Crossref
journal-article
Elsevier BV
Journal of Molecular Biology (78)
References
45
Referenced
92
10.1146/annurev.bi.61.070192.004503
/ Annu. Rev. Biochem. / Amyloidosis by Sipe (1992)10.1016/S0959-440X(99)00049-4
/ Curr. Opin. Struct. Biol. / Amyloid fibrillogenesis: themes and variations by Rochet (2000)10.1038/nature02261
/ Nature / Protein folding and misfolding by Dobson (2003)10.1038/nature02265
/ Nature / Therapeutic approaches to protein-misfolding diseases by Cohen (2003)10.1038/nsb792
/ Nature Struct. Biol. / Mapping the core of the β2-microglobulin amyloid fibrils by H/D exchange by Hoshino (2002)10.1021/bi048292u
/ Biochemistry / H/D exchange mapping of Ab1-40 amyloid fibril structure using NMR spectroscopy by Whittemore (2005)10.1006/jmbi.2000.3908
/ J. Mol. Biol. / The protofilament substructure of amyloid fibrils by Serpell (2000)10.1073/pnas.142459399
/ Proc. Natl Acad. Sci. USA / The protofilament structure of insulin amyloid fibrils by Jimenez (2002)10.1021/bi027378p
/ Biochemistry / Insight into the amyloid folding problem from solid-state NMR by Tycko (2003)10.1073/pnas.0406847102
/ Proc. Natl Acad. Sci. USA / Molecular basis for amyloid fibril formation and stability by Markin (2005)10.1016/S0092-8674(00)81163-0
/ Cell / Prion protein biology by Prusiner (1998)10.1146/annurev.neuro.24.1.519
/ Annu. Rev. Neurosci. / Prion diseases of humans and animals: their causes and molecular basis by Collinge (2001)10.1146/annurev.biochem.72.121801.161837
/ Annu. Rev. Biochem. / Emerging principles of conformation-based prion inheritance by Chien (2004)10.1038/nature02392
/ Nature / Conformational variations in an infectious protein determine prion strain differences by Tanaka (2004)10.1126/science.1100195
/ Science / Synthetic mammalian prions by Legname (2004)10.1126/science.1105850
/ Science / Self-propagating, molecular-level polymorphism in Alzheimer's β-amyloid fibrils by Petkova (2005)10.1110/ps.03607204
/ Protein Sci. / Insulin forms amyloid in a strain-dependent manner: an FT-IR spectroscopic study by Dzwolak (2004)10.1016/j.cell.2005.01.034
/ Cell / Fibril Conformation as the basis of species-and strain-dependent seeding specificity of mammalian prion amyloids by Jones (2005)10.1016/j.cell.2005.03.008
/ Cell / Mechanism of cross-species prion transmission: an infectious conformation compatible with two highly divergent yeast prion proteins by Tanaka (2005)10.1038/329506a0
/ Nature / Structure of the human class I histocompatibility antigen, HLA-A2 by Bjorkman (1987)10.1016/0006-291X(85)91948-5
/ Biochem. Biophys. Res. Commun. / A new form of amyloid protein associated with chronic hemodialysis was identified as β2-microglobulin by Gejyo (1985)10.3109/13506129709003833
/ Amyloid / Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro by Naiki (1997)10.1006/jmbi.2001.5071
/ J. Mol. Biol. / β2-Microglobulin and its deamidated variant, N17D form amyloid fibrils with a range of morphologies in vitro by Kad (2001)10.1016/S0022-2836(03)00583-7
/ J. Mol. Biol. / Hierarchical assembly of β2-microglobulin amyloid in vitro revealed by atomic force microscopy by Kad (2003)10.1073/pnas.0403756101
/ Proc. Natl Acad. Sci. USA / An amyloid-forming segment of β2-microglobulin suggests a molecular model for the fibril by Ivanova (2004)10.1110/ps.9.5.831
/ Protein Sci. / Removal of the N-terminal hexapeptide from human β2-microglobulin facilitates protein aggregation and fibril formation by Esposito (2000)10.1006/jmbi.2001.4661
/ J. Mol. Biol. / Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation by Morgan (2001)10.1074/jbc.M310779200
/ J. Biol. Chem. / Properties of some variants of human β2-microglobulin and amyloidogenesis by Corazza (2004)10.1074/jbc.M411949200
/ J. Biol. Chem. / Seeding-dependent maturation of β2-microglobulin amyloid fibrils at neutral pH by Kihara (2005)10.1006/jmbi.2000.3600
/ J. Mol. Biol. / Chemical dissection and reassembly of amyloid fibrils formed by a peptide fragment of trysthyretin by MacPhee (2000)10.1021/bi0011330
/ Biochemistry / Amyloid fibril formation by Aβ 16-22, a seven-residue fragment of the Alzheimer's β-amyloid peptide, a structural characterization by solid state NMR by Balbach (2000)10.1074/jbc.M108753200
/ J. Biol. Chem. / Investigation of a peptide responsible for amyloid fibril formation of β2-microglobulin by Acromobacter protease I by Kozhukh (2001)10.1074/jbc.M310334200
/ J. Biol. Chem. / Optimum amyloid fibril formation of a peptide fragment suggests the amyloidogenic preference of β2-microglobulin under physiological conditions by Ohhashi (2004)10.1021/bi0485880
/ Biochemistry / Stereospecific amyloid-like fibril formation by a peptide fragment of β2-microglobulin by Wadai (2005)10.1016/j.jsb.2004.11.008
/ J. Struct. Biol. / Association of thin filaments into thick filaments revealing the structural hierarchy of amyloid fibrils by Kanno (2005)10.1093/emboj/19.7.1441
/ EMBO J. / Mutational analysis of the propencity for amyloid formation by a globular protein by Chiti (2000)10.1110/ps.ps.10201
/ Protein Sci. / Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from HypF N-terminal domain by Chiti (2001)10.1002/bip.10179
/ Biopolymers / Structural transformation and aggregation of human alpha-synuclein in trifluoroethanol by Li (2002)10.1063/1.461939
/ J. Chem. Phys. / Model calculations on the amide-I infrared bands of globular proteins by Torii (1992)10.1002/bip.360370404
/ Biopolymers / The conformational analysis of peptides using fourier transform IR spectroscopy by Haris (1995)10.1002/bip.1975.360140402
/ Biopolymers / Estimation of amino acid residue side-chain absorption in the infrared spectra of protein solutions in heavy water by Chirgadze (1975)10.1021/bi00768a022
/ Biochemistry / Interactions contributing to the tyrosyl circular dichroism bands of ribonuclease-S and -A by Strickland (1972)10.1016/S0021-9258(18)64546-6
/ J. Biol. Chem. / Interpretation of the ultraviolet spectral changes of proteins by Yanari (1960)10.1006/jmbi.1997.1468
/ J. Mol. Biol. / Group additive contributions to the alcohol-induced α-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins by Nakaoka (1998)10.1107/S0021889891004399
/ J. Appl. Crystallog. / MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures by Kraulis (1991)
@article{Yamaguchi_2005, title={Seeding-dependent Propagation and Maturation of Amyloid Fibril Conformation}, volume={352}, ISSN={0022-2836}, url={http://dx.doi.org/10.1016/j.jmb.2005.07.061}, DOI={10.1016/j.jmb.2005.07.061}, number={4}, journal={Journal of Molecular Biology}, publisher={Elsevier BV}, author={Yamaguchi, Kei-ichi and Takahashi, Satoshi and Kawai, Tomoji and Naiki, Hironobu and Goto, Yuji}, year={2005}, month=sep, pages={952–960} }