • Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs
    • [14] Forman, M.S., Trojanowski, J.Q., Lee, V.M., Neurodegenerative diseases: a decade of discoveries paves the way for therapeutic breakthroughs. Nat. Med. 10 (2004), 1055–1063.
    • (2004) Nat. Med. , vol.10 , pp. 1055-1063
    • Forman, M.S.1    Trojanowski, J.Q.2    Lee, V.M.3
  • 15
    • 84918572107 scopus 로고    scopus 로고
    • Characterization of pre-molten globule state of yeast iso-1-cytochrome c and its deletants at pH 6.0 and 25 degrees C
    • [15] Haque, M.A., Ubaid-Ullah, S., Zaidi, S., Hassan, M.I., Islam, A., Batra, J.K., Ahmad, F., Characterization of pre-molten globule state of yeast iso-1-cytochrome c and its deletants at pH 6.0 and 25 degrees C. Int. J. Biol. Macromol. 72 (2015), 1406–1418.
    • (2015) Int. J. Biol. Macromol. , vol.72 , pp. 1406-1418
    • Haque, M.A.1    Ubaid-Ullah, S.2    Zaidi, S.3    Hassan, M.I.4    Islam, A.5    Batra, J.K.6    Ahmad, F.7
  • 16
    • 84939967481 scopus 로고    scopus 로고
    • In vitro and in silico studies of urea-induced denaturation of yeast iso-1-cytochrome c and its deletants at pH 6.0 and 25 degrees C
    • [16] Haque, M.A., Zaidi, S., Ubaid-Ullah, S., Prakash, A., Hassan, M.I., Islam, A., Batra, J.K., Ahmad, F., In vitro and in silico studies of urea-induced denaturation of yeast iso-1-cytochrome c and its deletants at pH 6.0 and 25 degrees C. J. Biomol. Struct. Dyn. 33 (2014), 1493–1502.
    • (2014) J. Biomol. Struct. Dyn. , vol.33 , pp. 1493-1502
    • Haque, M.A.1    Zaidi, S.2    Ubaid-Ullah, S.3    Prakash, A.4    Hassan, M.I.5    Islam, A.6    Batra, J.K.7    Ahmad, F.8
  • 17
    • 85018173503 scopus 로고    scopus 로고
    • Denatured states of yeast cytochrome c induced by heat and guanidinium chloride are structurally and thermodynamically different
    • [17] Zaidi, S., Haque, M.A., Ubaid-Ullah, S., Prakash, A., Hassan, M.I., Islam, A., Batra, J.K., Ahmad, F., Denatured states of yeast cytochrome c induced by heat and guanidinium chloride are structurally and thermodynamically different. J. Biomol. Struct. Dyn., 2016, 1–16.
    • (2016) J. Biomol. Struct. Dyn. , pp. 1-16
    • Zaidi, S.1    Haque, M.A.2    Ubaid-Ullah, S.3    Prakash, A.4    Hassan, M.I.5    Islam, A.6    Batra, J.K.7    Ahmad, F.8
  • 18
    • 84892821358 scopus 로고    scopus 로고
    • The role of key residues in structure, function, and stability of cytochrome-c
    • [18] Zaidi, S., Hassan, M.I., Islam, A., Ahmad, F., The role of key residues in structure, function, and stability of cytochrome-c. Cell Mol. Life Sci. 71 (2014), 229–255.
    • (2014) Cell Mol. Life Sci. , vol.71 , pp. 229-255
    • Zaidi, S.1    Hassan, M.I.2    Islam, A.3    Ahmad, F.4
  • 19
    • 0021256895 scopus 로고
    • Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • [19] Glenner, G.G., Wong, C.W., Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem. Biophys. Res. Commun. 120 (1984), 885–890.
    • (1984) Biochem. Biophys. Res. Commun. , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 20
    • 0025904444 scopus 로고
    • A68: a major subunit of paired helical filaments and derivatized forms of normal Tau
    • [20] Lee, V.M., Balin, B.J., Otvos, L. Jr., Trojanowski, J.Q., A68: a major subunit of paired helical filaments and derivatized forms of normal Tau. Science 251 (1991), 675–678.
    • (1991) Science , vol.251 , pp. 675-678
    • Lee, V.M.1    Balin, B.J.2    Otvos, L.3    Trojanowski, J.Q.4
  • 21
    • 0038460184 scopus 로고    scopus 로고
    • Part II: alpha-synuclein and its molecular pathophysiological role in neurodegenerative disease
    • [21] Dev, K.K., Hofele, K., Barbieri, S., Buchman, V.L., van der Putten, H., Part II: alpha-synuclein and its molecular pathophysiological role in neurodegenerative disease. Neuropharmacology 45 (2003), 14–44.
    • (2003) Neuropharmacology , vol.45 , pp. 14-44
    • Dev, K.K.1    Hofele, K.2    Barbieri, S.3    Buchman, V.L.4    van der Putten, H.5
  • 22
    • 0035902194 scopus 로고    scopus 로고
    • Shattuck lecture–neurodegenerative diseases and prions
    • [22] Prusiner, S.B., Shattuck lecture–neurodegenerative diseases and prions. N. Engl. J. Med. 344 (2001), 1516–1526.
    • (2001) N. Engl. J. Med. , vol.344 , pp. 1516-1526
    • Prusiner, S.B.1
  • 23
    • 0032824836 scopus 로고    scopus 로고
    • Polyglutamine diseases: protein cleavage and aggregation
    • [23] Zoghbi, H.Y., Orr, H.T., Polyglutamine diseases: protein cleavage and aggregation. Curr. Opin. Neurobiol. 9 (1999), 566–570.
    • (1999) Curr. Opin. Neurobiol. , vol.9 , pp. 566-570
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 24
    • 22244479388 scopus 로고    scopus 로고
    • Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis
    • [24] Valentine, J.S., Doucette, P.A., Zittin Potter, S., Copper-zinc superoxide dismutase and amyotrophic lateral sclerosis. Annu. Rev. Biochem. 74 (2005), 563–593.
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 563-593
    • Valentine, J.S.1    Doucette, P.A.2    Zittin Potter, S.3
  • 25
    • 84976332555 scopus 로고
    • Delineating the relationship between amyotrophic lateral sclerosis and frontotemporal dementia: sequence and structure-based predictions
    • [25] Kumar, V., Islam, A., Hassan, M.I., Ahmad, F., Delineating the relationship between amyotrophic lateral sclerosis and frontotemporal dementia: sequence and structure-based predictions. Biochim. Biophys. Acta, 1862, 1742–1754.
    • (1862) Biochim. Biophys. Acta , pp. 1742-1754
    • Kumar, V.1    Islam, A.2    Hassan, M.I.3    Ahmad, F.4
  • 26
    • 84901921614 scopus 로고    scopus 로고
    • The triple power of D(3): protein intrinsic disorder in degenerative diseases
    • [26] Uversky, V.N., The triple power of D(3): protein intrinsic disorder in degenerative diseases. Front. Biosci. (Landmark Ed). 19 (2014), 181–258.
    • (2014) Front. Biosci. (Landmark Ed). , vol.19 , pp. 181-258
    • Uversky, V.N.1
  • 28
    • 45449091418 scopus 로고    scopus 로고
    • Amyloidogenesis of natively unfolded proteins
    • [28] Uversky, V.N., Amyloidogenesis of natively unfolded proteins. Curr. Alzheimer Res. 5 (2008), 260–287.
    • (2008) Curr. Alzheimer Res. , vol.5 , pp. 260-287
    • Uversky, V.N.1
  • 29
    • 48249097986 scopus 로고    scopus 로고
    • Intrinsically disordered proteins in human diseases: introducing the D2 concept
    • [29] Uversky, V.N., Oldfield, C.J., Dunker, A.K., Intrinsically disordered proteins in human diseases: introducing the D2 concept. Annu. Rev. Biophys. 37 (2008), 215–246.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 215-246
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 30
    • 82655179908 scopus 로고    scopus 로고
    • Disease mutations in disordered regions–exception to the rule?
    • [30] Vacic, V., Iakoucheva, L.M., Disease mutations in disordered regions–exception to the rule?. Mol. Biosyst. 8 (2012), 27–32.
    • (2012) Mol. Biosyst. , vol.8 , pp. 27-32
    • Vacic, V.1    Iakoucheva, L.M.2
  • 31
    • 1542358787 scopus 로고    scopus 로고
    • Prediction and functional analysis of native disorder in proteins from the three kingdoms of life
    • [31] Ward, J.J., Sodhi, J.S., McGuffin, L.J., Buxton, B.F., Jones, D.T., Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J. Mol. Biol. 337 (2004), 635–645.
    • (2004) J. Mol. Biol. , vol.337 , pp. 635-645
    • Ward, J.J.1    Sodhi, J.S.2    McGuffin, L.J.3    Buxton, B.F.4    Jones, D.T.5
  • 33
    • 84978852699 scopus 로고    scopus 로고
    • Molecular basis of the structural stability of hemochromatosis factor E: a combined molecular dynamic simulation and GdmCl-induced denaturation study
    • [33] Khan, P., Parkash, A., Islam, A., Ahmad, F., Hassan, M.I., Molecular basis of the structural stability of hemochromatosis factor E: a combined molecular dynamic simulation and GdmCl-induced denaturation study. Biopolymers 105 (2016), 133–142.
    • (2016) Biopolymers , vol.105 , pp. 133-142
    • Khan, P.1    Parkash, A.2    Islam, A.3    Ahmad, F.4    Hassan, M.I.5
  • 34
    • 84973868172 scopus 로고    scopus 로고
    • Effect of pH on the structure, function, and stability of human calcium/calmodulin-dependent protein kinase IV: combined spectroscopic and MD simulation studies
    • [34] Naz, H., Shahbaaz, M., Bisetty, K., Islam, A., Ahmad, F., Hassan, M.I., Effect of pH on the structure, function, and stability of human calcium/calmodulin-dependent protein kinase IV: combined spectroscopic and MD simulation studies. Biochem. Cell Biol. 94 (2016), 221–228.
    • (2016) Biochem. Cell Biol. , vol.94 , pp. 221-228
    • Naz, H.1    Shahbaaz, M.2    Bisetty, K.3    Islam, A.4    Ahmad, F.5    Hassan, M.I.6
  • 35
    • 85013423671 scopus 로고    scopus 로고
    • Urea-induced denaturation of human calcium/calmodulin-dependent protein kinase IV: a combined spectroscopic and MD simulation studies
    • [35] Naz, H., Shahbaaz, M., Haque, M.A., Bisetty, K., Islam, A., Ahmad, F., Hassan, M.I., Urea-induced denaturation of human calcium/calmodulin-dependent protein kinase IV: a combined spectroscopic and MD simulation studies. J. Biomol. Struct. Dyn., 2016, 1–13.
    • (2016) J. Biomol. Struct. Dyn. , pp. 1-13
    • Naz, H.1    Shahbaaz, M.2    Haque, M.A.3    Bisetty, K.4    Islam, A.5    Ahmad, F.6    Hassan, M.I.7
  • 36
    • 84928895487 scopus 로고    scopus 로고
    • Heterogeneity of equilibrium molten globule state of cytochrome c induced by weak salt denaturants under physiological condition
    • [36] Rahaman, H., Alam Khan, M.K., Hassan, M.I., Islam, A., Moosavi-Movahedi, A.A., Ahmad, F., Heterogeneity of equilibrium molten globule state of cytochrome c induced by weak salt denaturants under physiological condition. PLoS One, 10, 2015, e0120465.
    • (2015) PLoS One , vol.10 , pp. e0120465
    • Rahaman, H.1    Alam Khan, M.K.2    Hassan, M.I.3    Islam, A.4    Moosavi-Movahedi, A.A.5    Ahmad, F.6
  • 37
    • 79956130432 scopus 로고    scopus 로고
    • Structural diversity of class I MHC-like molecules and its implications in binding specificities
    • [37] Hassan, I., Ahmad, F., Structural diversity of class I MHC-like molecules and its implications in binding specificities. Adv. Protein Chem. Struct. Biol. 83 (2011), 223–270.
    • (2011) Adv. Protein Chem. Struct. Biol. , vol.83 , pp. 223-270
    • Hassan, I.1    Ahmad, F.2
  • 38
    • 84938964674 scopus 로고    scopus 로고
    • Structural characterization of MG and pre-MG states of proteins by MD simulations, NMR, and other techniques
    • [38] Naiyer, A., Hassan, M.I., Islam, A., Sundd, M., Ahmad, F., Structural characterization of MG and pre-MG states of proteins by MD simulations, NMR, and other techniques. J. Biomol. Struct. Dyn. 33 (2015), 2267–2284.
    • (2015) J. Biomol. Struct. Dyn. , vol.33 , pp. 2267-2284
    • Naiyer, A.1    Hassan, M.I.2    Islam, A.3    Sundd, M.4    Ahmad, F.5
  • 39
    • 66849106554 scopus 로고    scopus 로고
    • An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms
    • [39] Bartlett, A.I., Radford, S.E., An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms. Nat. Struct. Mol. Biol. 16 (2009), 582–588.
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 582-588
    • Bartlett, A.I.1    Radford, S.E.2
  • 40
    • 34548200331 scopus 로고    scopus 로고
    • Protein folding and misfolding inside and outside the cell
    • [40] Dobson, C.M., Ellis, R.J., Protein folding and misfolding inside and outside the cell. EMBO J. 17 (1998), 5251–5254.
    • (1998) EMBO J. , vol.17 , pp. 5251-5254
    • Dobson, C.M.1    Ellis, R.J.2
  • 41
    • 36749078792 scopus 로고    scopus 로고
    • Folding versus aggregation: polypeptide conformations on competing pathways
    • [41] Jahn, T.R., Radford, S.E., Folding versus aggregation: polypeptide conformations on competing pathways. Arch. Biochem. Biophys. 469 (2008), 100–117.
    • (2008) Arch. Biochem. Biophys. , vol.469 , pp. 100-117
    • Jahn, T.R.1    Radford, S.E.2
  • 42
    • 0009586942 scopus 로고    scopus 로고
    • Understanding protein folding via free-energy surfaces from theory and experiment
    • [42] Dinner, A.R., Sali, A., Smith, L.J., Dobson, C.M., Karplus, M., Understanding protein folding via free-energy surfaces from theory and experiment. Trends Biochem. Sci. 25 (2000), 331–339.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 331-339
    • Dinner, A.R.1    Sali, A.2    Smith, L.J.3    Dobson, C.M.4    Karplus, M.5
  • 43
    • 28244437028 scopus 로고    scopus 로고
    • The Yin and Yang of protein folding
    • [43] Jahn, T.R., Radford, S.E., The Yin and Yang of protein folding. FEBS J. 272 (2005), 5962–5970.
    • (2005) FEBS J. , vol.272 , pp. 5962-5970
    • Jahn, T.R.1    Radford, S.E.2
  • 44
    • 0035827318 scopus 로고    scopus 로고
    • Protein misfolding and disease; protein refolding and therapy
    • [44] Soto, C., Protein misfolding and disease; protein refolding and therapy. FEBS Lett. 498 (2001), 204–207.
    • (2001) FEBS Lett. , vol.498 , pp. 204-207
    • Soto, C.1
  • 45
    • 0029981197 scopus 로고    scopus 로고
    • Alternative conformations of amyloidogenic proteins govern their behavior
    • [45] Kelly, J.W., Alternative conformations of amyloidogenic proteins govern their behavior. Curr. Opin. Struct. Biol. 6 (1996), 11–17.
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 11-17
    • Kelly, J.W.1
  • 46
    • 0035916279 scopus 로고    scopus 로고
    • Amyloid-induced aggregation and precipitation of soluble proteins: an electrostatic contribution of the Alzheimer's beta(25-35) amyloid fibril
    • [46] Konno, T., Amyloid-induced aggregation and precipitation of soluble proteins: an electrostatic contribution of the Alzheimer's beta(25-35) amyloid fibril. Biochemistry 40 (2001), 2148–2154.
    • (2001) Biochemistry , vol.40 , pp. 2148-2154
    • Konno, T.1
  • 47
    • 0037155826 scopus 로고    scopus 로고
    • A designed system for assessing how sequence affects alpha to beta conformational transitions in proteins
    • [47] Ciani, B., Hutchinson, E.G., Sessions, R.B., Woolfson, D.N., A designed system for assessing how sequence affects alpha to beta conformational transitions in proteins. J. Biol. Chem. 277 (2002), 10150–10155.
    • (2002) J. Biol. Chem. , vol.277 , pp. 10150-10155
    • Ciani, B.1    Hutchinson, E.G.2    Sessions, R.B.3    Woolfson, D.N.4
  • 48
    • 0042467550 scopus 로고    scopus 로고
    • Rationalization of the effects of mutations on peptide and protein aggregation rates
    • [48] Chiti, F., Stefani, M., Taddei, N., Ramponi, G., Dobson, C.M., Rationalization of the effects of mutations on peptide and protein aggregation rates. Nature 424 (2003), 805–808.
    • (2003) Nature , vol.424 , pp. 805-808
    • Chiti, F.1    Stefani, M.2    Taddei, N.3    Ramponi, G.4    Dobson, C.M.5
  • 49
    • 0037044732 scopus 로고    scopus 로고
    • Charge attraction and beta propensity are necessary for amyloid fibril formation from tetrapeptides
    • [49] Tjernberg, L., Hosia, W., Bark, N., Thyberg, J., Johansson, J., Charge attraction and beta propensity are necessary for amyloid fibril formation from tetrapeptides. J. Biol. Chem. 277 (2002), 43243–43246.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43243-43246
    • Tjernberg, L.1    Hosia, W.2    Bark, N.3    Thyberg, J.4    Johansson, J.5
  • 51
    • 1842611349 scopus 로고    scopus 로고
    • Factors involved in the stability of isolated beta-sheets: turn sequence, beta-sheet twisting, and hydrophobic surface burial
    • [51] Santiveri, C.M., Santoro, J., Rico, M., Jimenez, M.A., Factors involved in the stability of isolated beta-sheets: turn sequence, beta-sheet twisting, and hydrophobic surface burial. Protein Sci. 13 (2004), 1134–1147.
    • (2004) Protein Sci. , vol.13 , pp. 1134-1147
    • Santiveri, C.M.1    Santoro, J.2    Rico, M.3    Jimenez, M.A.4
  • 52
    • 40849089197 scopus 로고    scopus 로고
    • A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif
    • [52] Lee, J., Dubey, V.K., Longo, L.M., Blaber, M., A logical OR redundancy within the Asx-Pro-Asx-Gly type I beta-turn motif. J. Mol. Biol. 377 (2008), 1251–1264.
    • (2008) J. Mol. Biol. , vol.377 , pp. 1251-1264
    • Lee, J.1    Dubey, V.K.2    Longo, L.M.3    Blaber, M.4
  • 53
    • 47749136312 scopus 로고    scopus 로고
    • Roles of beta-turns in protein folding: from peptide models to protein engineering
    • [53] Marcelino, A.M., Gierasch, L.M., Roles of beta-turns in protein folding: from peptide models to protein engineering. Biopolymers 89 (2008), 380–391.
    • (2008) Biopolymers , vol.89 , pp. 380-391
    • Marcelino, A.M.1    Gierasch, L.M.2
  • 54
    • 77957242403 scopus 로고    scopus 로고
    • Proteome-level interplay between folding and aggregation propensities of proteins
    • [54] Tartaglia, G.G., Vendruscolo, M., Proteome-level interplay between folding and aggregation propensities of proteins. J. Mol. Biol. 402 (2010), 919–928.
    • (2010) J. Mol. Biol. , vol.402 , pp. 919-928
    • Tartaglia, G.G.1    Vendruscolo, M.2
  • 55
    • 84863981137 scopus 로고    scopus 로고
    • From macroscopic measurements to microscopic mechanisms of protein aggregation
    • [55] Cohen, S.I., Vendruscolo, M., Dobson, C.M., Knowles, T.P., From macroscopic measurements to microscopic mechanisms of protein aggregation. J. Mol. Biol. 421 (2012), 160–171.
    • (2012) J. Mol. Biol. , vol.421 , pp. 160-171
    • Cohen, S.I.1    Vendruscolo, M.2    Dobson, C.M.3    Knowles, T.P.4
  • 56
    • 0032006678 scopus 로고    scopus 로고
    • The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways
    • [56] Kelly, J.W., The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. Curr. Opin. Struct. Biol. 8 (1998), 101–106.
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 101-106
    • Kelly, J.W.1
  • 57
    • 84858978818 scopus 로고    scopus 로고
    • Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships
    • [57] Bemporad, F., Chiti, F., Protein misfolded oligomers: experimental approaches, mechanism of formation, and structure-toxicity relationships. Chem. Biol. 19 (2012), 315–327.
    • (2012) Chem. Biol. , vol.19 , pp. 315-327
    • Bemporad, F.1    Chiti, F.2
  • 58
    • 0036415838 scopus 로고    scopus 로고
    • Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils
    • [58] Lashuel, H.A., Petre, B.M., Wall, J., Simon, M., Nowak, R.J., Walz, T., Lansbury, P.T. Jr., Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils. J. Mol. Biol. 322 (2002), 1089–1102.
    • (2002) J. Mol. Biol. , vol.322 , pp. 1089-1102
    • Lashuel, H.A.1    Petre, B.M.2    Wall, J.3    Simon, M.4    Nowak, R.J.5    Walz, T.6    Lansbury, P.T.7
  • 59
    • 0037174879 scopus 로고    scopus 로고
    • Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization
    • [59] Poirier, M.A., Li, H., Macosko, J., Cai, S., Amzel, M., Ross, C.A., Huntingtin spheroids and protofibrils as precursors in polyglutamine fibrilization. J. Biol. Chem. 277 (2002), 41032–41037.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41032-41037
    • Poirier, M.A.1    Li, H.2    Macosko, J.3    Cai, S.4    Amzel, M.5    Ross, C.A.6
  • 60
    • 80053563923 scopus 로고    scopus 로고
    • Misfolded protein aggregates: mechanisms, structures and potential for disease transmission
    • [60] Moreno-Gonzalez, I., Soto, C., Misfolded protein aggregates: mechanisms, structures and potential for disease transmission. Semin. Cell Dev. Biol. 22 (2011), 482–487.
    • (2011) Semin. Cell Dev. Biol. , vol.22 , pp. 482-487
    • Moreno-Gonzalez, I.1    Soto, C.2
  • 61
    • 84869887960 scopus 로고    scopus 로고
    • Structural features and cytotoxicity of amyloid oligomers: implications in Alzheimer's disease and other diseases with amyloid deposits
    • [61] Stefani, M., Structural features and cytotoxicity of amyloid oligomers: implications in Alzheimer's disease and other diseases with amyloid deposits. Prog. Neurobiol. 99 (2012), 226–245.
    • (2012) Prog. Neurobiol. , vol.99 , pp. 226-245
    • Stefani, M.1
  • 63
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • [63] Kayed, R., Head, E., Thompson, J.L., McIntire, T.M., Milton, S.C., Cotman, C.W., Glabe, C.G., Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300 (2003), 486–489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 64
    • 33644893050 scopus 로고    scopus 로고
    • Tetracycline inhibits W7FW14F apomyoglobin fibril extension and keeps the amyloid protein in a pre-fibrillar, highly cytotoxic state
    • [64] Malmo, C., Vilasi, S., Iannuzzi, C., Tacchi, S., Cametti, C., Irace, G., Sirangelo, I., Tetracycline inhibits W7FW14F apomyoglobin fibril extension and keeps the amyloid protein in a pre-fibrillar, highly cytotoxic state. FASEB J. 20 (2006), 346–347.
    • (2006) FASEB J. , vol.20 , pp. 346-347
    • Malmo, C.1    Vilasi, S.2    Iannuzzi, C.3    Tacchi, S.4    Cametti, C.5    Irace, G.6    Sirangelo, I.7
  • 66
    • 84885176987 scopus 로고    scopus 로고
    • The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity
    • [66] Cecchi, C., Stefani, M., The amyloid-cell membrane system. The interplay between the biophysical features of oligomers/fibrils and cell membrane defines amyloid toxicity. Biophys. Chem. 182 (2013), 30–43.
    • (2013) Biophys. Chem. , vol.182 , pp. 30-43
    • Cecchi, C.1    Stefani, M.2
  • 67
  • 68
    • 84884274578 scopus 로고    scopus 로고
    • Electrostatics controls the formation of amyloid superstructures in protein aggregation
    • [68] Fodera, V., Zaccone, A., Lattuada, M., Donald, A.M., Electrostatics controls the formation of amyloid superstructures in protein aggregation. Phys. Rev. Lett., 111, 2013, 108105.
    • (2013) Phys. Rev. Lett. , vol.111 , pp. 108105
    • Fodera, V.1    Zaccone, A.2    Lattuada, M.3    Donald, A.M.4
  • 69
    • 84942294422 scopus 로고    scopus 로고
    • The route to protein aggregate superstructures: Particulates and amyloid-like spherulites
    • [69] Vetri, V., Fodera, V., The route to protein aggregate superstructures: Particulates and amyloid-like spherulites. FEBS Lett. 589 (2015), 2448–2463.
    • (2015) FEBS Lett. , vol.589 , pp. 2448-2463
    • Vetri, V.1    Fodera, V.2
  • 70
    • 84902064401 scopus 로고    scopus 로고
    • The formation of amyloid-like superstructures: on the growth of amyloid spherulites
    • (Chapter 28)
    • [70] Foderà, V., Donald, A.M., The formation of amyloid-like superstructures: on the growth of amyloid spherulites. Bionanoimaging, 2014, 301–308 (Chapter 28).
    • (2014) Bionanoimaging , pp. 301-308
    • Foderà, V.1    Donald, A.M.2
  • 71
    • 70349180743 scopus 로고    scopus 로고
    • Inhibition of amyloid formation by ionic liquids: ionic liquids affecting intermediate oligomers
    • [71] Kalhor, H.R., Kamizi, M., Akbari, J., Heydari, A., Inhibition of amyloid formation by ionic liquids: ionic liquids affecting intermediate oligomers. Biomacromolecules 10 (2009), 2468–2475.
    • (2009) Biomacromolecules , vol.10 , pp. 2468-2475
    • Kalhor, H.R.1    Kamizi, M.2    Akbari, J.3    Heydari, A.4
  • 72
    • 79959977900 scopus 로고    scopus 로고
    • Rottlerin dissolves pre-formed protein amyloid: a study on hen egg white lysozyme
    • [72] Sarkar, N., Kumar, M., Dubey, V.K., Rottlerin dissolves pre-formed protein amyloid: a study on hen egg white lysozyme. Biochim. Biophys. Acta 1810 (2011), 809–814.
    • (2011) Biochim. Biophys. Acta , vol.1810 , pp. 809-814
    • Sarkar, N.1    Kumar, M.2    Dubey, V.K.3
  • 73
    • 79953187568 scopus 로고    scopus 로고
    • Exploring possibility of promiscuity of amyloid inhibitor: studies on effect of selected compounds on folding and amyloid formation of proteins
    • [73] Sarkar, N., Kumar, M., Dubey, V.K., Exploring possibility of promiscuity of amyloid inhibitor: studies on effect of selected compounds on folding and amyloid formation of proteins. Process Biochem. 46 (2011), 1179–1185.
    • (2011) Process Biochem. , vol.46 , pp. 1179-1185
    • Sarkar, N.1    Kumar, M.2    Dubey, V.K.3
  • 74
    • 84900026924 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril growth and dissolution of amyloid fibrils by curcumin-gold nanoparticles
    • [74] Palmal, S., Maity, A.R., Singh, B.K., Basu, S., Jana, N.R., Inhibition of amyloid fibril growth and dissolution of amyloid fibrils by curcumin-gold nanoparticles. Chemistry 20 (2014), 6184–6191.
    • (2014) Chemistry , vol.20 , pp. 6184-6191
    • Palmal, S.1    Maity, A.R.2    Singh, B.K.3    Basu, S.4    Jana, N.R.5
  • 75
    • 84949599389 scopus 로고    scopus 로고
    • EPPS rescues hippocampus-dependent cognitive deficits in APP/PS1 mice by disaggregation of amyloid-beta oligomers and plaques
    • [75] Kim, H.Y., Kim, H.V., Jo, S., Lee, C.J., Choi, S.Y., Kim, D.J., Kim, Y., EPPS rescues hippocampus-dependent cognitive deficits in APP/PS1 mice by disaggregation of amyloid-beta oligomers and plaques. Nat. Commun., 6, 2015, 8997.
    • (2015) Nat. Commun. , vol.6 , pp. 8997
    • Kim, H.Y.1    Kim, H.V.2    Jo, S.3    Lee, C.J.4    Choi, S.Y.5    Kim, D.J.6    Kim, Y.7
  • 77
    • 84903742654 scopus 로고    scopus 로고
    • beta-cyclodextrin and curcumin, a potent cocktail for disaggregating and/or inhibiting amyloids: a case study with alpha-synuclein
    • [77] Gautam, S., Karmakar, S., Bose, A., Chowdhury, P.K., beta-cyclodextrin and curcumin, a potent cocktail for disaggregating and/or inhibiting amyloids: a case study with alpha-synuclein. Biochemistry 53 (2014), 4081–4083.
    • (2014) Biochemistry , vol.53 , pp. 4081-4083
    • Gautam, S.1    Karmakar, S.2    Bose, A.3    Chowdhury, P.K.4
  • 78
    • 84897083544 scopus 로고    scopus 로고
    • Investigation of the aggregation process of amyloid-beta-(16-22) peptides and the dissolution of intermediate aggregates
    • [78] Lin, D., Luo, Y., Wu, S., Ma, Q., Wei, G., Yang, X., Investigation of the aggregation process of amyloid-beta-(16-22) peptides and the dissolution of intermediate aggregates. Langmuir 30 (2014), 3170–3175.
    • (2014) Langmuir , vol.30 , pp. 3170-3175
    • Lin, D.1    Luo, Y.2    Wu, S.3    Ma, Q.4    Wei, G.5    Yang, X.6
  • 81
    • 0033600301 scopus 로고    scopus 로고
    • Molecular basis of the neurodegenerative disorders
    • [81] Martin, J.B., Molecular basis of the neurodegenerative disorders. N. Engl. J. Med. 340 (1999), 1970–1980.
    • (1999) N. Engl. J. Med. , vol.340 , pp. 1970-1980
    • Martin, J.B.1
  • 82
    • 0023473138 scopus 로고
    • Neuron numbers in Alzheimer's disease: cell-specific pathology
    • [82] Hyman, B.T., Van Hoesen, G.W., Neuron numbers in Alzheimer's disease: cell-specific pathology. Neurobiol. Aging 8 (1987), 555–556.
    • (1987) Neurobiol. Aging , vol.8 , pp. 555-556
    • Hyman, B.T.1    Van Hoesen, G.W.2
  • 83
    • 0029981526 scopus 로고    scopus 로고
    • Neuropathology of Parkinson's disease
    • [83] Forno, L.S., Neuropathology of Parkinson's disease. J. Neuropathol. Exp. Neurol. 55 (1996), 259–272.
    • (1996) J. Neuropathol. Exp. Neurol. , vol.55 , pp. 259-272
    • Forno, L.S.1
  • 85
    • 0020392210 scopus 로고
    • Pathology of amyotrophic lateral sclerosis
    • [85] Hughes, J.T., Pathology of amyotrophic lateral sclerosis. Adv. Neurol. 36 (1982), 61–74.
    • (1982) Adv. Neurol. , vol.36 , pp. 61-74
    • Hughes, J.T.1
  • 87
    • 0034329742 scopus 로고    scopus 로고
    • Apoptosis in neurodegenerative disorders
    • [87] Mattson, M.P., Apoptosis in neurodegenerative disorders. Nat. Rev. Mol. Cell Biol. 1 (2000), 120–129.
    • (2000) Nat. Rev. Mol. Cell Biol. , vol.1 , pp. 120-129
    • Mattson, M.P.1
  • 93
    • 0036470471 scopus 로고    scopus 로고
    • Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration
    • [93] Mallucci, G.R., Ratte, S., Asante, E.A., Linehan, J., Gowland, I., Jefferys, J.G., Collinge, J., Post-natal knockout of prion protein alters hippocampal CA1 properties, but does not result in neurodegeneration. EMBO J. 21 (2002), 202–210.
    • (2002) EMBO J. , vol.21 , pp. 202-210
    • Mallucci, G.R.1    Ratte, S.2    Asante, E.A.3    Linehan, J.4    Gowland, I.5    Jefferys, J.G.6    Collinge, J.7
  • 96
    • 0031680014 scopus 로고    scopus 로고
    • A cellular model that recapitulates major pathogenic steps of Huntington's disease
    • [96] Lunkes, A., Mandel, J.L., A cellular model that recapitulates major pathogenic steps of Huntington's disease. Hum. Mol. Genet. 7 (1998), 1355–1361.
    • (1998) Hum. Mol. Genet. , vol.7 , pp. 1355-1361
    • Lunkes, A.1    Mandel, J.L.2
  • 97
    • 0032573597 scopus 로고    scopus 로고
    • Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments
    • [97] El-Agnaf, O.M., Jakes, R., Curran, M.D., Middleton, D., Ingenito, R., Bianchi, E., Pessi, A., Neill, D., Wallace, A., Aggregates from mutant and wild-type alpha-synuclein proteins and NAC peptide induce apoptotic cell death in human neuroblastoma cells by formation of beta-sheet and amyloid-like filaments. FEBS Lett. 440 (1998), 71–75.
    • (1998) FEBS Lett. , vol.440 , pp. 71-75
    • El-Agnaf, O.M.1    Jakes, R.2    Curran, M.D.3    Middleton, D.4    Ingenito, R.5    Bianchi, E.6    Pessi, A.7    Neill, D.8    Wallace, A.9
  • 99
    • 0031838352 scopus 로고    scopus 로고
    • Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1
    • [99] Cummings, C.J., Mancini, M.A., Antalffy, B., DeFranco, D.B., Orr, H.T., Zoghbi, H.Y., Chaperone suppression of aggregation and altered subcellular proteasome localization imply protein misfolding in SCA1. Nat. Genet. 19 (1998), 148–154.
    • (1998) Nat. Genet. , vol.19 , pp. 148-154
    • Cummings, C.J.1    Mancini, M.A.2    Antalffy, B.3    DeFranco, D.B.4    Orr, H.T.5    Zoghbi, H.Y.6
  • 100
    • 0030830270 scopus 로고    scopus 로고
    • Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly
    • [100] Ii, K., Ito, H., Tanaka, K., Hirano, A., Immunocytochemical co-localization of the proteasome in ubiquitinated structures in neurodegenerative diseases and the elderly. J. Neuropathol. Exp. Neurol. 56 (1997), 125–131.
    • (1997) J. Neuropathol. Exp. Neurol. , vol.56 , pp. 125-131
    • Ii, K.1    Ito, H.2    Tanaka, K.3    Hirano, A.4
  • 101
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum
    • [101] Arispe, N., Rojas, E., Pollard, H.B., Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. Proc. Natl. Acad. Sci. U. S. A. 90 (1993), 567–571.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 102
    • 0031024927 scopus 로고    scopus 로고
    • Channel formation by a neurotoxic prion protein fragment
    • [102] Lin, M.C., Mirzabekov, T., Kagan, B.L., Channel formation by a neurotoxic prion protein fragment. J. Biol. Chem. 272 (1997), 44–47.
    • (1997) J. Biol. Chem. , vol.272 , pp. 44-47
    • Lin, M.C.1    Mirzabekov, T.2    Kagan, B.L.3
  • 103
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • [103] Behl, C., Davis, J.B., Lesley, R., Schubert, D., Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 77 (1994), 817–827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 105
    • 0036685522 scopus 로고    scopus 로고
    • Inflammation in neurodegenerative disease–a double-edged sword
    • [105] Wyss-Coray, T., Mucke, L., Inflammation in neurodegenerative disease–a double-edged sword. Neuron 35 (2002), 419–432.
    • (2002) Neuron , vol.35 , pp. 419-432
    • Wyss-Coray, T.1    Mucke, L.2
  • 108
    • 0029610011 scopus 로고
    • The inflammatory response system of brain: implications for therapy of Alzheimer and other neurodegenerative diseases
    • [108] McGeer, P.L., McGeer, E.G., The inflammatory response system of brain: implications for therapy of Alzheimer and other neurodegenerative diseases. Brain Res. Brain Res. Rev. 21 (1995), 195–218.
    • (1995) Brain Res. Brain Res. Rev. , vol.21 , pp. 195-218
    • McGeer, P.L.1    McGeer, E.G.2
  • 109
    • 0032917904 scopus 로고    scopus 로고
    • Chemokines/chemokine receptors in the central nervous system and Alzheimer's disease
    • [109] Xia, M.Q., Hyman, B.T., Chemokines/chemokine receptors in the central nervous system and Alzheimer's disease. J. Neurovirol. 5 (1999), 32–41.
    • (1999) J. Neurovirol. , vol.5 , pp. 32-41
    • Xia, M.Q.1    Hyman, B.T.2
  • 110
    • 0033982028 scopus 로고    scopus 로고
    • Amyloid beta and amylin fibrils induce increases in proinflammatory cytokine and chemokine production by THP-1 cells and murine microglia
    • [110] Yates, S.L., Burgess, L.H., Kocsis-Angle, J., Antal, J.M., Dority, M.D., Embury, P.B., Piotrkowski, A.M., Brunden, K.R., Amyloid beta and amylin fibrils induce increases in proinflammatory cytokine and chemokine production by THP-1 cells and murine microglia. J. Neurochem. 74 (2000), 1017–1025.
    • (2000) J. Neurochem. , vol.74 , pp. 1017-1025
    • Yates, S.L.1    Burgess, L.H.2    Kocsis-Angle, J.3    Antal, J.M.4    Dority, M.D.5    Embury, P.B.6    Piotrkowski, A.M.7    Brunden, K.R.8
  • 111
    • 0029811901 scopus 로고    scopus 로고
    • Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: a review of 17 epidemiologic studies
    • [111] McGeer, P.L., Schulzer, M., McGeer, E.G., Arthritis and anti-inflammatory agents as possible protective factors for Alzheimer's disease: a review of 17 epidemiologic studies. Neurology 47 (1996), 425–432.
    • (1996) Neurology , vol.47 , pp. 425-432
    • McGeer, P.L.1    Schulzer, M.2    McGeer, E.G.3
  • 112
    • 84877346858 scopus 로고    scopus 로고
    • Analysis of protein aggregation in neurodegenerative disease
    • [112] Pedersen, J.T., Heegaard, N.H., Analysis of protein aggregation in neurodegenerative disease. Anal. Chem. 85 (2013), 4215–4227.
    • (2013) Anal. Chem. , vol.85 , pp. 4215-4227
    • Pedersen, J.T.1    Heegaard, N.H.2
  • 113
    • 34547174917 scopus 로고    scopus 로고
    • Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins
    • [113] Munishkina, L.A., Fink, A.L., Fluorescence as a method to reveal structures and membrane-interactions of amyloidogenic proteins. Biochim. Biophys. Acta 1768 (2007), 1862–1885.
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1862-1885
    • Munishkina, L.A.1    Fink, A.L.2
  • 114
    • 36849078628 scopus 로고    scopus 로고
    • Insight into the kinetic of amyloid beta (1-42) peptide self-aggregation: elucidation of inhibitors' mechanism of action
    • [114] Bartolini, M., Bertucci, C., Bolognesi, M.L., Cavalli, A., Melchiorre, C., Andrisano, V., Insight into the kinetic of amyloid beta (1-42) peptide self-aggregation: elucidation of inhibitors' mechanism of action. Chembiochem 8 (2007), 2152–2161.
    • (2007) Chembiochem , vol.8 , pp. 2152-2161
    • Bartolini, M.1    Bertucci, C.2    Bolognesi, M.L.3    Cavalli, A.4    Melchiorre, C.5    Andrisano, V.6
  • 115
    • 52049121032 scopus 로고    scopus 로고
    • Impact of Tyr to Ala mutations on alpha-synuclein fibrillation and structural properties
    • [115] Ulrih, N.P., Barry, C.H., Fink, A.L., Impact of Tyr to Ala mutations on alpha-synuclein fibrillation and structural properties. Biochim. Biophys. Acta 1782 (2008), 581–585.
    • (2008) Biochim. Biophys. Acta , vol.1782 , pp. 581-585
    • Ulrih, N.P.1    Barry, C.H.2    Fink, A.L.3
  • 116
    • 0028982292 scopus 로고
    • Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes
    • [116] Terzi, E., Holzemann, G., Seelig, J., Self-association of beta-amyloid peptide (1-40) in solution and binding to lipid membranes. J. Mol. Biol. 252 (1995), 633–642.
    • (1995) J. Mol. Biol. , vol.252 , pp. 633-642
    • Terzi, E.1    Holzemann, G.2    Seelig, J.3
  • 117
    • 36749021816 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopy as a tool for drug design: from membrane-embedded targets to amyloid fibrils
    • [117] Middleton, D.A., Solid-state NMR spectroscopy as a tool for drug design: from membrane-embedded targets to amyloid fibrils. Biochem. Soc. Trans. 35 (2007), 985–990.
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 985-990
    • Middleton, D.A.1
  • 120
    • 22144490779 scopus 로고    scopus 로고
    • Acetylcholinesterase-amyloid-beta-peptide interaction: effect of Congo Red and the role of the Wnt pathway
    • [120] Inestrosa, N.C., Alvarez, A., Dinamarca, M.C., Perez-Acle, T., Colombres, M., Acetylcholinesterase-amyloid-beta-peptide interaction: effect of Congo Red and the role of the Wnt pathway. Curr. Alzheimer Res. 2 (2005), 301–306.
    • (2005) Curr. Alzheimer Res. , vol.2 , pp. 301-306
    • Inestrosa, N.C.1    Alvarez, A.2    Dinamarca, M.C.3    Perez-Acle, T.4    Colombres, M.5
  • 121
    • 33845192482 scopus 로고    scopus 로고
    • Congo red and protein aggregation in neurodegenerative diseases
    • [121] Frid, P., Anisimov, S.V., Popovic, N., Congo red and protein aggregation in neurodegenerative diseases. Brain Res. Rev. 53 (2007), 135–160.
    • (2007) Brain Res. Rev. , vol.53 , pp. 135-160
    • Frid, P.1    Anisimov, S.V.2    Popovic, N.3
  • 122
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution
    • [122] LeVine, H. 3rd, Thioflavine T interaction with synthetic Alzheimer's disease beta-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 2 (1993), 404–410.
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine, H.1
  • 123
    • 3343003514 scopus 로고    scopus 로고
    • Techniques to study amyloid fibril formation in vitro
    • [123] Nilsson, M.R., Techniques to study amyloid fibril formation in vitro. Methods 34 (2004), 151–160.
    • (2004) Methods , vol.34 , pp. 151-160
    • Nilsson, M.R.1
  • 124
    • 76649138290 scopus 로고    scopus 로고
    • Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status
    • [124] Groenning, M., Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status. J. Chem. Biol. 3 (2010), 1–18.
    • (2010) J. Chem. Biol. , vol.3 , pp. 1-18
    • Groenning, M.1
  • 125
    • 68949085124 scopus 로고    scopus 로고
    • Protein aggregation: pathways, induction factors and analysis
    • [125] Mahler, H.C., Friess, W., Grauschopf, U., Kiese, S., Protein aggregation: pathways, induction factors and analysis. J. Pharm. Sci. 98 (2009), 2909–2934.
    • (2009) J. Pharm. Sci. , vol.98 , pp. 2909-2934
    • Mahler, H.C.1    Friess, W.2    Grauschopf, U.3    Kiese, S.4
  • 126
    • 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
    • [126] 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. 66 (1997), 385–407.
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.2
  • 127
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants
    • [127] Lomakin, A., Chung, D.S., Benedek, G.B., Kirschner, D.A., Teplow, D.B., On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants. Proc. Natl. Acad. Sci. U. S. A. 93 (1996), 1125–1129.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 128
    • 84864590986 scopus 로고    scopus 로고
    • Quasielastic light scattering study of amyloid beta-protein fibrillogenesis
    • [128] Lomakin, A., Teplow, D.B., Quasielastic light scattering study of amyloid beta-protein fibrillogenesis. Methods Mol. Biol. 849 (2012), 69–83.
    • (2012) Methods Mol. Biol. , vol.849 , pp. 69-83
    • Lomakin, A.1    Teplow, D.B.2
  • 129
    • 0041845349 scopus 로고    scopus 로고
    • Certain metals trigger fibrillation of methionine-oxidized alpha-synuclein
    • [129] Yamin, G., Glaser, C.B., Uversky, V.N., Fink, A.L., Certain metals trigger fibrillation of methionine-oxidized alpha-synuclein. J. Biol. Chem. 278 (2003), 27630–27635.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27630-27635
    • Yamin, G.1    Glaser, C.B.2    Uversky, V.N.3    Fink, A.L.4
  • 131
    • 4644327652 scopus 로고    scopus 로고
    • Native protein mass spectrometry: from intact oligomers to functional machineries
    • [131] van den Heuvel, R.H., Heck, A.J., Native protein mass spectrometry: from intact oligomers to functional machineries. Curr. Opin. Chem. Biol. 8 (2004), 519–526.
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 519-526
    • van den Heuvel, R.H.1    Heck, A.J.2
  • 132
    • 4444243006 scopus 로고    scopus 로고
    • Investigation of intact protein complexes by mass spectrometry
    • [132] Heck, A.J., Van Den Heuvel, R.H., Investigation of intact protein complexes by mass spectrometry. Mass Spectrom. Rev. 23 (2004), 368–389.
    • (2004) Mass Spectrom. Rev. , vol.23 , pp. 368-389
    • Heck, A.J.1    Van Den Heuvel, R.H.2
  • 134
    • 27344436619 scopus 로고    scopus 로고
    • Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level
    • [134] Del Mar, C., Greenbaum, E.A., Mayne, L., Englander, S.W., Woods, V.L. Jr., Structure and properties of alpha-synuclein and other amyloids determined at the amino acid level. Proc. Natl. Acad. Sci. U. S. A. 102 (2005), 15477–15482.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 15477-15482
    • Del Mar, C.1    Greenbaum, E.A.2    Mayne, L.3    Englander, S.W.4    Woods, V.L.5
  • 137
    • 77955682352 scopus 로고    scopus 로고
    • Structure and intermolecular dynamics of aggregates populated during amyloid fibril formation studied by hydrogen/deuterium exchange
    • [137] Carulla, N., Zhou, M., Giralt, E., Robinson, C.V., Dobson, C.M., Structure and intermolecular dynamics of aggregates populated during amyloid fibril formation studied by hydrogen/deuterium exchange. Acc. Chem. Res. 43 (2010), 1072–1079.
    • (2010) Acc. Chem. Res. , vol.43 , pp. 1072-1079
    • Carulla, N.1    Zhou, M.2    Giralt, E.3    Robinson, C.V.4    Dobson, C.M.5
  • 138
    • 70349160466 scopus 로고    scopus 로고
    • Cross-beta-sheet structure in amyloid fiber formation
    • [138] Xu, S., Cross-beta-sheet structure in amyloid fiber formation. J. Phys. Chem. B 113 (2009), 12447–12455.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 12447-12455
    • Xu, S.1
  • 139
    • 68949142908 scopus 로고    scopus 로고
    • Amyloid fibril-like structure underlies the aggregate structure across the pH range for beta-lactoglobulin
    • [139] Krebs, M.R., Devlin, G.L., Donald, A.M., Amyloid fibril-like structure underlies the aggregate structure across the pH range for beta-lactoglobulin. Biophys. J. 96 (2009), 5013–5019.
    • (2009) Biophys. J. , vol.96 , pp. 5013-5019
    • Krebs, M.R.1    Devlin, G.L.2    Donald, A.M.3
  • 140
    • 53349144370 scopus 로고    scopus 로고
    • The natively unfolded character of tau and its aggregation to Alzheimer-like paired helical filaments
    • [140] Jeganathan, S., von Bergen, M., Mandelkow, E.M., Mandelkow, E., The natively unfolded character of tau and its aggregation to Alzheimer-like paired helical filaments. Biochemistry 47 (2008), 10526–10539.
    • (2008) Biochemistry , vol.47 , pp. 10526-10539
    • Jeganathan, S.1    von Bergen, M.2    Mandelkow, E.M.3    Mandelkow, E.4
  • 142
    • 0013892617 scopus 로고
    • The ultrastructure of human amyloid as revealed by the negative staining technique
    • [142] Bladen, H.A., Nylen, M.U., Glenner, G.G., The ultrastructure of human amyloid as revealed by the negative staining technique. J. Ultrastruct. Res. 14 (1966), 449–459.
    • (1966) J. Ultrastruct. Res. , vol.14 , pp. 449-459
    • Bladen, H.A.1    Nylen, M.U.2    Glenner, G.G.3
  • 143
    • 0001611370 scopus 로고
    • Electron microscopic observations on a fibrous component in amyloid of diverse origins
    • [143] Cohen, A.S., Calkins, E., Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature 183 (1959), 1202–1203.
    • (1959) Nature , vol.183 , pp. 1202-1203
    • Cohen, A.S.1    Calkins, E.2
  • 144
    • 22844440807 scopus 로고    scopus 로고
    • Molecular electron microscopy approaches to elucidating the mechanisms of protein fibrillogenesis
    • [144] Lashuel, H.A., Wall, J.S., Molecular electron microscopy approaches to elucidating the mechanisms of protein fibrillogenesis. Methods Mol. Biol. 299 (2005), 81–101.
    • (2005) Methods Mol. Biol. , vol.299 , pp. 81-101
    • Lashuel, H.A.1    Wall, J.S.2
  • 145
    • 11844249291 scopus 로고    scopus 로고
    • Rapid assembly of amyloid-beta peptide at a liquid/liquid interface produces unstable beta-sheet fibers
    • [145] Nichols, M.R., Moss, M.A., Reed, D.K., Hoh, J.H., Rosenberry, T.L., Rapid assembly of amyloid-beta peptide at a liquid/liquid interface produces unstable beta-sheet fibers. Biochemistry 44 (2005), 165–173.
    • (2005) Biochemistry , vol.44 , pp. 165-173
    • Nichols, M.R.1    Moss, M.A.2    Reed, D.K.3    Hoh, J.H.4    Rosenberry, T.L.5
  • 147
    • 22844448175 scopus 로고    scopus 로고
    • Time-lapse atomic force microscopy in the characterization of amyloid-like fibril assembly and oligomeric intermediates
    • [147] Goldsbury, C., Green, J., Time-lapse atomic force microscopy in the characterization of amyloid-like fibril assembly and oligomeric intermediates. Methods Mol. Biol. 299 (2005), 103–128.
    • (2005) Methods Mol. Biol. , vol.299 , pp. 103-128
    • Goldsbury, C.1    Green, J.2
  • 149
    • 79959505737 scopus 로고    scopus 로고
    • Studies of the growth, evolution, and self-aggregation of beta-amyloid fibrils using tapping-mode atomic force microscopy
    • [149] Serem, W.K., Bett, C.K., Ngunjiri, J.N., Garno, J.C., Studies of the growth, evolution, and self-aggregation of beta-amyloid fibrils using tapping-mode atomic force microscopy. Microsc. Res. Tech. 74 (2011), 699–708.
    • (2011) Microsc. Res. Tech. , vol.74 , pp. 699-708
    • Serem, W.K.1    Bett, C.K.2    Ngunjiri, J.N.3    Garno, J.C.4
  • 150
    • 65949093940 scopus 로고    scopus 로고
    • CE can identify small molecules that selectively target soluble oligomers of amyloid beta protein and display antifibrillogenic activity
    • [150] Colombo, R., Carotti, A., Catto, M., Racchi, M., Lanni, C., Verga, L., Caccialanza, G., De Lorenzi, E., CE can identify small molecules that selectively target soluble oligomers of amyloid beta protein and display antifibrillogenic activity. Electrophoresis 30 (2009), 1418–1429.
    • (2009) Electrophoresis , vol.30 , pp. 1418-1429
    • Colombo, R.1    Carotti, A.2    Catto, M.3    Racchi, M.4    Lanni, C.5    Verga, L.6    Caccialanza, G.7    De Lorenzi, E.8
  • 152
    • 57549085173 scopus 로고    scopus 로고
    • Characterizing protein-protein interactions by sedimentation velocity analytical ultracentrifugation
    • Chapter 18, Unit 18 15
    • [152] Brown, P.H., Balbo, A., Schuck, P., Characterizing protein-protein interactions by sedimentation velocity analytical ultracentrifugation. Curr. Protoc. Immunol., Chapter 18, 2008 Unit 18 15.
    • (2008) Curr. Protoc. Immunol.
    • Brown, P.H.1    Balbo, A.2    Schuck, P.3
  • 153
    • 77949336151 scopus 로고    scopus 로고
    • Alzheimer's disease facts and figures
    • 2010
    • [153] 2010Alzheimer's disease facts and figures. Alzheimers Dement. 6 (2010), 158–194.
    • (2010) Alzheimers Dement. , vol.6 , pp. 158-194
  • 154
    • 85043805949 scopus 로고    scopus 로고
    • The State of Health and Aging in America Merck Company Foundation
    • Whitehouse Station New Jersey, USA
    • [154] Centers for Disease Control and Prevention and The Merck Company Foundation, The State of Health and Aging in America Merck Company Foundation. 2007, Whitehouse Station, New Jersey, USA.
    • (2007)
    • Centers for Disease Control and Prevention and The Merck Company Foundation1
  • 155
    • 65449161780 scopus 로고    scopus 로고
    • Alzheimer's disease facts and figures
    • 2009
    • [155] 2009Alzheimer's disease facts and figures. Alzheimers Dement. 5 (2009), 234–270.
    • (2009) Alzheimers Dement. , vol.5 , pp. 234-270
  • 157
    • 84875230719 scopus 로고    scopus 로고
    • Recent developments in targeting protein misfolding diseases
    • [157] Denny, R.A., Gavrin, L.K., Saiah, E., Recent developments in targeting protein misfolding diseases. Bioorg Med. Chem. Lett. 23 (2013), 1935–1944.
    • (2013) Bioorg Med. Chem. Lett. , vol.23 , pp. 1935-1944
    • Denny, R.A.1    Gavrin, L.K.2    Saiah, E.3
  • 158
    • 84863987464 scopus 로고    scopus 로고
    • Inhibition of amyloid formation
    • [158] Hard, T., Lendel, C., Inhibition of amyloid formation. J. Mol. Biol. 421 (2012), 441–465.
    • (2012) J. Mol. Biol. , vol.421 , pp. 441-465
    • Hard, T.1    Lendel, C.2
  • 159
    • 77952138141 scopus 로고    scopus 로고
    • Strategies for the inhibition of protein aggregation in human diseases
    • [159] Bartolini, M., Andrisano, V., Strategies for the inhibition of protein aggregation in human diseases. Chembiochem 11 (2010), 1018–1035.
    • (2010) Chembiochem , vol.11 , pp. 1018-1035
    • Bartolini, M.1    Andrisano, V.2
  • 161
    • 77949272212 scopus 로고    scopus 로고
    • Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses
    • [161] Connelly, S., Choi, S., Johnson, S.M., Kelly, J.W., Wilson, I.A., Structure-based design of kinetic stabilizers that ameliorate the transthyretin amyloidoses. Curr. Opin. Struct. Biol. 20 (2010), 54–62.
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 54-62
    • Connelly, S.1    Choi, S.2    Johnson, S.M.3    Kelly, J.W.4    Wilson, I.A.5
  • 162
    • 0035964955 scopus 로고    scopus 로고
    • Trans-suppression of misfolding in an amyloid disease
    • [162] Hammarstrom, P., Schneider, F., Kelly, J.W., Trans-suppression of misfolding in an amyloid disease. Science 293 (2001), 2459–2462.
    • (2001) Science , vol.293 , pp. 2459-2462
    • Hammarstrom, P.1    Schneider, F.2    Kelly, J.W.3
  • 163
    • 84871650725 scopus 로고    scopus 로고
    • Small molecules that target protein misfolding
    • [163] Gavrin, L.K., Denny, R.A., Saiah, E., Small molecules that target protein misfolding. J. Med. Chem. 55 (2012), 10823–10843.
    • (2012) J. Med. Chem. , vol.55 , pp. 10823-10843
    • Gavrin, L.K.1    Denny, R.A.2    Saiah, E.3
  • 164
    • 0029832863 scopus 로고    scopus 로고
    • Chemical chaperones interfere with the formation of scrapie prion protein
    • [164] Tatzelt, J., Prusiner, S.B., Welch, W.J., Chemical chaperones interfere with the formation of scrapie prion protein. EMBO J. 15 (1996), 6363–6373.
    • (1996) EMBO J. , vol.15 , pp. 6363-6373
    • Tatzelt, J.1    Prusiner, S.B.2    Welch, W.J.3
  • 165
    • 0346727128 scopus 로고    scopus 로고
    • Therapeutic approaches to protein-misfolding diseases
    • [165] Cohen, F.E., Kelly, J.W., Therapeutic approaches to protein-misfolding diseases. Nature 426 (2003), 905–909.
    • (2003) Nature , vol.426 , pp. 905-909
    • Cohen, F.E.1    Kelly, J.W.2
  • 167
    • 14844361966 scopus 로고    scopus 로고
    • Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation
    • [167] Ray, S.S., Nowak, R.J., Brown, R.H. Jr., Lansbury, P.T. Jr., Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation. Proc. Natl. Acad. Sci. U. S. A. 102 (2005), 3639–3644.
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 3639-3644
    • Ray, S.S.1    Nowak, R.J.2    Brown, R.H.3    Lansbury, P.T.4
  • 168
    • 77950562400 scopus 로고    scopus 로고
    • Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods
    • [168] Nowak, R.J., Cuny, G.D., Choi, S., Lansbury, P.T., Ray, S.S., Improving binding specificity of pharmacological chaperones that target mutant superoxide dismutase-1 linked to familial amyotrophic lateral sclerosis using computational methods. J. Med. Chem. 53 (2010), 2709–2718.
    • (2010) J. Med. Chem. , vol.53 , pp. 2709-2718
    • Nowak, R.J.1    Cuny, G.D.2    Choi, S.3    Lansbury, P.T.4    Ray, S.S.5
  • 169
    • 80755163102 scopus 로고    scopus 로고
    • Molecular pathways of motor neuron injury in amyotrophic lateral sclerosis
    • [169] Ferraiuolo, L., Kirby, J., Grierson, A.J., Sendtner, M., Shaw, P.J., Molecular pathways of motor neuron injury in amyotrophic lateral sclerosis. Nat. Rev. Neurol. 7 (2011), 616–630.
    • (2011) Nat. Rev. Neurol. , vol.7 , pp. 616-630
    • Ferraiuolo, L.1    Kirby, J.2    Grierson, A.J.3    Sendtner, M.4    Shaw, P.J.5
  • 173
    • 0031873102 scopus 로고    scopus 로고
    • Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy
    • [173] Soto, C., Sigurdsson, E.M., Morelli, L., Kumar, R.A., Castano, E.M., Frangione, B., Beta-sheet breaker peptides inhibit fibrillogenesis in a rat brain model of amyloidosis: implications for Alzheimer's therapy. Nat. Med. 4 (1998), 822–826.
    • (1998) Nat. Med. , vol.4 , pp. 822-826
    • Soto, C.1    Sigurdsson, E.M.2    Morelli, L.3    Kumar, R.A.4    Castano, E.M.5    Frangione, B.6
  • 174
    • 0036615884 scopus 로고    scopus 로고
    • Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a beta-sheet breaker peptide
    • [174] Permanne, B., Adessi, C., Saborio, G.P., Fraga, S., Frossard, M.J., Van Dorpe, J., Dewachter, I., Banks, W.A., Van Leuven, F., Soto, C., Reduction of amyloid load and cerebral damage in a transgenic mouse model of Alzheimer's disease by treatment with a beta-sheet breaker peptide. FASEB J. 16 (2002), 860–862.
    • (2002) FASEB J. , vol.16 , pp. 860-862
    • Permanne, B.1    Adessi, C.2    Saborio, G.P.3    Fraga, S.4    Frossard, M.J.5    Van Dorpe, J.6    Dewachter, I.7    Banks, W.A.8    Van Leuven, F.9    Soto, C.10
  • 177
    • 33646130171 scopus 로고    scopus 로고
    • Inhibition of insulin fibrillogenesis with targeted peptides
    • [177] Gibson, T.J., Murphy, R.M., Inhibition of insulin fibrillogenesis with targeted peptides. Protein Sci. 15 (2006), 1133–1141.
    • (2006) Protein Sci. , vol.15 , pp. 1133-1141
    • Gibson, T.J.1    Murphy, R.M.2
  • 178
    • 0032557457 scopus 로고    scopus 로고
    • Specific inhibition of in vitro formation of protease-resistant prion protein by synthetic peptides
    • [178] Chabry, J., Caughey, B., Chesebro, B., Specific inhibition of in vitro formation of protease-resistant prion protein by synthetic peptides. J. Biol. Chem. 273 (1998), 13203–13207.
    • (1998) J. Biol. Chem. , vol.273 , pp. 13203-13207
    • Chabry, J.1    Caughey, B.2    Chesebro, B.3
  • 179
    • 8544272519 scopus 로고    scopus 로고
    • Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions
    • [179] Porat, Y., Mazor, Y., Efrat, S., Gazit, E., Inhibition of islet amyloid polypeptide fibril formation: a potential role for heteroaromatic interactions. Biochemistry 43 (2004), 14454–14462.
    • (2004) Biochemistry , vol.43 , pp. 14454-14462
    • Porat, Y.1    Mazor, Y.2    Efrat, S.3    Gazit, E.4
  • 181
    • 0036095659 scopus 로고    scopus 로고
    • Design and characterization of a membrane permeable N-methyl amino acid-containing peptide that inhibits Abeta1-40 fibrillogenesis
    • [181] Gordon, D.J., Tappe, R., Meredith, S.C., Design and characterization of a membrane permeable N-methyl amino acid-containing peptide that inhibits Abeta1-40 fibrillogenesis. J. Pept. Res. 60 (2002), 37–55.
    • (2002) J. Pept. Res. , vol.60 , pp. 37-55
    • Gordon, D.J.1    Tappe, R.2    Meredith, S.C.3
  • 182
    • 0034682788 scopus 로고    scopus 로고
    • Inhibition of toxicity in the beta-amyloid peptide fragment beta -(25-35) using N-methylated derivatives: a general strategy to prevent amyloid formation
    • [182] Hughes, E., Burke, R.M., Doig, A.J., Inhibition of toxicity in the beta-amyloid peptide fragment beta -(25-35) using N-methylated derivatives: a general strategy to prevent amyloid formation. J. Biol. Chem. 275 (2000), 25109–25115.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25109-25115
    • Hughes, E.1    Burke, R.M.2    Doig, A.J.3
  • 183
    • 33747484171 scopus 로고    scopus 로고
    • N-Methylated peptide inhibitors of beta-amyloid aggregation and toxicity. Optimization of the inhibitor structure
    • [183] Kokkoni, N., Stott, K., Amijee, H., Mason, J.M., Doig, A.J., N-Methylated peptide inhibitors of beta-amyloid aggregation and toxicity. Optimization of the inhibitor structure. Biochemistry 45 (2006), 9906–9918.
    • (2006) Biochemistry , vol.45 , pp. 9906-9918
    • Kokkoni, N.1    Stott, K.2    Amijee, H.3    Mason, J.M.4    Doig, A.J.5
  • 184
    • 45749101292 scopus 로고    scopus 로고
    • Design of an N-methylated peptide inhibitor of alpha-synuclein aggregation guided by solid-state NMR
    • [184] Madine, J., Doig, A.J., Middleton, D.A., Design of an N-methylated peptide inhibitor of alpha-synuclein aggregation guided by solid-state NMR. J. Am. Chem. Soc. 130 (2008), 7873–7881.
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 7873-7881
    • Madine, J.1    Doig, A.J.2    Middleton, D.A.3
  • 186
    • 0036527699 scopus 로고    scopus 로고
    • Therapeutic strategies for human amyloid diseases
    • [186] Sacchettini, J.C., Kelly, J.W., Therapeutic strategies for human amyloid diseases. Nat. Rev. Drug Discov. 1 (2002), 267–275.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 267-275
    • Sacchettini, J.C.1    Kelly, J.W.2
  • 187
    • 0035983921 scopus 로고    scopus 로고
    • The challenge of inhibiting Abeta polymerization
    • [187] LeVine, H., The challenge of inhibiting Abeta polymerization. Curr. Med. Chem. 9 (2002), 1121–1133.
    • (2002) Curr. Med. Chem. , vol.9 , pp. 1121-1133
    • LeVine, H.1
  • 195
    • 34147130637 scopus 로고    scopus 로고
    • Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha-synuclein-induced toxicity
    • [195] Emadi, S., Barkhordarian, H., Wang, M.S., Schulz, P., Sierks, M.R., Isolation of a human single chain antibody fragment against oligomeric alpha-synuclein that inhibits aggregation and prevents alpha-synuclein-induced toxicity. J. Mol. Biol. 368 (2007), 1132–1144.
    • (2007) J. Mol. Biol. , vol.368 , pp. 1132-1144
    • Emadi, S.1    Barkhordarian, H.2    Wang, M.S.3    Schulz, P.4    Sierks, M.R.5
  • 196
    • 0037154165 scopus 로고    scopus 로고
    • Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity
    • [196] Khoshnan, A., Ko, J., Patterson, P.H., Effects of intracellular expression of anti-huntingtin antibodies of various specificities on mutant huntingtin aggregation and toxicity. Proc. Natl. Acad. Sci. U. S. A. 99 (2002), 1002–1007.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1002-1007
    • Khoshnan, A.1    Ko, J.2    Patterson, P.H.3
  • 198
    • 34548146119 scopus 로고    scopus 로고
    • Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements
    • [198] Asuni, A.A., Boutajangout, A., Quartermain, D., Sigurdsson, E.M., Immunotherapy targeting pathological tau conformers in a tangle mouse model reduces brain pathology with associated functional improvements. J. Neurosci. 27 (2007), 9115–9129.
    • (2007) J. Neurosci. , vol.27 , pp. 9115-9129
    • Asuni, A.A.1    Boutajangout, A.2    Quartermain, D.3    Sigurdsson, E.M.4
  • 199
    • 77954656871 scopus 로고    scopus 로고
    • Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice
    • [199] Boimel, M., Grigoriadis, N., Lourbopoulos, A., Haber, E., Abramsky, O., Rosenmann, H., Efficacy and safety of immunization with phosphorylated tau against neurofibrillary tangles in mice. Exp. Neurol. 224 (2010), 472–485.
    • (2010) Exp. Neurol. , vol.224 , pp. 472-485
    • Boimel, M.1    Grigoriadis, N.2    Lourbopoulos, A.3    Haber, E.4    Abramsky, O.5    Rosenmann, H.6
  • 200
    • 0042838303 scopus 로고    scopus 로고
    • Alzheimer's disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss
    • [200] Gong, Y., Chang, L., Viola, K.L., Lacor, P.N., Lambert, M.P., Finch, C.E., Krafft, G.A., Klein, W.L., Alzheimer's disease-affected brain: presence of oligomeric A beta ligands (ADDLs) suggests a molecular basis for reversible memory loss. Proc. Natl. Acad. Sci. U. S. A. 100 (2003), 10417–10422.
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 10417-10422
    • Gong, Y.1    Chang, L.2    Viola, K.L.3    Lacor, P.N.4    Lambert, M.P.5    Finch, C.E.6    Krafft, G.A.7    Klein, W.L.8
  • 202
    • 33646865770 scopus 로고    scopus 로고
    • Diagnostic and therapeutic potential of amyloid-reactive IgG antibodies contained in human sera
    • [202] O'Nuallain, B., Hrncic, R., Wall, J.S., Weiss, D.T., Solomon, A., Diagnostic and therapeutic potential of amyloid-reactive IgG antibodies contained in human sera. J. Immunol. 176 (2006), 7071–7078.
    • (2006) J. Immunol. , vol.176 , pp. 7071-7078
    • O'Nuallain, B.1    Hrncic, R.2    Wall, J.S.3    Weiss, D.T.4    Solomon, A.5
  • 203
    • 78649754766 scopus 로고    scopus 로고
    • Amyloid-beta oligomer specificity mediated by the IgM isotype–implications for a specific protective mechanism exerted by endogenous auto-antibodies
    • [203] Lindhagen-Persson, M., Brannstrom, K., Vestling, M., Steinitz, M., Olofsson, A., Amyloid-beta oligomer specificity mediated by the IgM isotype–implications for a specific protective mechanism exerted by endogenous auto-antibodies. PLoS One, 5, 2010, e13928.
    • (2010) PLoS One , vol.5 , pp. e13928
    • Lindhagen-Persson, M.1    Brannstrom, K.2    Vestling, M.3    Steinitz, M.4    Olofsson, A.5
  • 204
    • 79955554760 scopus 로고    scopus 로고
    • alpha-synuclein reactive antibodies as diagnostic biomarkers in blood sera of Parkinson's disease patients
    • [204] Yanamandra, K., Gruden, M.A., Casaite, V., Meskys, R., Forsgren, L., Morozova-Roche, L.A., alpha-synuclein reactive antibodies as diagnostic biomarkers in blood sera of Parkinson's disease patients. PLoS One, 6, 2011, e18513.
    • (2011) PLoS One , vol.6 , pp. e18513
    • Yanamandra, K.1    Gruden, M.A.2    Casaite, V.3    Meskys, R.4    Forsgren, L.5    Morozova-Roche, L.A.6
  • 209
    • 51749097108 scopus 로고    scopus 로고
    • Immunotherapy and naturally occurring autoantibodies in neurodegenerative disorders
    • [209] Neff, F., Wei, X., Nolker, C., Bacher, M., Du, Y., Dodel, R., Immunotherapy and naturally occurring autoantibodies in neurodegenerative disorders. Autoimmun. Rev. 7 (2008), 501–507.
    • (2008) Autoimmun. Rev. , vol.7 , pp. 501-507
    • Neff, F.1    Wei, X.2    Nolker, C.3    Bacher, M.4    Du, Y.5    Dodel, R.6
  • 210
    • 33750681275 scopus 로고    scopus 로고
    • Detection of circulating antibodies against tau protein in its unphosphorylated and in its neurofibrillary tangles-related phosphorylated state in Alzheimer's disease and healthy subjects
    • [210] Rosenmann, H., Meiner, Z., Geylis, V., Abramsky, O., Steinitz, M., Detection of circulating antibodies against tau protein in its unphosphorylated and in its neurofibrillary tangles-related phosphorylated state in Alzheimer's disease and healthy subjects. Neurosci. Lett. 410 (2006), 90–93.
    • (2006) Neurosci. Lett. , vol.410 , pp. 90-93
    • Rosenmann, H.1    Meiner, Z.2    Geylis, V.3    Abramsky, O.4    Steinitz, M.5
  • 213
    • 50549094090 scopus 로고    scopus 로고
    • The potential of intracellular antibodies for therapeutic targeting of protein-misfolding diseases
    • [213] Cardinale, A., Biocca, S., The potential of intracellular antibodies for therapeutic targeting of protein-misfolding diseases. Trends Mol. Med. 14 (2008), 373–380.
    • (2008) Trends Mol. Med. , vol.14 , pp. 373-380
    • Cardinale, A.1    Biocca, S.2
  • 216
    • 84879601934 scopus 로고    scopus 로고
    • Current advances in the treatment of Alzheimer's disease: focused on considerations targeting Abeta and tau
    • [216] Hong-Qi, Y., Zhi-Kun, S., Sheng-Di, C., Current advances in the treatment of Alzheimer's disease: focused on considerations targeting Abeta and tau. Transl. Neurodegener., 1, 2012, 21.
    • (2012) Transl. Neurodegener. , vol.1 , pp. 21
    • Hong-Qi, Y.1    Zhi-Kun, S.2    Sheng-Di, C.3
  • 217
    • 33750731675 scopus 로고    scopus 로고
    • 100 years and counting: prospects for defeating Alzheimer's disease
    • [217] Roberson, E.D., Mucke, L., 100 years and counting: prospects for defeating Alzheimer's disease. Science 314 (2006), 781–784.
    • (2006) Science , vol.314 , pp. 781-784
    • Roberson, E.D.1    Mucke, L.2
  • 218
    • 84904413178 scopus 로고    scopus 로고
    • Role of medium chain triglycerides (Axona(R)) in the treatment of mild to moderate Alzheimer's disease
    • [218] Sharma, A., Bemis, M., Desilets, A.R., Role of medium chain triglycerides (Axona(R)) in the treatment of mild to moderate Alzheimer's disease. Am. J. Alzheimers Dis. Other Dement. 29 (2014), 409–414.
    • (2014) Am. J. Alzheimers Dis. Other Dement. , vol.29 , pp. 409-414
    • Sharma, A.1    Bemis, M.2    Desilets, A.R.3
  • 219
    • 0037176848 scopus 로고    scopus 로고
    • Levodopa strengths and weaknesses
    • [219] Jankovic, J., Levodopa strengths and weaknesses. Neurology 58 (2002), S19–S32.
    • (2002) Neurology , vol.58 , pp. S19-S32
    • Jankovic, J.1
  • 220
    • 0033595201 scopus 로고    scopus 로고
    • A 3-year randomized trial of ropinirole and bromocriptine in early Parkinson's disease. The 053 Study Group
    • [220] Korczyn, A.D., Brunt, E.R., Larsen, J.P., Nagy, Z., Poewe, W.H., Ruggieri, S., A 3-year randomized trial of ropinirole and bromocriptine in early Parkinson's disease. The 053 Study Group. Neurology 53 (1999), 364–370.
    • (1999) Neurology , vol.53 , pp. 364-370
    • Korczyn, A.D.1    Brunt, E.R.2    Larsen, J.P.3    Nagy, Z.4    Poewe, W.H.5    Ruggieri, S.6
  • 221
    • 0032910048 scopus 로고    scopus 로고
    • Efficacy and tolerability of a novel sublingual apomorphine preparation in patients with fluctuating Parkinson's disease
    • [221] Ondo, W., Hunter, C., Almaguer, M., Gancher, S., Jankovic, J., Efficacy and tolerability of a novel sublingual apomorphine preparation in patients with fluctuating Parkinson's disease. Clin. Neuropharmacol. 22 (1999), 1–4.
    • (1999) Clin. Neuropharmacol. , vol.22 , pp. 1-4
    • Ondo, W.1    Hunter, C.2    Almaguer, M.3    Gancher, S.4    Jankovic, J.5
  • 222
    • 34249033784 scopus 로고    scopus 로고
    • Transdermal rotigotine: double-blind, placebo-controlled trial in Parkinson disease
    • [222] Jankovic, J., Watts, R.L., Martin, W., Boroojerdi, B., Transdermal rotigotine: double-blind, placebo-controlled trial in Parkinson disease. Arch. Neurol. 64 (2007), 676–682.
    • (2007) Arch. Neurol. , vol.64 , pp. 676-682
    • Jankovic, J.1    Watts, R.L.2    Martin, W.3    Boroojerdi, B.4
  • 223
    • 0035668372 scopus 로고    scopus 로고
    • Huntington's disease
    • [223] Davies, S., Ramsden, D.B., Huntington's disease. Mol. Pathol. 54 (2001), 409–413.
    • (2001) Mol. Pathol. , vol.54 , pp. 409-413
    • Davies, S.1    Ramsden, D.B.2
  • 224
    • 79951974420 scopus 로고    scopus 로고
    • Tetrabenazine: the first approved drug for the treatment of chorea in US patients with Huntington disease
    • [224] Frank, S., Tetrabenazine: the first approved drug for the treatment of chorea in US patients with Huntington disease. Neuropsychiatr. Dis. Treat. 6 (2010), 657–665.
    • (2010) Neuropsychiatr. Dis. Treat. , vol.6 , pp. 657-665
    • Frank, S.1
  • 225
    • 77954103868 scopus 로고    scopus 로고
    • Motor neuron diversity in development and disease
    • [225] Kanning, K.C., Kaplan, A., Henderson, C.E., Motor neuron diversity in development and disease. Annu. Rev. Neurosci. 33 (2010), 409–440.
    • (2010) Annu. Rev. Neurosci. , vol.33 , pp. 409-440
    • Kanning, K.C.1    Kaplan, A.2    Henderson, C.E.3
  • 226
    • 44649173763 scopus 로고    scopus 로고
    • Riluzole blocks persistent Na+ and Ca2+ currents and modulates release of glutamate via presynaptic NMDA receptors on neonatal rat hypoglossal motoneurons in vitro
    • [226] Lamanauskas, N., Nistri, A., Riluzole blocks persistent Na+ and Ca2+ currents and modulates release of glutamate via presynaptic NMDA receptors on neonatal rat hypoglossal motoneurons in vitro. Eur. J. Neurosci. 27 (2008), 2501–2514.
    • (2008) Eur. J. Neurosci. , vol.27 , pp. 2501-2514
    • Lamanauskas, N.1    Nistri, A.2
  • 227
    • 77953368849 scopus 로고    scopus 로고
    • Evidence-based drug treatment in amyotrophic lateral sclerosis and upcoming clinical trials
    • [227] Ludolph, A.C., Jesse, S., Evidence-based drug treatment in amyotrophic lateral sclerosis and upcoming clinical trials. Ther. Adv. Neurol. Disord. 2 (2009), 319–326.
    • (2009) Ther. Adv. Neurol. Disord. , vol.2 , pp. 319-326
    • Ludolph, A.C.1    Jesse, S.2
  • 228
    • 84977664415 scopus 로고    scopus 로고
    • Therapeutic progress in amyotrophic lateral sclerosis-beginning to learning
    • [228] V. Kumar, A. Islam, M.I. Hassan, F. Ahmad, Therapeutic progress in amyotrophic lateral sclerosis-beginning to learning, Eur. J. Med. Chem. http://dx.doi.org/10.1016/j.ejmech.2016.06.017.
    • Eur. J. Med. Chem.
    • Kumar, V.1    Islam, A.2    Hassan, M.I.3    Ahmad, F.4
  • 229
    • 84921531498 scopus 로고    scopus 로고
    • Insight into inhibition of the human amyloid beta protein precursor (APP: PDB ID) using (E)-N-(pyridin-2-ylmethylene)arylamine (LR) models: structure elucidation of a family of ZnX2-LR complexes
    • [229] Basu Baul, T.S., Kundu, S., Singh, P., Shaveta, Guedes da Silva, M.F., Insight into inhibition of the human amyloid beta protein precursor (APP: PDB ID ) using (E)-N-(pyridin-2-ylmethylene)arylamine (LR) models: structure elucidation of a family of ZnX2-LR complexes. Dalton Trans. 44 (2015), 2359–2369.
    • (2015) Dalton Trans. , vol.44 , pp. 2359-2369
    • Basu Baul, T.S.1    Kundu, S.2    Singh, P.3    Shaveta4    Guedes da Silva, M.F.5
  • 231
    • 84889263105 scopus 로고    scopus 로고
    • Inhibition of amyloid-beta production by anti-amyloid precursor protein antibodies in primary mouse cortical neurones
    • [231] Thomas, R.S., Hvoslef-Eide, M., Good, M.A., Kidd, E.J., Inhibition of amyloid-beta production by anti-amyloid precursor protein antibodies in primary mouse cortical neurones. Neuroreport 24 (2013), 1058–1061.
    • (2013) Neuroreport , vol.24 , pp. 1058-1061
    • Thomas, R.S.1    Hvoslef-Eide, M.2    Good, M.A.3    Kidd, E.J.4
  • 232
    • 84885165023 scopus 로고    scopus 로고
    • Suppression of amyloid-beta production by 24S-hydroxycholesterol via inhibition of intracellular amyloid precursor protein trafficking
    • [232] Urano, Y., Ochiai, S., Noguchi, N., Suppression of amyloid-beta production by 24S-hydroxycholesterol via inhibition of intracellular amyloid precursor protein trafficking. FASEB J. 27 (2013), 4305–4315.
    • (2013) FASEB J. , vol.27 , pp. 4305-4315
    • Urano, Y.1    Ochiai, S.2    Noguchi, N.3
  • 233
    • 84868687820 scopus 로고    scopus 로고
    • Glycogen synthase kinase 3 inhibition promotes lysosomal biogenesis and autophagic degradation of the amyloid-beta precursor protein
    • [233] Parr, C., Carzaniga, R., Gentleman, S.M., Van Leuven, F., Walter, J., Sastre, M., Glycogen synthase kinase 3 inhibition promotes lysosomal biogenesis and autophagic degradation of the amyloid-beta precursor protein. Mol. Cell Biol. 32 (2012), 4410–4418.
    • (2012) Mol. Cell Biol. , vol.32 , pp. 4410-4418
    • Parr, C.1    Carzaniga, R.2    Gentleman, S.M.3    Van Leuven, F.4    Walter, J.5    Sastre, M.6
  • 234
    • 84862867033 scopus 로고    scopus 로고
    • Pyruvate prevents the inhibition of the long-term potentiation induced by amyloid-beta through protein phosphatase 2A inactivation
    • [234] Wang, X., Takata, T., Bai, X., Ou, F., Yokono, K., Sakurai, T., Pyruvate prevents the inhibition of the long-term potentiation induced by amyloid-beta through protein phosphatase 2A inactivation. J. Alzheimers Dis. 30 (2012), 665–673.
    • (2012) J. Alzheimers Dis. , vol.30 , pp. 665-673
    • Wang, X.1    Takata, T.2    Bai, X.3    Ou, F.4    Yokono, K.5    Sakurai, T.6
  • 235
    • 77956920667 scopus 로고    scopus 로고
    • Icariin attenuates beta-amyloid-induced neurotoxicity by inhibition of tau protein hyperphosphorylation in PC12 cells
    • [235] Zeng, K.W., Ko, H., Yang, H.O., Wang, X.M., Icariin attenuates beta-amyloid-induced neurotoxicity by inhibition of tau protein hyperphosphorylation in PC12 cells. Neuropharmacology 59 (2010), 542–550.
    • (2010) Neuropharmacology , vol.59 , pp. 542-550
    • Zeng, K.W.1    Ko, H.2    Yang, H.O.3    Wang, X.M.4
  • 236
    • 84941600642 scopus 로고    scopus 로고
    • Early investigational drugs targeting tau protein for the treatment of Alzheimer's disease
    • [236] Anand, K., Sabbagh, M., Early investigational drugs targeting tau protein for the treatment of Alzheimer's disease. Expert Opin. Investig. Drugs, 2015, 1–6.
    • (2015) Expert Opin. Investig. Drugs , pp. 1-6
    • Anand, K.1    Sabbagh, M.2
  • 237
    • 84925500787 scopus 로고    scopus 로고
    • Inhibition of HDAC6 modifies tau inclusion body formation and impairs autophagic clearance
    • [237] Leyk, J., Goldbaum, O., Noack, M., Richter-Landsberg, C., Inhibition of HDAC6 modifies tau inclusion body formation and impairs autophagic clearance. J. Mol. Neurosci. 55 (2015), 1031–1046.
    • (2015) J. Mol. Neurosci. , vol.55 , pp. 1031-1046
    • Leyk, J.1    Goldbaum, O.2    Noack, M.3    Richter-Landsberg, C.4
  • 238
    • 84919673394 scopus 로고    scopus 로고
    • Structure and mechanism of action of tau aggregation inhibitors
    • [238] Cisek, K., Cooper, G.L., Huseby, C.J., Kuret, J., Structure and mechanism of action of tau aggregation inhibitors. Curr. Alzheimer Res. 11 (2014), 918–927.
    • (2014) Curr. Alzheimer Res. , vol.11 , pp. 918-927
    • Cisek, K.1    Cooper, G.L.2    Huseby, C.J.3    Kuret, J.4
  • 239
    • 84891704820 scopus 로고    scopus 로고
    • Research progress of abnormal phosphorylation of microtubule-associated tau protein and of the targeted inhibition of the phosphorylation
    • [239] Zhou, F., Chen, S., Sun, X., Research progress of abnormal phosphorylation of microtubule-associated tau protein and of the targeted inhibition of the phosphorylation. Sheng Wu Yi Xue Gong Cheng Xue Za Zhi 29 (2012), 788–792.
    • (2012) Sheng Wu Yi Xue Gong Cheng Xue Za Zhi , vol.29 , pp. 788-792
    • Zhou, F.1    Chen, S.2    Sun, X.3
  • 240
    • 78751700479 scopus 로고    scopus 로고
    • Inhibition of glycogen synthase kinase-3beta by Angelica sinensis extract decreases beta-amyloid-induced neurotoxicity and tau phosphorylation in cultured cortical neurons
    • [240] Zhang, Z., Zhao, R., Qi, J., Wen, S., Tang, Y., Wang, D., Inhibition of glycogen synthase kinase-3beta by Angelica sinensis extract decreases beta-amyloid-induced neurotoxicity and tau phosphorylation in cultured cortical neurons. J. Neurosci. Res. 89 (2011), 437–447.
    • (2011) J. Neurosci. Res. , vol.89 , pp. 437-447
    • Zhang, Z.1    Zhao, R.2    Qi, J.3    Wen, S.4    Tang, Y.5    Wang, D.6
  • 243
    • 84883039771 scopus 로고    scopus 로고
    • Tyrosine kinase inhibition facilitates autophagic SNCA/alpha-synuclein clearance
    • [243] Hebron, M.L., Lonskaya, I., Moussa, C.E., Tyrosine kinase inhibition facilitates autophagic SNCA/alpha-synuclein clearance. Autophagy 9 (2013), 1249–1250.
    • (2013) Autophagy , vol.9 , pp. 1249-1250
    • Hebron, M.L.1    Lonskaya, I.2    Moussa, C.E.3
  • 244
    • 84869065872 scopus 로고    scopus 로고
    • Proteasomal inhibition as a treatment strategy for Parkinson's disease: the impact of alpha-synuclein on Nurr1
    • [244] Devine, M.J., Proteasomal inhibition as a treatment strategy for Parkinson's disease: the impact of alpha-synuclein on Nurr1. J. Neurosci. 32 (2012), 16071–16073.
    • (2012) J. Neurosci. , vol.32 , pp. 16071-16073
    • Devine, M.J.1
  • 246
    • 79954437554 scopus 로고    scopus 로고
    • Inhibition and disaggregation of alpha-synuclein oligomers by natural polyphenolic compounds
    • [246] Caruana, M., Hogen, T., Levin, J., Hillmer, A., Giese, A., Vassallo, N., Inhibition and disaggregation of alpha-synuclein oligomers by natural polyphenolic compounds. FEBS Lett. 585 (2011), 1113–1120.
    • (2011) FEBS Lett. , vol.585 , pp. 1113-1120
    • Caruana, M.1    Hogen, T.2    Levin, J.3    Hillmer, A.4    Giese, A.5    Vassallo, N.6
  • 247
    • 84920374074 scopus 로고    scopus 로고
    • HDAC inhibition imparts beneficial transgenerational effects in Huntington's disease mice via altered DNA and histone methylation
    • [247] Jia, H., Morris, C.D., Williams, R.M., Loring, J.F., Thomas, E.A., HDAC inhibition imparts beneficial transgenerational effects in Huntington's disease mice via altered DNA and histone methylation. Proc. Natl. Acad. Sci. U. S. A. 112 (2015), E56–E64.
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. E56-E64
    • Jia, H.1    Morris, C.D.2    Williams, R.M.3    Loring, J.F.4    Thomas, E.A.5
  • 248
    • 84906096688 scopus 로고    scopus 로고
    • Therapeutic approaches for inhibition of protein aggregation in Huntington's disease
    • [248] Kim, S., Kim, K.T., Therapeutic approaches for inhibition of protein aggregation in Huntington's disease. Exp. Neurobiol. 23 (2014), 36–44.
    • (2014) Exp. Neurobiol. , vol.23 , pp. 36-44
    • Kim, S.1    Kim, K.T.2
  • 249
    • 84901357581 scopus 로고    scopus 로고
    • Deciphering the roles of trehalose and Hsp104 in the inhibition of aggregation of mutant huntingtin in a yeast model of Huntington's disease
    • [249] Chaudhary, R.K., Kardani, J., Singh, K., Banerjee, R., Roy, I., Deciphering the roles of trehalose and Hsp104 in the inhibition of aggregation of mutant huntingtin in a yeast model of Huntington's disease. Neuromol. Med. 16 (2014), 280–291.
    • (2014) Neuromol. Med. , vol.16 , pp. 280-291
    • Chaudhary, R.K.1    Kardani, J.2    Singh, K.3    Banerjee, R.4    Roy, I.5
  • 250
    • 84859509100 scopus 로고    scopus 로고
    • Disrupted GABAAR trafficking and synaptic inhibition in a mouse model of Huntington's disease
    • [250] Yuen, E.Y., Wei, J., Zhong, P., Yan, Z., Disrupted GABAAR trafficking and synaptic inhibition in a mouse model of Huntington's disease. Neurobiol. Dis. 46 (2012), 497–502.
    • (2012) Neurobiol. Dis. , vol.46 , pp. 497-502
    • Yuen, E.Y.1    Wei, J.2    Zhong, P.3    Yan, Z.4
  • 252
    • 79953803100 scopus 로고    scopus 로고
    • Pyrimidine-2,4,6-trione derivatives and their inhibition of mutant SOD1-dependent protein aggregation. Toward a treatment for amyotrophic lateral sclerosis
    • [252] Xia, G., Benmohamed, R., Kim, J., Arvanites, A.C., Morimoto, R.I., Ferrante, R.J., Kirsch, D.R., Silverman, R.B., Pyrimidine-2,4,6-trione derivatives and their inhibition of mutant SOD1-dependent protein aggregation. Toward a treatment for amyotrophic lateral sclerosis. J. Med. Chem. 54 (2011), 2409–2421.
    • (2011) J. Med. Chem. , vol.54 , pp. 2409-2421
    • Xia, G.1    Benmohamed, R.2    Kim, J.3    Arvanites, A.C.4    Morimoto, R.I.5    Ferrante, R.J.6    Kirsch, D.R.7    Silverman, R.B.8
  • 253
    • 84939974477 scopus 로고    scopus 로고
    • RNA-targeted therapeutics for ALS
    • [253] Reddy, L.V., Miller, T.M., RNA-targeted therapeutics for ALS. Neurotherapeutics 12 (2015), 424–427.
    • (2015) Neurotherapeutics , vol.12 , pp. 424-427
    • Reddy, L.V.1    Miller, T.M.2
  • 254
    • 84881638591 scopus 로고    scopus 로고
    • Autophagy activation and neuroprotection by progesterone in the G93A-SOD1 transgenic mouse model of amyotrophic lateral sclerosis
    • [254] Kim, J., Kim, T.Y., Cho, K.S., Kim, H.N., Koh, J.Y., Autophagy activation and neuroprotection by progesterone in the G93A-SOD1 transgenic mouse model of amyotrophic lateral sclerosis. Neurobiol. Dis. 59 (2013), 80–85.
    • (2013) Neurobiol. Dis. , vol.59 , pp. 80-85
    • Kim, J.1    Kim, T.Y.2    Cho, K.S.3    Kim, H.N.4    Koh, J.Y.5
  • 257
    • 84860217270 scopus 로고    scopus 로고
    • Inhibition of amyloid precursor protein beta-secretase cleavage site affects survival and motor functions of amyotrophic lateral sclerosis transgenic mice
    • [257] Rabinovich-Toidman, P., Becker, M., Barbiro, B., Solomon, B., Inhibition of amyloid precursor protein beta-secretase cleavage site affects survival and motor functions of amyotrophic lateral sclerosis transgenic mice. Neurodegener. Dis. 10 (2012), 30–33.
    • (2012) Neurodegener. Dis. , vol.10 , pp. 30-33
    • Rabinovich-Toidman, P.1    Becker, M.2    Barbiro, B.3    Solomon, B.4
  • 258
    • 84892683414 scopus 로고    scopus 로고
    • Nuclear TAR DNA-binding protein 43: a new target for amyotrophic lateral sclerosis treatment
    • [258] Zheng, M., Shi, Y., Fan, D., Nuclear TAR DNA-binding protein 43: a new target for amyotrophic lateral sclerosis treatment. Neural Regen. Res. 8 (2013), 3284–3295.
    • (2013) Neural Regen. Res. , vol.8 , pp. 3284-3295
    • Zheng, M.1    Shi, Y.2    Fan, D.3
  • 259
    • 84921455929 scopus 로고    scopus 로고
    • In silico studies and fluorescence binding assays of potential anti-prion compounds reveal an important binding site for prion inhibition from PrP(C) to PrP(Sc)
    • [259] Pagadala, N.S., Perez-Pineiro, R., Wishart, D.S., Tuszynski, J.A., In silico studies and fluorescence binding assays of potential anti-prion compounds reveal an important binding site for prion inhibition from PrP(C) to PrP(Sc). Eur. J. Med. Chem. 91 (2015), 118–131.
    • (2015) Eur. J. Med. Chem. , vol.91 , pp. 118-131
    • Pagadala, N.S.1    Perez-Pineiro, R.2    Wishart, D.S.3    Tuszynski, J.A.4
  • 261
    • 84874818722 scopus 로고    scopus 로고
    • The molecular mechanism of Hsp100 chaperone inhibition by the prion curing agent guanidinium chloride
    • [261] Zeymer, C., Werbeck, N.D., Schlichting, I., Reinstein, J., The molecular mechanism of Hsp100 chaperone inhibition by the prion curing agent guanidinium chloride. J. Biol. Chem. 288 (2013), 7065–7076.
    • (2013) J. Biol. Chem. , vol.288 , pp. 7065-7076
    • Zeymer, C.1    Werbeck, N.D.2    Schlichting, I.3    Reinstein, J.4
  • 262
    • 84865342901 scopus 로고    scopus 로고
    • Inhibition of cytosolic Phospholipase A2 prevents prion peptide-induced neuronal damage and co-localisation with Beta III Tubulin
    • [262] Last, V., Williams, A., Werling, D., Inhibition of cytosolic Phospholipase A2 prevents prion peptide-induced neuronal damage and co-localisation with Beta III Tubulin. BMC Neurosci., 13, 2012, 106.
    • (2012) BMC Neurosci. , vol.13 , pp. 106
    • Last, V.1    Williams, A.2    Werling, D.3
  • 264
    • 84865139100 scopus 로고    scopus 로고
    • Antibody-mediated inhibition of integrin alpha5beta1 blocks neurotoxic prion peptide PrP106-126-induced activation of BV2 microglia
    • [264] Chang, J., Yang, L., Kouadir, M., Peng, Y., Zhang, S., Shi, F., Zhou, X., Yin, X., Zhao, D., Antibody-mediated inhibition of integrin alpha5beta1 blocks neurotoxic prion peptide PrP106-126-induced activation of BV2 microglia. J. Mol. Neurosci. 48 (2012), 248–252.
    • (2012) J. Mol. Neurosci. , vol.48 , pp. 248-252
    • Chang, J.1    Yang, L.2    Kouadir, M.3    Peng, Y.4    Zhang, S.5    Shi, F.6    Zhou, X.7    Yin, X.8    Zhao, D.9
  • 265
    • 80455155974 scopus 로고    scopus 로고
    • Analysis of nucleic acid chaperoning by the prion protein and its inhibition by oligonucleotides
    • [265] Guichard, C., Ivanyi-Nagy, R., Sharma, K.K., Gabus, C., Marc, D., Mely, Y., Darlix, J.L., Analysis of nucleic acid chaperoning by the prion protein and its inhibition by oligonucleotides. Nucleic Acids Res. 39 (2011), 8544–8558.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 8544-8558
    • Guichard, C.1    Ivanyi-Nagy, R.2    Sharma, K.K.3    Gabus, C.4    Marc, D.5    Mely, Y.6    Darlix, J.L.7
  • 266
    • 78449257695 scopus 로고    scopus 로고
    • Calcineurin inhibition at the clinical phase of prion disease reduces neurodegeneration, improves behavioral alterations and increases animal survival
    • [266] Mukherjee, A., Morales-Scheihing, D., Gonzalez-Romero, D., Green, K., Taglialatela, G., Soto, C., Calcineurin inhibition at the clinical phase of prion disease reduces neurodegeneration, improves behavioral alterations and increases animal survival. PLoS Pathog., 6, 2010, e1001138.
    • (2010) PLoS Pathog. , vol.6 , pp. e1001138
    • Mukherjee, A.1    Morales-Scheihing, D.2    Gonzalez-Romero, D.3    Green, K.4    Taglialatela, G.5    Soto, C.6
  • 267
    • 74449085875 scopus 로고    scopus 로고
    • The inhibition of prions through blocking prion conversion by permanently charged branched polyamines of low cytotoxicity
    • [267] Lim, Y.B., Mays, C.E., Kim, Y., Titlow, W.B., Ryou, C., The inhibition of prions through blocking prion conversion by permanently charged branched polyamines of low cytotoxicity. Biomaterials 31 (2010), 2025–2033.
    • (2010) Biomaterials , vol.31 , pp. 2025-2033
    • Lim, Y.B.1    Mays, C.E.2    Kim, Y.3    Titlow, W.B.4    Ryou, C.5
  • 268
    • 84945315616 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibition with linagliptin and effects on hyperglycaemia and albuminuria in patients with type 2 diabetes and renal dysfunction: rationale and design of the MARLINA-T2D trial
    • [268] Groop, P.H., Cooper, M.E., Perkovic, V., Sharma, K., Schernthaner, G., Haneda, M., Hocher, B., Gordat, M., Cescutti, J., Woerle, H.J., von Eynatten, M., Dipeptidyl peptidase-4 inhibition with linagliptin and effects on hyperglycaemia and albuminuria in patients with type 2 diabetes and renal dysfunction: rationale and design of the MARLINA-T2D trial. Diab Vasc. Dis. Res. 12 (2015), 455–462.
    • (2015) Diab Vasc. Dis. Res. , vol.12 , pp. 455-462
    • Groop, P.H.1    Cooper, M.E.2    Perkovic, V.3    Sharma, K.4    Schernthaner, G.5    Haneda, M.6    Hocher, B.7    Gordat, M.8    Cescutti, J.9    Woerle, H.J.10    von Eynatten, M.11
  • 269
    • 84899091067 scopus 로고    scopus 로고
    • Dipeptidyl peptidase-4 inhibition in patients with type 2 diabetes treated with saxagliptin, sitagliptin, or vildagliptin
    • [269] Tatosian, D.A., Guo, Y., Schaeffer, A.K., Gaibu, N., Popa, S., Stoch, A., Langdon, R.B., Kauh, E.A., Dipeptidyl peptidase-4 inhibition in patients with type 2 diabetes treated with saxagliptin, sitagliptin, or vildagliptin. Diabetes Ther. 4 (2013), 431–442.
    • (2013) Diabetes Ther. , vol.4 , pp. 431-442
    • Tatosian, D.A.1    Guo, Y.2    Schaeffer, A.K.3    Gaibu, N.4    Popa, S.5    Stoch, A.6    Langdon, R.B.7    Kauh, E.A.8
  • 270
    • 84886890870 scopus 로고    scopus 로고
    • SGLT2 inhibition with dapagliflozin – a novel approach for the management of type 2 diabetes
    • [270] Kilov, G., Leow, S., Thomas, M., SGLT2 inhibition with dapagliflozin – a novel approach for the management of type 2 diabetes. Aust. Fam. Physician 42 (2013), 706–710.
    • (2013) Aust. Fam. Physician , vol.42 , pp. 706-710
    • Kilov, G.1    Leow, S.2    Thomas, M.3
  • 271
    • 84876417308 scopus 로고    scopus 로고
    • Cyclic AMP and PKA: how can a lot of good come from the potentially bad? : editorial to: “phosphodiesterase III inhibition increases cAMP levels and augments the infarct size limiting effect of a DPP-4 inhibitor in mice with type-2 diabetes mellitus” by Y. Birnbaum et al
    • [271] Huisamen, B., Cyclic AMP and PKA: how can a lot of good come from the potentially bad? : editorial to: “phosphodiesterase III inhibition increases cAMP levels and augments the infarct size limiting effect of a DPP-4 inhibitor in mice with type-2 diabetes mellitus” by Y. Birnbaum et al. Cardiovasc. Drugs Ther. 26 (2012), 435–436.
    • (2012) Cardiovasc. Drugs Ther. , vol.26 , pp. 435-436
    • Huisamen, B.1
  • 273
    • 84921046996 scopus 로고    scopus 로고
    • Tuning transthyretin amyloidosis inhibition properties of iododiflunisal by combinatorial engineering of the nonsalicylic ring substitutions
    • [273] Vilaro, M., Nieto, J., La Parra, J.R., Almeida, M.R., Ballesteros, A., Planas, A., Arsequell, G., Valencia, G., Tuning transthyretin amyloidosis inhibition properties of iododiflunisal by combinatorial engineering of the nonsalicylic ring substitutions. ACS Comb. Sci. 17 (2015), 32–38.
    • (2015) ACS Comb. Sci. , vol.17 , pp. 32-38
    • Vilaro, M.1    Nieto, J.2    La Parra, J.R.3    Almeida, M.R.4    Ballesteros, A.5    Planas, A.6    Arsequell, G.7    Valencia, G.8
  • 275
    • 84875073880 scopus 로고    scopus 로고
    • Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis
    • [275] Sant'anna, R.O., Braga, C.A., Polikarpov, I., Ventura, S., Lima, L.M., Foguel, D., Inhibition of human transthyretin aggregation by non-steroidal anti-inflammatory compounds: a structural and thermodynamic analysis. Int. J. Mol. Sci. 14 (2013), 5284–5311.
    • (2013) Int. J. Mol. Sci. , vol.14 , pp. 5284-5311
    • Sant'anna, R.O.1    Braga, C.A.2    Polikarpov, I.3    Ventura, S.4    Lima, L.M.5    Foguel, D.6
  • 276
    • 84868592337 scopus 로고    scopus 로고
    • Dietary curcumin counteracts extracellular transthyretin deposition: insights on the mechanism of amyloid inhibition
    • [276] Ferreira, N., Santos, S.A., Domingues, M.R., Saraiva, M.J., Almeida, M.R., Dietary curcumin counteracts extracellular transthyretin deposition: insights on the mechanism of amyloid inhibition. Biochim. Biophys. Acta 1832 (2013), 39–45.
    • (2013) Biochim. Biophys. Acta , vol.1832 , pp. 39-45
    • Ferreira, N.1    Santos, S.A.2    Domingues, M.R.3    Saraiva, M.J.4    Almeida, M.R.5
  • 279
    • 84904559289 scopus 로고    scopus 로고
    • Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly
    • [279] Karamanos, T.K., Kalverda, A.P., Thompson, G.S., Radford, S.E., Visualization of transient protein-protein interactions that promote or inhibit amyloid assembly. Mol. Cell 55 (2014), 214–226.
    • (2014) Mol. Cell , vol.55 , pp. 214-226
    • Karamanos, T.K.1    Kalverda, A.P.2    Thompson, G.S.3    Radford, S.E.4


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