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Supramolecular Structural Constraints on Alzheimer's β-Amyloid Fibrils from Electron Microscopy and Solid-State Nuclear Magnetic Resonance†
Biochemistry
◽
10.1021/bi0204185
◽
2002
◽
Vol 41
(51)
◽
pp. 15436-15450
◽
Cited By ~ 191
Author(s):
Oleg N. Antzutkin
◽
Richard D. Leapman
◽
John J. Balbach
◽
Robert Tycko
Keyword(s):
Electron Microscopy
◽
Nuclear Magnetic Resonance
◽
Solid State
◽
Magnetic Resonance
◽
Amyloid Fibrils
◽
Structural Constraints
◽
Β Amyloid
◽
Nuclear Magnetic
Download Full-text
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Supramolecular Structure in Full-Length Alzheimer's β-Amyloid Fibrils: Evidence for a Parallel β-Sheet Organization from Solid-State Nuclear Magnetic Resonance
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◽
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◽
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◽
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Models of Wild-Type and Disease-Causing Mutant β-Amyloid Fibrils: Insights from Solid-State Nuclear Magnetic Resonance Spectroscopy
Molecular Medicine and Medicinal Chemistry - Alzheimer's Disease: Insights into Low Molecular Weight and Cytotoxic Aggregates fromIn Vitroand Computer Experiments
◽
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◽
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◽
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Structural and dynamical characterization of tubular HIV-1 capsid protein assemblies by solid state nuclear magnetic resonance and electron microscopy
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◽
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◽
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◽
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◽
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◽
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Hydration and Dynamics of Full-Length Tau Amyloid Fibrils Investigated by Solid-State Nuclear Magnetic Resonance
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◽
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◽
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