Early events in amyloid-β self-assembly probed by time-resolved solid state NMR and light scattering
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R. Tycko | W. Yau | Jaekyun Jeon | J. Jeon | Wai‐Ming Yau
[1] R. Tycko,et al. Nitroxide-based triradical dopants for efficient low-temperature dynamic nuclear polarization in aqueous solutions over a broad pH range. , 2022, Journal of magnetic resonance.
[2] R. Tycko,et al. Millisecond Time-Resolved Solid-State NMR Initiated by Rapid Inverse Temperature Jumps. , 2022, Journal of the American Chemical Society.
[3] A. Murzin,et al. Cryo-EM structures of amyloid-β 42 filaments from human brains , 2022, Science.
[4] J. Collinge,et al. Structural differences in amyloid-β fibrils from brains of nondemented elderly individuals and Alzheimer's disease patients , 2021, Proceedings of the National Academy of Sciences.
[5] T. Mittag,et al. A multi-step nucleation process determines the kinetics of prion-like domain phase separation , 2021, Nature Communications.
[6] B. Strodel,et al. Amyloid-β peptide dimers undergo a random coil to β-sheet transition in the aqueous phase but not at the neuronal membrane , 2021, Proceedings of the National Academy of Sciences.
[7] R. Tycko,et al. Molecular structure of a prevalent amyloid-β fibril polymorph from Alzheimer's disease brain tissue , 2020, Proceedings of the National Academy of Sciences.
[8] R. Tycko,et al. Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase. , 2020, Journal of the American Chemical Society.
[9] Alexander J. Bryer,et al. Atomic-resolution structure of HIV-1 capsid tubes by magic-angle spinning NMR , 2020, Nature Structural & Molecular Biology.
[10] C. Dobson,et al. Kinetic diversity of amyloid oligomers , 2020, Proceedings of the National Academy of Sciences.
[11] A. Šarić,et al. Dynamics of oligomer populations formed during the aggregation of Alzheimer’s Aβ42 peptide , 2020, bioRxiv.
[12] Y. Ishii,et al. NMR-based site-resolved profiling of β-amyloid misfolding reveals structural transitions from pathologically relevant spherical oligomer to fibril , 2019, The Journal of Biological Chemistry.
[13] C. Sigurdson,et al. Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue , 2019, Nature Communications.
[14] A. Bax,et al. Observation of β-Amyloid Peptide Oligomerization by Pressure-Jump NMR Spectroscopy. , 2019, Journal of the American Chemical Society.
[15] R. Ghirlando,et al. Application of millisecond time-resolved solid state NMR to the kinetics and mechanism of melittin self-assembly , 2019, Proceedings of the National Academy of Sciences.
[16] G. Ullah,et al. Origin of metastable oligomers and their effects on amyloid fibril self-assembly† †Electronic supplementary information (ESI) available. See DOI: 10.1039/c8sc01479e , 2018, Chemical science.
[17] R. Best,et al. Highly Disordered Amyloid-β Monomer Probed by Single-Molecule FRET and MD Simulation. , 2018, Biophysical journal.
[18] G. Ullah,et al. Origin of metastable oligomers and their e ff ects on amyloid fi bril self-assembly † , 2018 .
[19] G. Schröder,et al. Fibril structure of amyloid-β(1–42) by cryo–electron microscopy , 2017, Science.
[20] Galia T Debelouchina,et al. A molecular engineering toolbox for the structural biologist , 2017, Quarterly Reviews of Biophysics.
[21] D. Otzen,et al. ThT 101: a primer on the use of thioflavin T to investigate amyloid formation , 2017, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.
[22] Peter Güntert,et al. Atomic-resolution structure of a disease-relevant Aβ(1–42) amyloid fibril , 2016, Proceedings of the National Academy of Sciences.
[23] Sara Linse,et al. Atomic Resolution Structure of Monomorphic Aβ42 Amyloid Fibrils. , 2016, Journal of the American Chemical Society.
[24] R. Tycko,et al. Low-temperature dynamic nuclear polarization with helium-cooled samples and nitrogen-driven magic-angle spinning. , 2016, Journal of magnetic resonance.
[25] A. Bax,et al. Monomeric Aβ1–40 and Aβ1–42 Peptides in Solution Adopt Very Similar Ramachandran Map Distributions That Closely Resemble Random Coil , 2016, Biochemistry.
[26] R. Ghirlando,et al. Successive Stages of Amyloid-β Self-Assembly Characterized by Solid-State Nuclear Magnetic Resonance with Dynamic Nuclear Polarization. , 2015, Journal of the American Chemical Society.
[27] Y. Ishii,et al. Structural Insight into an Alzheimer’s Brain-Derived Spherical Assembly of Amyloid β by Solid-State NMR , 2015, Journal of the American Chemical Society.
[28] C. Dobson,et al. Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation , 2015, Proceedings of the National Academy of Sciences.
[29] Ruth Nussinov,et al. Aβ(1–42) Fibril Structure Illuminates Self-recognition and Replication of Amyloid in Alzheimer’s , 2015, Nature Structural &Molecular Biology.
[30] R. Glockshuber,et al. Atomic-Resolution Three-Dimensional Structure of Amyloid β Fibrils Bearing the Osaka Mutation , 2014, Angewandte Chemie.
[31] O. Antzutkin,et al. A hexameric peptide barrel as building block of amyloid-β protofibrils. , 2014, Angewandte Chemie.
[32] H. Mootz,et al. Click-tag and amine-tag: chemical tag approaches for efficient protein labeling in vitro and on live cells using the naturally split Npu DnaE intein. , 2014, Angewandte Chemie.
[33] Charles D. Schwieters,et al. Molecular Structure of β-Amyloid Fibrils in Alzheimer’s Disease Brain Tissue , 2013, Cell.
[34] T. Rosenberry,et al. The Alzheimer's amyloid-β(1-42) peptide forms off-pathway oligomers and fibrils that are distinguished structurally by intermolecular organization. , 2013, Journal of molecular biology.
[35] Michele Vendruscolo,et al. Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism , 2013, Proceedings of the National Academy of Sciences.
[36] R. Tycko,et al. Polymorph-specific kinetics and thermodynamics of β-amyloid fibril growth. , 2013, Journal of the American Chemical Society.
[37] C. Jaroniec,et al. Nmrglue: an open source Python package for the analysis of multidimensional NMR data , 2013, Journal of biomolecular NMR.
[38] U. Fink,et al. Structural properties of EGCG-induced, nontoxic Alzheimer's disease Aβ oligomers. , 2012, Journal of molecular biology.
[39] H. Scheidt,et al. Solid-state NMR Reveals a Close Structural Relationship between Amyloid-β Protofibrils and Oligomers* , 2012, The Journal of Biological Chemistry.
[40] Mark P Mattson,et al. Antiparallel β-sheet architecture in Iowa-mutant β-amyloid fibrils , 2012, Proceedings of the National Academy of Sciences.
[41] I. Bertini,et al. A new structural model of Aβ40 fibrils. , 2011, Journal of the American Chemical Society.
[42] Judianne Davis,et al. Structural conversion of neurotoxic amyloid-β(1–42) oligomers to fibrils , 2010, Nature Structural &Molecular Biology.
[43] R. Tycko,et al. Measurement of sample temperatures under magic-angle spinning from the chemical shift and spin-lattice relaxation rate of 79Br in KBr powder. , 2009, Journal of magnetic resonance.
[44] Richard D. Leapman,et al. Molecular structural basis for polymorphism in Alzheimer's β-amyloid fibrils , 2008, Proceedings of the National Academy of Sciences.
[45] Robert G Griffin,et al. Dynamic nuclear polarization at high magnetic fields. , 2008, The Journal of chemical physics.
[46] Y. Ishii,et al. Evidence of fibril-like β-sheet structures in a neurotoxic amyloid intermediate of Alzheimer's β-amyloid , 2007, Nature Structural &Molecular Biology.
[47] A. Naito,et al. Solid-state NMR studies of two backbone conformations at Tyr185 as a function of retinal configurations in the dark, light, and pressure adapted bacteriorhodopsins. , 2007, Journal of the American Chemical Society.
[48] S. Müller,et al. Multiple Assembly Pathways Underlie Amyloid-β Fibril Polymorphisms , 2005 .
[49] David T. Kaleta,et al. Structural properties of Abeta protofibrils stabilized by a small molecule. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[50] Aleksey LOMAKINtt,et al. On the nucleation and growth of amyloid ,8-protein fibrils: Detection of nuclei and quantitation of rate constants , 2005 .
[51] M. Kirkitadze,et al. Amyloid β-protein (Aβ) assembly: Aβ40 and Aβ42 oligomerize through distinct pathways , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[52] R. Leapman,et al. Supramolecular structural constraints on Alzheimer's beta-amyloid fibrils from electron microscopy and solid-state nuclear magnetic resonance. , 2002, Biochemistry.
[53] D. Weliky,et al. Application of REDOR subtraction for filtered MAS observation of labeled backbone carbons of membrane-bound fusion peptides. , 2002, Journal of magnetic resonance.
[54] Ralf Langen,et al. Structural and Dynamic Features of Alzheimer's Aβ Peptide in Amyloid Fibrils Studied by Site-directed Spin Labeling* , 2002, The Journal of Biological Chemistry.
[55] R. Riek,et al. NMR studies in aqueous solution fail to identify significant conformational differences between the monomeric forms of two Alzheimer peptides with widely different plaque-competence, A beta(1-40)(ox) and A beta(1-42)(ox). , 2001, European Journal of Biochemistry.
[56] R. Murphy,et al. A mathematical model of the kinetics of beta-amyloid fibril growth from the denatured state. , 2001, Biophysical journal.
[57] R. Leapman,et al. Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of β-sheets in Alzheimer's β-amyloid fibrils , 2000 .
[58] Regina M. Murphy,et al. Probing the Kinetics of β-Amyloid Self-Association , 2000 .
[59] S. Müller,et al. Studies on the in Vitro Assembly of Aβ 1–40: Implications for the Search for Aβ Fibril Formation Inhibitors , 2000 .
[60] C. Rienstra,et al. Fivefold symmetric homonuclear dipolar recoupling in rotating solids: Application to double quantum spectroscopy , 1999 .
[61] T. Benzinger,et al. Propagating structure of Alzheimer’s β-amyloid(10–35) is parallel β-sheet with residues in exact register , 1998 .
[62] George B. Benedek,et al. Kinetic theory of fibrillogenesis of amyloid β-protein , 1997 .
[63] Peter T. Lansbury,et al. Observation of metastable Aβ amyloid protofibrils by atomic force microscopy , 1997 .
[64] D. Kirschner,et al. On the nucleation and growth of amyloid beta-protein fibrils: detection of nuclei and quantitation of rate constants. , 1996, Proceedings of the National Academy of Sciences of the United States of America.
[65] S. Grzesiek,et al. NMRPipe: A multidimensional spectral processing system based on UNIX pipes , 1995, Journal of biomolecular NMR.
[66] Andrew E. Bennett,et al. Heteronuclear decoupling in rotating solids , 1995 .
[67] R. Hodges,et al. 1H, 13C and 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects , 1995, Journal of biomolecular NMR.
[68] K. Grzeschik,et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor , 1987, Nature.
[69] G. Glenner,et al. Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein. , 1984, Biochemical and biophysical research communications.
[70] D. Lilly,et al. Solutions to the equations for the kinetics of coagulation , 1965 .
[71] G. Oster. Light scattering from polymerizing and coagulating systems , 1947 .
[72] P. Debye,et al. Molecular-weight determination by light scattering. , 1947, The Journal of physical and colloid chemistry.
[73] S. Chandrasekhar. Stochastic problems in Physics and Astronomy , 1943 .