메뉴 건너뛰기




Volumn 425, Issue 14, 2013, Pages 2397-2411

Nanobodies raised against monomeric α-synuclein distinguish between fibrils at different maturation stages

Author keywords

amyloid; fibril; ITC; nanobody; NMR; synuclein

Indexed keywords

ALPHA SYNUCLEIN; NANOBODY; NANOBODY NBSYN2; NANOBODY NBSYN87; UNCLASSIFIED DRUG;

EID: 84879554975     PISSN: 00222836     EISSN: 10898638     Source Type: Journal    
DOI: 10.1016/j.jmb.2013.01.040     Document Type: Article
Times cited : (86)

References (60)
  • 1
    • 0031989197 scopus 로고    scopus 로고
    • Parkinsonism: Onset, progression, and mortality. 1967
    • M.M. Hoehn, and M.D. Yahr Parkinsonism: onset, progression, and mortality. 1967 Neurology 50 1998 318 334
    • (1998) Neurology , vol.50 , pp. 318-334
    • Hoehn, M.M.1    Yahr, M.D.2
  • 2
    • 0029981526 scopus 로고    scopus 로고
    • Neuropathology of Parkinson's disease
    • L.S. Forno 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
  • 3
    • 0031941058 scopus 로고    scopus 로고
    • Aggregation of α-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies
    • M. Baba, S. Nakajo, P.H. Tu, T. Tomita, K. Nakaya, and V.M. Lee Aggregation of α-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies Am. J. Pathol. 152 1998 879 884
    • (1998) Am. J. Pathol. , vol.152 , pp. 879-884
    • Baba, M.1    Nakajo, S.2    Tu, P.H.3    Tomita, T.4    Nakaya, K.5    Lee, V.M.6
  • 4
    • 22244442489 scopus 로고    scopus 로고
    • The biochemistry of Parkinson's disease
    • M.R. Cookson The biochemistry of Parkinson's disease Annu. Rev. Biochem. 74 2005 29 52
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 29-52
    • Cookson, M.R.1
  • 5
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • F. Chiti, and C.M. Dobson 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
  • 8
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease
    • R. Kruger, W. Kuhn, T. Muller, D. Woitalla, M. Graeber, and S. Kosel Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease Nat. Genet. 18 1998 106 108
    • (1998) Nat. Genet. , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3    Woitalla, D.4    Graeber, M.5    Kosel, S.6
  • 10
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-synuclein gene identified in families with Parkinson's disease
    • M.H. Polymeropoulos, C. Lavedan, E. Leroy, S.E. Ide, A. Dehejia, and A. Dutra Mutation in the α-synuclein gene identified in families with Parkinson's disease Science 276 1997 2045 2047
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5    Dutra, A.6
  • 12
    • 0032546895 scopus 로고    scopus 로고
    • α-Synuclein immunoreactivity in glial cytoplasmic inclusions in multiple system atrophy
    • K. Wakabayashi, M. Yoshimoto, S. Tsuji, and H. Takahashi α-Synuclein immunoreactivity in glial cytoplasmic inclusions in multiple system atrophy Neurosci. Lett. 249 1998 180 182
    • (1998) Neurosci. Lett. , vol.249 , pp. 180-182
    • Wakabayashi, K.1    Yoshimoto, M.2    Tsuji, S.3    Takahashi, H.4
  • 13
    • 0031713491 scopus 로고    scopus 로고
    • Glial cytoplasmic inclusions in white matter oligodendrocytes of multiple system atrophy brains contain insoluble α-synuclein
    • P.H. Tu, J.E. Galvin, M. Baba, B. Giasson, T. Tomita, and S. Leight Glial cytoplasmic inclusions in white matter oligodendrocytes of multiple system atrophy brains contain insoluble α-synuclein Ann. Neurol. 44 1998 415 422
    • (1998) Ann. Neurol. , vol.44 , pp. 415-422
    • Tu, P.H.1    Galvin, J.E.2    Baba, M.3    Giasson, B.4    Tomita, T.5    Leight, S.6
  • 14
    • 0032886707 scopus 로고    scopus 로고
    • Tau and synuclein and their role in neuropathology
    • D.W. Dickson Tau and synuclein and their role in neuropathology Brain Pathol. 9 1999 657 661
    • (1999) Brain Pathol. , vol.9 , pp. 657-661
    • Dickson, D.W.1
  • 15
  • 16
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the α-synuclein protofibril by a dopamine-α-synuclein adduct
    • K.A. Conway, J.C. Rochet, R.M. Bieganski, and P.T. Lansbury Kinetic stabilization of the α-synuclein protofibril by a dopamine-α- synuclein adduct Science 294 2001 1346 1349
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury, P.T.4
  • 17
    • 0034609561 scopus 로고    scopus 로고
    • Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse α-synuclein
    • J.C. Rochet, K.A. Conway, and P.T. Lansbury Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse α-synuclein Biochemistry 39 2000 10619 10626
    • (2000) Biochemistry , vol.39 , pp. 10619-10626
    • Rochet, J.C.1    Conway, K.A.2    Lansbury, P.T.3
  • 18
    • 0034681163 scopus 로고    scopus 로고
    • Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: Implications for pathogenesis and therapy
    • K.A. Conway, S.J. Lee, J.C. Rochet, T.T. Ding, R.E. Williamson, and P.T. Lansbury Acceleration of oligomerization, not fibrillization, is a shared property of both α-synuclein mutations linked to early-onset Parkinson's disease: implications for pathogenesis and therapy Proc. Natl Acad. Sci. USA 97 2000 571 576
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 571-576
    • Conway, K.A.1    Lee, S.J.2    Rochet, J.C.3    Ding, T.T.4    Williamson, R.E.5    Lansbury, P.T.6
  • 19
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of α-synuclein
    • N. Cremades, S.I. Cohen, E. Deas, A.Y. Abramov, A.Y. Chen, and A. Orte Direct observation of the interconversion of normal and toxic forms of α-synuclein Cell 149 2012 1048 1059
    • (2012) Cell , vol.149 , pp. 1048-1059
    • Cremades, N.1    Cohen, S.I.2    Deas, E.3    Abramov, A.Y.4    Chen, A.Y.5    Orte, A.6
  • 20
    • 0037023699 scopus 로고    scopus 로고
    • Biophysical properties of the synucleins and their propensities to fibrillate: Inhibition of α-synuclein assembly by β- And γ-synucleins
    • V.N. Uversky, J. Li, P. Souillac, I.S. Millett, S. Doniach, and R. Jakes Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of α-synuclein assembly by β- and γ-synucleins J. Biol. Chem. 277 2002 11970 11978
    • (2002) J. Biol. Chem. , vol.277 , pp. 11970-11978
    • Uversky, V.N.1    Li, J.2    Souillac, P.3    Millett, I.S.4    Doniach, S.5    Jakes, R.6
  • 21
    • 67649380327 scopus 로고    scopus 로고
    • Multiple tight phospholipid-binding modes of α-synuclein revealed by solution NMR spectroscopy
    • C.R. Bodner, C.M. Dobson, and A. Bax Multiple tight phospholipid-binding modes of α-synuclein revealed by solution NMR spectroscopy J. Mol. Biol. 390 2009 775 790
    • (2009) J. Mol. Biol. , vol.390 , pp. 775-790
    • Bodner, C.R.1    Dobson, C.M.2    Bax, A.3
  • 22
    • 15744362063 scopus 로고    scopus 로고
    • Structure and dynamics of micelle-bound human α-synuclein
    • T.S. Ulmer, A. Bax, N.B. Cole, and R.L. Nussbaum Structure and dynamics of micelle-bound human α-synuclein J. Biol. Chem. 280 2005 9595 9603
    • (2005) J. Biol. Chem. , vol.280 , pp. 9595-9603
    • Ulmer, T.S.1    Bax, A.2    Cole, N.B.3    Nussbaum, R.L.4
  • 23
    • 84859577559 scopus 로고    scopus 로고
    • α-Synuclein in the central nervous system and from erythrocytes, mammalian cells and E. coli exists predominantly as a disordered monomer
    • B. Fauvet, M.K. Mbefo, M.B. Fares, C. Desobry, S. Michael, and M.T. Ardah α-Synuclein in the central nervous system and from erythrocytes, mammalian cells and E. coli exists predominantly as a disordered monomer J. Biol. Chem. 287 2012 15345 15364
    • (2012) J. Biol. Chem. , vol.287 , pp. 15345-15364
    • Fauvet, B.1    Mbefo, M.K.2    Fares, M.B.3    Desobry, C.4    Michael, S.5    Ardah, M.T.6
  • 25
    • 80052398365 scopus 로고    scopus 로고
    • α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation
    • T. Bartels, J.G. Choi, and D.J. Selkoe α-Synuclein occurs physiologically as a helically folded tetramer that resists aggregation Nature 477 2011 107 110
    • (2011) Nature , vol.477 , pp. 107-110
    • Bartels, T.1    Choi, J.G.2    Selkoe, D.J.3
  • 26
    • 0034077041 scopus 로고    scopus 로고
    • Mice lacking α-synuclein display functional deficits in the nigrostriatal dopamine system
    • A. Abeliovich, Y. Schmitz, I. Farinas, D. Choi-Lundberg, W.H. Ho, and P.E. Castillo Mice lacking α-synuclein display functional deficits in the nigrostriatal dopamine system Neuron 25 2000 239 252
    • (2000) Neuron , vol.25 , pp. 239-252
    • Abeliovich, A.1    Schmitz, Y.2    Farinas, I.3    Choi-Lundberg, D.4    Ho, W.H.5    Castillo, P.E.6
  • 27
    • 0034193399 scopus 로고    scopus 로고
    • Synucleins are developmentally expressed, and α-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons
    • D.D. Murphy, S.M. Rueter, J.Q. Trojanowski, and V.M. Lee Synucleins are developmentally expressed, and α-synuclein regulates the size of the presynaptic vesicular pool in primary hippocampal neurons J. Neurosci. 20 2000 3214 3220
    • (2000) J. Neurosci. , vol.20 , pp. 3214-3220
    • Murphy, D.D.1    Rueter, S.M.2    Trojanowski, J.Q.3    Lee, V.M.4
  • 28
    • 0037109727 scopus 로고    scopus 로고
    • Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking α-synuclein
    • D.E. Cabin, K. Shimazu, D. Murphy, N.B. Cole, W. Gottschalk, and K.L. McIlwain Synaptic vesicle depletion correlates with attenuated synaptic responses to prolonged repetitive stimulation in mice lacking α-synuclein J. Neurosci. 22 2002 8797 8807
    • (2002) J. Neurosci. , vol.22 , pp. 8797-8807
    • Cabin, D.E.1    Shimazu, K.2    Murphy, D.3    Cole, N.B.4    Gottschalk, W.5    McIlwain, K.L.6
  • 29
    • 0034646391 scopus 로고    scopus 로고
    • Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid
    • K.A. Conway, J.D. Harper, and P.T. Lansbury Fibrils formed in vitro from α-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid Biochemistry 39 2000 2552 2563
    • (2000) Biochemistry , vol.39 , pp. 2552-2563
    • Conway, K.A.1    Harper, J.D.2    Lansbury, P.T.3
  • 30
    • 0037166267 scopus 로고    scopus 로고
    • Biochemical characterization of the core structure of α-synuclein filaments
    • H. Miake, H. Mizusawa, T. Iwatsubo, and M. Hasegawa Biochemical characterization of the core structure of α-synuclein filaments Int. J. Biol. Chem. 277 2002 19213 19219
    • (2002) Int. J. Biol. Chem. , vol.277 , pp. 19213-19219
    • Miake, H.1    Mizusawa, H.2    Iwatsubo, T.3    Hasegawa, M.4
  • 31
    • 0141733169 scopus 로고    scopus 로고
    • Structural organization of α-synuclein fibrils studied by site-directed spin labeling
    • A. Der-Sarkissian, C.C. Jao, J. Chen, and R. Langen Structural organization of α-synuclein fibrils studied by site-directed spin labeling J. Biol. Chem. 278 2003 37530 37535
    • (2003) J. Biol. Chem. , vol.278 , pp. 37530-37535
    • Der-Sarkissian, A.1    Jao, C.C.2    Chen, J.3    Langen, R.4
  • 32
    • 27344436619 scopus 로고    scopus 로고
    • Structure and properties of α-synuclein and other amyloids determined at the amino acid level
    • C. Del Mar, E.A. Greenbaum, L. Mayne, S.W. Englander, and V.L. Woods Structure and properties of α-synuclein and other amyloids determined at the amino acid level Proc. Natl Acad. Sci. USA 102 2005 15477 15482
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 15477-15482
    • Del Mar, C.1    Greenbaum, E.A.2    Mayne, L.3    Englander, S.W.4    Woods, V.L.5
  • 33
    • 27644518721 scopus 로고    scopus 로고
    • Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR
    • H. Heise, W. Hoyer, S. Becker, O.C. Andronesi, D. Riedel, and M. Baldus Molecular-level secondary structure, polymorphism, and dynamics of full-length α-synuclein fibrils studied by solid-state NMR Proc. Natl Acad. Sci. USA 102 2005 15871 15876
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 15871-15876
    • Heise, H.1    Hoyer, W.2    Becker, S.3    Andronesi, O.C.4    Riedel, D.5    Baldus, M.6
  • 34
    • 36248965693 scopus 로고    scopus 로고
    • Role of different regions of α-synuclein in the assembly of fibrils
    • Z. Qin, D. Hu, S. Han, D.-P. Hong, and A.L. Fink Role of different regions of α-synuclein in the assembly of fibrils Biochemistry 46 2007 13322 13330
    • (2007) Biochemistry , vol.46 , pp. 13322-13330
    • Qin, Z.1    Hu, D.2    Han, S.3    Hong, D.-P.4    Fink, A.L.5
  • 36
    • 70349296921 scopus 로고    scopus 로고
    • Quantitative approaches to defining normal and aberrant protein homeostasis
    • discussion 359-372
    • M. Vendruscolo, and C.M. Dobson Quantitative approaches to defining normal and aberrant protein homeostasis Faraday Discuss. 143 2009 277 291 discussion 359-372
    • (2009) Faraday Discuss. , vol.143 , pp. 277-291
    • Vendruscolo, M.1    Dobson, C.M.2
  • 37
    • 84934434673 scopus 로고    scopus 로고
    • Nanobodies as structural probes of protein misfolding and fibril formation
    • E. De Genst, and C.M. Dobson Nanobodies as structural probes of protein misfolding and fibril formation Methods Mol. Biol. 911 2012 533 558
    • (2012) Methods Mol. Biol. , vol.911 , pp. 533-558
    • De Genst, E.1    Dobson, C.M.2
  • 38
    • 0042467574 scopus 로고    scopus 로고
    • A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme
    • M. Dumoulin, A.M. Last, A. Desmyter, K. Decanniere, D. Canet, and G. Larsson A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme Nature 424 2003 783 788
    • (2003) Nature , vol.424 , pp. 783-788
    • Dumoulin, M.1    Last, A.M.2    Desmyter, A.3    Decanniere, K.4    Canet, D.5    Larsson, G.6
  • 39
    • 8844257296 scopus 로고    scopus 로고
    • Probing the origins, diagnosis and treatment of amyloid diseases using antibodies
    • M. Dumoulin, and C.M. Dobson Probing the origins, diagnosis and treatment of amyloid diseases using antibodies Biochimie 86 2004 589 600
    • (2004) Biochimie , vol.86 , pp. 589-600
    • Dumoulin, M.1    Dobson, C.M.2
  • 40
    • 77956885443 scopus 로고    scopus 로고
    • Structure and properties of a complex of α-synuclein and a single-domain camelid antibody
    • E. De Genst, T. Guilliams, J. Wellens, E. O'day, C. Waudby, and S. Meehan Structure and properties of a complex of α-synuclein and a single-domain camelid antibody J. Mol. Biol. 402 2010 326 343
    • (2010) J. Mol. Biol. , vol.402 , pp. 326-343
    • De Genst, E.1    Guilliams, T.2    Wellens, J.3    O'Day, E.4    Waudby, C.5    Meehan, S.6
  • 41
    • 54349118166 scopus 로고    scopus 로고
    • Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils
    • P.H. Chan, E. Pardon, L. Menzer, E. De Genst, J.R. Kumita, and J. Christodoulou Engineering a camelid antibody fragment that binds to the active site of human lysozyme and inhibits its conversion into amyloid fibrils Biochemistry 47 2008 11041 11054
    • (2008) Biochemistry , vol.47 , pp. 11041-11054
    • Chan, P.H.1    Pardon, E.2    Menzer, L.3    De Genst, E.4    Kumita, J.R.5    Christodoulou, J.6
  • 44
  • 50
    • 0035815115 scopus 로고    scopus 로고
    • Conformational properties of α-synuclein in its free and lipid-associated states
    • D. Eliezer, E. Kutluay, R. Bussell Jr., and G. Browne Conformational properties of α-synuclein in its free and lipid-associated states J. Mol. Biol. 307 2001 1061 1073
    • (2001) J. Mol. Biol. , vol.307 , pp. 1061-1073
    • Eliezer, D.1    Kutluay, E.2    Bussell, Jr.R.3    Browne, G.4
  • 55
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • M. Bouchard, J. Zurdo, E.J. Nettleton, C.M. Dobson, and C.V. Robinson Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy Protein Sci. 9 2000 1960 1967
    • (2000) Protein Sci. , vol.9 , pp. 1960-1967
    • Bouchard, M.1    Zurdo, J.2    Nettleton, E.J.3    Dobson, C.M.4    Robinson, C.V.5
  • 57
    • 0033561250 scopus 로고    scopus 로고
    • A single-domain antibody fragment in complex with RNase A: Non-canonical loop structures and nanomolar affinity using two CDR loops
    • K. Decanniere, A. Desmyter, M. Lauwereys, M.A. Ghahroudi, S. Muyldermans, and L. Wyns A single-domain antibody fragment in complex with RNase A: non-canonical loop structures and nanomolar affinity using two CDR loops Structure 7 1999 361 370
    • (1999) Structure , vol.7 , pp. 361-370
    • Decanniere, K.1    Desmyter, A.2    Lauwereys, M.3    Ghahroudi, M.A.4    Muyldermans, S.5    Wyns, L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.