Crystallographic studies of prion protein (PrP) segments suggest how structural changes encoded by polymorphism at residue 129 modulate susceptibility to human prion disease, J. Biol. Chem, vol.285, pp.29671-29675, 2010. ,
Cross polarization in the tilted frame: assignment and spectral simplification in heteronuclear spin systems, Mol. Phys, vol.95, pp.1197-1207, 1998. ,
Specific in situ discrimination of amyloid fibrils versus, Mol. BioSystems, vol.8, pp.557-564, 2012. ,
Inhibition of amyloid aggregation by formation of helical assemblies, Chem. Eur. J, vol.17, pp.10651-10661, 2011. ,
Advanced solid-state NMR methods for the elucidation of structure and dynamics of molecular, macromolecular, and supramolecular systems, Chem. Rev, vol.101, pp.4125-4156, 2001. ,
Ultrastructural organization of amyloid fibrils by atomic force microscopy, Biophys. J, vol.79, pp.3282-3293, 2000. ,
Amyloids: not only pathological agents but also ordered nanomaterials, Angew. Chem. Int. Ed. Engl, vol.47, pp.4062-4069, 2008. ,
Atomic resolution structure of monomorphic A?42 amyloid fibrils, J. Am. Chem. Soc, vol.138, pp.9663-9674, 2016. ,
AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides, BMC Bioinformatics, vol.8, p.65, 2007. ,
The protein-folding problem, 50 years on, Science, vol.338, pp.1042-1046, 2012. ,
Getting out of shape, Nature, vol.418, pp.729-730, 2002. ,
Protein folding and misfolding, Nature, vol.426, pp.884-890, 2003. ,
The fundamentals of protein folding: bringing together theory and experiment, Curr. Opin. Struct. Biol, vol.9, pp.92-101, 1999. ,
X-ray diffraction studies on amyloid filaments, J. Histochem. Cytochem, vol.16, pp.673-677, 1968. ,
Structural studies of amyloid proteins at the molecular level, Annu. Rev. Biochem, vol.86, pp.69-95, 2017. ,
Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins, Nat. Biotechnol, vol.22, pp.1302-1306, 2004. ,
Atomic structure and hierarchical assembly of a cross-beta amyloid fibril, PNAS, vol.110, pp.5468-5473, 2013. ,
Cryo-EM structures of tau filaments from Alzheimer's disease, Nature, vol.547, pp.185-190, 2017. ,
pH-dependent structural transitions of Alzheimer amyloid peptides, Biophys. J, vol.60, pp.1190-1201, 1991. ,
Fibril formation by primate, rodent, and Dutch-hemorrhagic analogues of Alzheimer amyloid beta-protein, Biochemistry, vol.31, pp.10716-10723, 1992. ,
Cross-beta" conformation in proteins, J. Mol. Biol, vol.32, pp.343-358, 1968. ,
Structure analysis of an amyloid-forming model peptide by a systematic glycine and proline scan, Biomacromolecules, vol.12, pp.2988-2996, 2011. ,
Fluorinated amino acids in amyloid formation: a symphony of size, hydrophobicity and [small alpha]-helix propensity, Chem. Sci, vol.5, pp.819-830, 2014. ,
Fibril structure of amyloid-beta(1-42) by cryo-electron microscopy, Science, vol.358, pp.116-119, 2017. ,
, FIT2D V9.129 Reference Manual V3.1 ESRF Internal Report, 1998.
Transferred-echo double-resonance NMR, J. Magn. Reson, issue.96, pp.205-209, 1969. ,
NFGAIL amyloid oligomers: the onset of beta-sheet formation and the mechanism for fibril formation, J. Am. Chem. Soc, 2017. ,
Resonance assignment of 13C/15N labeled solid proteins by two-and three-dimensional magic-angle-spinning NMR, J. Biomol. NMR, vol.15, pp.1-14, 1999. ,
Determination of multiple ***&phi, 1999. ,
-torsion angles in proteins by selective and extensive (13)C labeling and two-dimensional solid-state NMR, J. Magn. Resonance, vol.139, pp.389-401, 1997. ,
Frequency selective heteronuclear dipolar recoupling in rotating solids: accurate 13C-15N distance measurements in uniformly 13C,15N-labeled peptides, J. Am. Chem. Soc, vol.123, pp.3507-3519, 2001. ,
X-ray diffraction from intraneuronal paired helical filaments and extraneuronal amyloid fibers in Alzheimer disease indicates cross-beta conformation, PNAS, vol.83, pp.503-507, 1986. ,
Synthetic peptide homologous to beta protein from Alzheimer disease forms amyloidlike fibrils in vitro, PNAS, vol.84, pp.6953-6957, 1987. ,
Protofilaments, filaments, ribbons, and fibrils from peptidomimetic self-assembly: implications for amyloid fibril formation and materials science, J. Am. Chem. Soc, vol.122, pp.5262-5277, 2000. ,
Structure analysis using acoustically levitated droplets, Anal. Bioanal. Chem, vol.391, pp.1221-1228, 2008. ,
A comparative study of the relationship between protein structure and ?-aggregation in globular and intrinsically disordered proteins, J. Mol. Biol, vol.342, pp.345-353, 2004. ,
3D structure of Alzheimer's amyloid-?(1-42) fibrils, PNAS, vol.102, pp.17342-17347, 2005. ,
Engineered and designed peptide-based fibrous biomaterials, Curr. Opin. Solid State Mater. Sci, vol.8, pp.141-149, 2004. ,
Structures for amyloid fibrils, FEBS J, vol.272, pp.5950-5961, 2005. ,
Molecular basis for amyloid fibril formation and stability, PNAS, vol.102, pp.315-320, 2005. ,
Analysis of the secondary structure of beta-amyloid (Abeta42) fibrils by systematic proline replacement, J. Biol. Chem, vol.279, pp.52781-52788, 2004. ,
Enhancement of nuclear magnetic-resonance signals by polarization transfer, J. Am. Chem. Soc, vol.101, pp.760-762, 1979. ,
From natural to designer self-assembling biopolymers, the structural characterisation of fibrous proteins & peptides using fibre diffraction, Chem. Soc. Rev, vol.39, pp.3445-3453, 2010. ,
Structure of the cross-? spine of amyloid-like fibrils, Nature, vol.435, pp.773-778, 2005. ,
How metal ions affect amyloid formation: Cu2+-and Zn2+-sensitive peptides, Chembiochem, vol.9, pp.531-536, 2008. ,
Following polypeptide folding and assembly with conformational switches, Curr. Opin. Chem. Biol, vol.12, pp.730-739, 2008. ,
From [small alpha]-helix to [small beta]-sheet -a reversible metal ion induced peptide secondary structure switch, Org. Biomol. Chem, vol.3, pp.2500-2502, 2005. ,
, , 2006.
, Journal of Structural Biology, vol.203, pp.263-272, 2018.
, Random coils, ?-sheet ribbons, and ?-helical fibers: one peptide adopting three different secondary structures at will, J. Am. Chem. Soc, vol.128, pp.2196-2197
Intramolecular charge interactions as a tool to control the coiled-coil-toamyloid transformation, Chem. Eur. J, vol.14, pp.11442-11451, 2008. ,
A new experimental station for simultaneous X-ray microbeam scanning for small-and wide-angle scattering and fluorescence at BESSY II, J. Appl. Crystallogr, vol.40, pp.466-470, 2007. ,
Backbone and side-chain 13C and 15N signal assignments of the alpha-spectrin SH3 domain by magic angle spinning solid-state NMR at 17.6 Tesla, pp.2272-2281, 2001. ,
A structural model for Alzheimer's ?-amyloid fibrils based on experimental constraints from solid state NMR, Proc. Natl. Acad. Sci, vol.99, pp.16742-16747, 2002. ,
Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide, J. Mol. Biol, vol.335, pp.247-260, 2004. ,
Nanoscale structure and spectroscopic probing of Abeta1-40 fibril bundle formation, p.44, 2016. ,
Structural variation in amyloid-beta fibrils from Alzheimer's disease clinical subtypes, Nature, vol.541, pp.217-221, 2017. ,
ARIA2: automated NOE assignment and data integration in NMR structure calculation, Bioinformatics, vol.23, pp.381-382, 2007. ,
Protein aggregation and amyloidosis: confusion of the kinds?, Curr. Opin. Struct. Biol, vol.16, pp.118-126, 2006. ,
Folding proteins in fatal ways, Nature, vol.426, pp.900-904, 2003. ,
An infrared spectroscopy approach to follow ?-sheet formation in peptide amyloid assemblies, Nat. Chem, vol.9, p.39, 2016. ,
TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts, J. Biomol. NMR, vol.44, pp.213-223, 2009. ,
X-ray scattering study of the effect of hydration on the cross-beta structure of amyloid fibrils, J. Am. Chem. Soc, vol.128, pp.11738-11739, 2006. ,
Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution, J. Mol. Med, vol.81, pp.678-699, 2003. ,
A software framework for analysing solid-state MAS NMR data, J. Biomol. NMR, vol.51, pp.437-447, 2011. ,
Experiments and strategies for the assignment of fully13C/15N-labelled polypeptides by solid state NMR, J. Biomol. NMR, vol.12, pp.39-50, 1998. ,
Developments in fiber diffraction, Curr. Opin. Struct. Biol, vol.9, pp.615-619, 1999. ,
Common core structure of amyloid fibrils by synchrotron X-ray diffraction, J. Mol. Biol, vol.273, pp.729-739, 1997. ,
Observation of spin exchange by two-dimensional fourier transform 13 C cross polarization-magic-angle spinning, J. Magn. Reson, vol.47, pp.462-475, 1982. ,
Solid-state NMR studies of amyloid fibril structure, Annu. Rev. Phys. Chem, vol.62, pp.279-299, 2011. ,
The CCPN data model for NMR spectroscopy: development of a software pipeline, Proteins Struct. Funct. Genet, vol.59, pp.687-696, 2005. ,
Atomic-resolution structure of a disease-relevant A?(1-42) amyloid fibril, Proc. Natl. Acad. Sci, vol.113, pp.4976-4984, 2016. ,
Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis, J. Mol. Biol, vol.335, pp.833-842, 2004. ,
Alanine scanning mutagenesis of Abeta (1-40) amyloid fibril stability, J. Mol. Biol, vol.357, pp.1283-1294, 2006. ,
Template-based and free modeling of I-TASSER and QUARK pipelines using predicted contact maps in CASP12, Proteins: Struct. Funct. Bioinf, pp.1-16, 2017. ,
, Journal of Structural Biology, vol.203, pp.263-272, 2018.