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Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy
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The authors provide a detailed view of the immunoglobulin light-chain fibrillization pathway. Several oligomeric species were identified by atomic force microscopy, including filaments (height = 2.4 nm), protofibrils (height = 4.0 nm), type I fibrils (height = 8.3 nm) and type II fibrils (height = 5.9 nm). The results suggest a model in which protofibrils, type I fibrils and type II fibrils are formed by the winding of two filaments, two protofibrils and three filaments, respectively
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Ionescu-Zanetti C., Khurana R., Gillespie J.R., Petrick J.S., Trabachino L.C., Minert L.J., Carter S.A., Fink A.L. Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy. Proc Natl Acad Sci USA. 96:1999;13175-13179. The authors provide a detailed view of the immunoglobulin light-chain fibrillization pathway. Several oligomeric species were identified by atomic force microscopy, including filaments (height = 2.4 nm), protofibrils (height = 4.0 nm), type I fibrils (height = 8.3 nm) and type II fibrils (height = 5.9 nm). The results suggest a model in which protofibrils, type I fibrils and type II fibrils are formed by the winding of two filaments, two protofibrils and three filaments, respectively.
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(1999)
Proc Natl Acad Sci USA
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Ionescu-Zanetti, C.1
Khurana, R.2
Gillespie, J.R.3
Petrick, J.S.4
Trabachino, L.C.5
Minert, L.J.6
Carter, S.A.7
Fink, A.L.8
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75
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0033352083
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Furin mediates enhanced production of fibrillogenic ABri peptides in familial British dementia
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Kim S-H., Wang R., Gordon D.J., Bass J., Steiner D.F., Lynn D.G., Thinakaran G., Meredith S.C., Sisodia S.S. Furin mediates enhanced production of fibrillogenic ABri peptides in familial British dementia. Nat Neurosci. 2:1999;984-988.
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(1999)
Nat Neurosci
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Kim, S.-H.1
Wang, R.2
Gordon, D.J.3
Bass, J.4
Steiner, D.F.5
Lynn, D.G.6
Thinakaran, G.7
Meredith, S.C.8
Sisodia, S.S.9
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76
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0032755251
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Manipulating the amyloid-β aggregation pathway with chemical chaperones
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Yang D-S., Yip C.M., Huang T.H.J., Chakrabartty A., Fraser P.E. Manipulating the amyloid-β aggregation pathway with chemical chaperones. J Biol Chem. 274:1999;32970-32974.
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J Biol Chem
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Yang, D.-S.1
Yip, C.M.2
Huang, T.H.J.3
Chakrabartty, A.4
Fraser, P.E.5
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77
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0034681163
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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
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The authors show, for the first time, that a mutant of α-synuclein (A30P) linked to early-onset Parkinson's disease fibrillizes less rapidly, but forms nonfibrillar oligomers more rapidly, than the wild-type protein. Several nonfibrillar assemblies, including 'spheres', 'chains' and 'rings', were isolated by gel filtration and characterized by atomic force microscopy. The results are of considerable importance, as they suggest that drugs designed to inhibit the fibrillization of α-synuclein may in fact promote the accumulation of toxic oligomeric species
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Conway K.A., Lee S-J., Rochet J-C., Ding T.T., Williamson R.E., Lansbury P.T. Jr. 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. The authors show, for the first time, that a mutant of α-synuclein (A30P) linked to early-onset Parkinson's disease fibrillizes less rapidly, but forms nonfibrillar oligomers more rapidly, than the wild-type protein. Several nonfibrillar assemblies, including 'spheres', 'chains' and 'rings', were isolated by gel filtration and characterized by atomic force microscopy. The results are of considerable importance, as they suggest that drugs designed to inhibit the fibrillization of α-synuclein may in fact promote the accumulation of toxic oligomeric species.
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(2000)
Proc Natl Acad Sci USA
, vol.97
, pp. 571-576
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Conway, K.A.1
Lee, S.-J.2
Rochet, J.-C.3
Ding, T.T.4
Williamson, R.E.5
Lansbury P.T., Jr.6
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