Protein misfolding, functional amyloid, and human disease.
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[1] M. Amaral,et al. CFTR and chaperones , 2007, Journal of Molecular Neuroscience.
[2] C. Dobson,et al. Probing the mechanism of amyloidogenesis through a tandem repeat of the PI3-SH3 domain suggests a generic model for protein aggregation and fibril formation. , 2006, Journal of molecular biology.
[3] Jesper Søndergaard Pedersen,et al. The changing face of glucagon fibrillation: structural polymorphism and conformational imprinting. , 2006, Journal of molecular biology.
[4] Richard M. Page,et al. Intraneuronal Aβ, non-amyloid aggregates and neurodegeneration in a Drosophila model of Alzheimer’s disease , 2005, Neuroscience.
[5] S. Teichmann,et al. The importance of sequence diversity in the aggregation and evolution of proteins , 2005, Nature.
[6] S. Becker,et al. Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[7] Virgil L. Woods,et al. Structure and properties of α-synuclein and other amyloids determined at the amino acid level , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[8] Sarah A. Petty,et al. Intersheet rearrangement of polypeptides during nucleation of β-sheet aggregates , 2005 .
[9] G. J. Raymond,et al. The most infectious prion protein particles , 2005, Nature.
[10] C. Dobson,et al. Evidence for a mechanism of amyloid formation involving molecular reorganisation within native-like precursor aggregates. , 2005, Journal of molecular biology.
[11] S. Radford,et al. Competing pathways determine fibril morphology in the self-assembly of beta2-microglobulin into amyloid. , 2005, Journal of molecular biology.
[12] C. Dobson,et al. Glycine residues appear to be evolutionarily conserved for their ability to inhibit aggregation. , 2005, Structure.
[13] R. Wickner,et al. Yeast prions [URE3] and [PSI+] are diseases. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[14] Michele Vendruscolo,et al. Prediction of "aggregation-prone" and "aggregation-susceptible" regions in proteins associated with neurodegenerative diseases. , 2005, Journal of molecular biology.
[15] Naomi E Chayen,et al. Methods for separating nucleation and growth in protein crystallisation. , 2005, Progress in Biophysics and Molecular Biology.
[16] Thorsten Lührs,et al. Correlation of structural elements and infectivity of the HET-s prion , 2005, Nature.
[17] Robert A. Grothe,et al. Structure of the cross-β spine of amyloid-like fibrils , 2005, Nature.
[18] S. Lindquist,et al. Structural insights into a yeast prion illuminate nucleation and strain diversity , 2005, Nature.
[19] 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.
[20] Shinya Honda,et al. Higher-order molecular packing in amyloid-like fibrils constructed with linear arrangements of hydrophobic and hydrogen-bonding side-chains. , 2005, Journal of molecular biology.
[21] Dennis C Winkler,et al. Filaments of the Ure2p prion protein have a cross-β core structure , 2005 .
[22] Ueli Aebi,et al. The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin. , 2005, Journal of molecular biology.
[23] P. Westermark,et al. Protein fibrils in nature can enhance amyloid protein A amyloidosis in mice: Cross-seeding as a disease mechanism , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[24] E. M. Jones,et al. Fibril Conformation as the Basis of Species- and Strain-Dependent Seeding Specificity of Mammalian Prion Amyloids , 2005, Cell.
[25] J. Weissman,et al. Mechanism of Cross-Species Prion Transmission An Infectious Conformation Compatible withTwo Highly Divergent Yeast Prion Proteins , 2005, Cell.
[26] C. Pál,et al. Molecular chaperones as regulatory elements of cellular networks. , 2005, Current opinion in cell biology.
[27] C. Dobson,et al. Amyloid formation from HypF-N under conditions in which the protein is initially in its native state. , 2005, Journal of molecular biology.
[28] Fabrizio Chiti,et al. Investigating the Effects of Mutations on Protein Aggregation in the Cell* , 2005, Journal of Biological Chemistry.
[29] Peter T Lansbury,et al. Small-molecule-mediated stabilization of familial amyotrophic lateral sclerosis-linked superoxide dismutase mutants against unfolding and aggregation. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[30] Giampaolo Merlini,et al. Amyloid: Toward terminology clarification Report from the Nomenclature Committee of the International Society of Amyloidosis , 2005, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.
[31] Thorsteinn Adalsteinsson,et al. Correlations among morphology, beta-sheet stability, and molecular structure in prion peptide aggregates. , 2005, Biochemistry.
[32] A. Darinskas,et al. Does the Cytotoxic Effect of Transient Amyloid Oligomers from Common Equine Lysozyme in Vitro Imply Innate Amyloid Toxicity?* , 2005, Journal of Biological Chemistry.
[33] C. Griesinger,et al. Release of long-range tertiary interactions potentiates aggregation of natively unstructured alpha-synuclein. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[34] C. Dobson,et al. Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations. , 2005, Journal of the American Chemical Society.
[35] Richard D. Leapman,et al. Self-Propagating, Molecular-Level Polymorphism in Alzheimer's ß-Amyloid Fibrils , 2005, Science.
[36] M. DePristo,et al. Simultaneous determination of protein structure and dynamics , 2005, Nature.
[37] Pawel Sikorski,et al. Molecular basis for amyloid fibril formation and stability. , 2005, Proceedings of the National Academy of Sciences of the United States of America.
[38] A. Alexandrescu. Amyloid accomplices and enforcers , 2005, Protein science : a publication of the Protein Society.
[39] M. Fändrich,et al. FTIR reveals structural differences between native β‐sheet proteins and amyloid fibrils , 2004, Protein science : a publication of the Protein Society.
[40] V. Subramaniam,et al. Impact of the acidic C-terminal region comprising amino acids 109-140 on alpha-synuclein aggregation in vitro. , 2004, Biochemistry.
[41] C. Hall,et al. Molecular dynamics simulations of spontaneous fibril formation by random-coil peptides. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[42] Lisa D. Cabrita,et al. Polyglutamine Expansion in Ataxin-3 Does Not Affect Protein Stability , 2004, Journal of Biological Chemistry.
[43] Ralf Langen,et al. Identifying Structural Features of Fibrillar Islet Amyloid Polypeptide Using Site-directed Spin Labeling* , 2004, Journal of Biological Chemistry.
[44] R. Kayed,et al. Permeabilization of Lipid Bilayers Is a Common Conformation-dependent Activity of Soluble Amyloid Oligomers in Protein Misfolding Diseases* , 2004, Journal of Biological Chemistry.
[45] A. Miller,et al. The formation of spherulites by amyloid fibrils of bovine insulin. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[46] L. Serrano,et al. Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins , 2004, Nature Biotechnology.
[47] Heather L. True,et al. Epigenetic regulation of translation reveals hidden genetic variation to produce complex traits , 2004, Nature.
[48] M. R. Nilsson. Techniques to study amyloid fibril formation in vitro. , 2004, Methods.
[49] Michele Vendruscolo,et al. Prediction of the absolute aggregation rates of amyloidogenic polypeptide chains. , 2004, Journal of molecular biology.
[50] Jesper Søndergaard Pedersen,et al. Modulation of S6 fibrillation by unfolding rates and gatekeeper residues. , 2004, Journal of molecular biology.
[51] F. Cohen,et al. Synthetic Mammalian Prions , 2004, Science.
[52] Ralf Langen,et al. Template-assisted filament growth by parallel stacking of tau. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[53] M. P. Kirpichnikov,et al. Fibrillation of carrier protein albebetin and its biologically active constructs. Multiple oligomeric intermediates and pathways. , 2004, Biochemistry.
[54] C. Dobson,et al. Observation of sequence specificity in the seeding of protein amyloid fibrils , 2004, Protein science : a publication of the Protein Society.
[55] A. Cavalli,et al. The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates , 2004, Protein science : a publication of the Protein Society.
[56] Peter Chien,et al. Emerging principles of conformation-based prion inheritance. , 2004, Annual review of biochemistry.
[57] Andrey V Kajava,et al. A model for Ure2p prion filaments and other amyloids: the parallel superpleated beta-structure. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[58] V. Subramaniam,et al. NMR of α‐synuclein–polyamine complexes elucidates the mechanism and kinetics of induced aggregation , 2004, The EMBO journal.
[59] V. Uversky,et al. Conformational constraints for amyloid fibrillation: the importance of being unfolded. , 2004, Biochimica et biophysica acta.
[60] P. Decottignies,et al. Structural characterization of the fibrillar form of the yeast Saccharomyces cerevisiae prion Ure2p. , 2004, Biochemistry.
[61] M. Hoshino,et al. Core and heterogeneity of beta2-microglobulin amyloid fibrils as revealed by H/D exchange. , 2004, Journal of molecular biology.
[62] Ann-Shyn Chiang,et al. Dissecting the pathological effects of human Aβ40 and Aβ42 in Drosophila: A potential model for Alzheimer's disease , 2004 .
[63] R. Lerner,et al. Metabolite-initiated protein misfolding may trigger Alzheimer's disease. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[64] F. Chiti,et al. Aggregation of the Acylphosphatase from Sulfolobus solfataricus , 2004, Journal of Biological Chemistry.
[65] M. Papa,et al. Fibrillogenesis and Cytotoxic Activity of the Amyloid-forming Apomyoglobin Mutant W7FW14F* , 2004, Journal of Biological Chemistry.
[66] J. Kelly,et al. Tissue damage in the amyloidoses: Transthyretin monomers and nonnative oligomers are the major cytotoxic species in tissue culture. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[67] Fabrizio Chiti,et al. The regions of the sequence most exposed to the solvent within the amyloidogenic state of a protein initiate the aggregation process. , 2004, Journal of molecular biology.
[68] G. Merlini,et al. The systemic amyloidoses: clearer understanding of the molecular mechanisms offers hope for more effective therapies , 2004, Journal of internal medicine.
[69] L. Serpell,et al. Structural characterisation of islet amyloid polypeptide fibrils. , 2004, Journal of molecular biology.
[70] C. Dobson,et al. High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[71] Ying Xu,et al. Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis. , 2004, Journal of molecular biology.
[72] Zoya Ignatova,et al. Monitoring protein stability and aggregation in vivo by real-time fluorescent labeling. , 2004, Proceedings of the National Academy of Sciences of the United States of America.
[73] E. Kandel,et al. A Neuronal Isoform of the Aplysia CPEB Has Prion-Like Properties , 2003, Cell.
[74] Fred E. Cohen,et al. Therapeutic approaches to protein-misfolding diseases , 2003, Nature.
[75] Bart Kahr,et al. Imaging linear birefringence and dichroism in cerebral amyloid pathologies , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[76] Christopher M Dobson,et al. Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments , 2003, Proceedings of the National Academy of Sciences of the United States of America.
[77] P. Hawkins,et al. Amyloidosis: new strategies for treatment. , 2003, The international journal of biochemistry & cell biology.
[78] U. Baxa,et al. Architecture of Ure2p Prion Filaments , 2003, Journal of Biological Chemistry.
[79] J. M. Scholtz,et al. The role of protein stability, solubility, and net charge in amyloid fibril formation , 2003, Protein science : a publication of the Protein Society.
[80] Ralf Langen,et al. Structural Organization of α-Synuclein Fibrils Studied by Site-directed Spin Labeling* , 2003, Journal of Biological Chemistry.
[81] C. Dobson,et al. Protein aggregation and aggregate toxicity: new insights into protein folding, misfolding diseases and biological evolution , 2003, Journal of Molecular Medicine.
[82] C. Dobson,et al. Rationalization of the effects of mutations on peptide andprotein aggregation rates , 2003, Nature.
[83] Christopher M. Dobson,et al. A camelid antibody fragment inhibits the formation of amyloid fibrils by human lysozyme , 2003, Nature.
[84] Giampaolo Merlini,et al. Molecular mechanisms of amyloidosis. , 2003, The New England journal of medicine.
[85] C. Dobson,et al. Amyloid protofilaments from the calcium-binding protein equine lysozyme: formation of ring and linear structures depends on pH and metal ion concentration. , 2003, Journal of Molecular Biology.
[86] Dennis Claessen,et al. A novel class of secreted hydrophobic proteins is involved in aerial hyphae formation in Streptomyces coelicolor by forming amyloid-like fibrils. , 2003, Genes & development.
[87] G. Raposo,et al. Proprotein convertase cleavage liberates a fibrillogenic fragment of a resident glycoprotein to initiate melanosome biogenesis , 2003, The Journal of cell biology.
[88] Christiane Ritter,et al. Domain organization and structure–function relationship of the HET‐s prion protein of Podospora anserina , 2003, The EMBO journal.
[89] J. Trojanowski,et al. Initiation and Synergistic Fibrillization of Tau and Alpha-Synuclein , 2003, Science.
[90] Carl W. Cotman,et al. Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis , 2003, Science.
[91] V. Uversky,et al. Polycation‐induced oligomerization and accelerated fibrillation of human α‐synuclein in vitro , 2003 .
[92] Ashley I. Bush,et al. The metallobiology of Alzheimer's disease , 2003, Trends in Neurosciences.
[93] R. Tycko. Insights into the amyloid folding problem from solid-state NMR. , 2003, Biochemistry.
[94] J. Doucet,et al. The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils. , 2003, Journal of structural biology.
[95] G. Damaschun,et al. Assembly of amyloid protofibrils via critical oligomers--a novel pathway of amyloid formation. , 2003, Journal of molecular biology.
[96] 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.
[97] Robert G Griffin,et al. Molecular conformation of a peptide fragment of transthyretin in an amyloid fibril , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[98] R. Leapman,et al. A structural model for Alzheimer's β-amyloid fibrils based on experimental constraints from solid state NMR , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[99] Fabrizio Chiti,et al. Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[100] J. Kelly,et al. Sequence-dependent denaturation energetics: A major determinant in amyloid disease diversity , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[101] Christopher M Dobson,et al. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation , 2002, The EMBO journal.
[102] 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.
[103] D. Teplow,et al. Kinetic Studies of Amyloid β-Protein Fibril Assembly , 2002, The Journal of Biological Chemistry.
[104] M. Monti,et al. Topological investigation of amyloid fibrils obtained from β2‐microglobulin , 2002, Protein science : a publication of the Protein Society.
[105] David A. Lomas,et al. Human genetics and disease: Serpinopathies and the conformational dementias , 2002, Nature Reviews Genetics.
[106] J. J. Balbach,et al. Supramolecular Structure in Full-Length Alzheimer's β-Amyloid Fibrils: Evidence for a Parallel β-Sheet Organization from Solid-State Nuclear Magnetic Resonance , 2002 .
[107] F. Vollrath,et al. Amyloidogenic nature of spider silk. , 2002, European journal of biochemistry.
[108] Ronald W. Davis,et al. Functional profiling of the Saccharomyces cerevisiae genome , 2002, Nature.
[109] P. Aebischer,et al. α-Synucleinopathy and selective dopaminergic neuron loss in a rat lentiviral-based model of Parkinson's disease , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[110] Christopher M. Dobson,et al. The protofilament structure of insulin amyloid fibrils , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[111] Christine Wurth,et al. Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis. , 2002, Journal of molecular biology.
[112] S. Radford,et al. The yeast prion Ure2p retains its native α‐helical conformation upon assembly into protein fibrils in vitro , 2002, The EMBO journal.
[113] T. Iwatsubo,et al. Biochemical Characterization of the Core Structure of α-Synuclein Filaments* , 2002, The Journal of Biological Chemistry.
[114] Sofia Nyström,et al. Transmissibility of systemic amyloidosis by a prion-like mechanism , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[115] J. Clarke,et al. Sequence conservation in Ig-like domains: the role of highly conserved proline residues in the fibronectin type III superfamily. , 2002, Journal of molecular biology.
[116] M. Hoshino,et al. Mapping the core of the β2-microglobulin amyloid fibril by H/D exchange , 2002, Nature Structural Biology.
[117] Xin Wu,et al. Immunization reverses memory deficits without reducing brain Aβ burden in Alzheimer's disease model , 2002, Nature Neuroscience.
[118] J T Finch,et al. Amyloid fibers are water-filled nanotubes , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[119] Sebastian Doniach,et al. Biophysical Properties of the Synucleins and Their Propensities to Fibrillate , 2002, The Journal of Biological Chemistry.
[120] C. Dobson,et al. Inherent toxicity of aggregates implies a common mechanism for protein misfolding diseases , 2002, Nature.
[121] V. Uversky. Natively unfolded proteins: A point where biology waits for physics , 2002, Protein science : a publication of the Protein Society.
[122] James C. Sacchettini,et al. Therapeutic strategies for human amyloid diseases , 2002, Nature Reviews Drug Discovery.
[123] C. Dobson,et al. Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme , 2002, Nature Structural Biology.
[124] Christopher M. Dobson,et al. Kinetic partitioning of protein folding and aggregation , 2002, Nature Structural Biology.
[125] Scott J. Hultgren,et al. Role of Escherichia coli Curli Operons in Directing Amyloid Fiber Formation , 2002, Science.
[126] D. Raleigh,et al. Low levels of asparagine deamidation can have a dramatic effect on aggregation of amyloidogenic peptides : Implications for the study of amyloid formation , 2000 .
[127] John Q. Trojanowski,et al. Chaperone Suppression of α-Synuclein Toxicity in a Drosophila Model for Parkinson's Disease , 2001, Science.
[128] M. Sousa,et al. Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates. , 2001, The American journal of pathology.
[129] G. Bitan,et al. Amyloid (cid:1) -Protein Oligomerization PRENUCLEATION INTERACTIONS REVEALED BY PHOTO-INDUCED CROSS-LINKING OF UNMODIFIED PROTEINS* , 2001 .
[130] R. Wetzel,et al. Structural features of the Abeta amyloid fibril elucidated by limited proteolysis. , 2001, Biochemistry.
[131] S. Younkin,et al. The 'Arctic' APP mutation (E693G) causes Alzheimer's disease by enhanced Aβ protofibril formation , 2001, Nature Neuroscience.
[132] G. Irvine,et al. Aggregation and neurotoxicity of α-synuclein and related peptides , 2001 .
[133] Rui M. M. Brito,et al. Tetramer Dissociation and Monomer Partial Unfolding Precedes Protofibril Formation in Amyloidogenic Transthyretin Variants* , 2001, The Journal of Biological Chemistry.
[134] V. Uversky,et al. Is Congo Red an Amyloid-specific Dye?* , 2001, The Journal of Biological Chemistry.
[135] J. King,et al. Frequencies of amino acid strings in globular protein sequences indicate suppression of blocks of consecutive hydrophobic residues , 2001, Protein science : a publication of the Protein Society.
[136] Y. Kallberg,et al. Prediction of Amyloid Fibril-forming Proteins* , 2001, The Journal of Biological Chemistry.
[137] C. Dobson,et al. Reduction of the amyloidogenicity of a protein by specific binding of ligands to the native conformation , 2001, Protein science : a publication of the Protein Society.
[138] M. Pepys. Pathogenesis, diagnosis and treatment of systemic amyloidosis. , 2001, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.
[139] T. Konno. Amyloid-induced aggregation and precipitation of soluble proteins: an electrostatic contribution of the Alzheimer's beta(25-35) amyloid fibril. , 2001, Biochemistry.
[140] J. Mackay,et al. The hydrophobin EAS is largely unstructured in solution and functions by forming amyloid-like structures. , 2001, Structure.
[141] R. Wetzel,et al. Abeta amyloid fibrils possess a core structure highly resistant to hydrogen exchange. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[142] 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 .
[143] H. True,et al. A yeast prion provides a mechanism for genetic variation and phenotypic diversity , 2000, Nature.
[144] S. Saupe,et al. Molecular Genetics of Heterokaryon Incompatibility in Filamentous Ascomycetes , 2000, Microbiology and Molecular Biology Reviews.
[145] D. Otzen,et al. Designed protein tetramer zipped together with a hydrophobic Alzheimer homology: a structural clue to amyloid assembly. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[146] S. Lindquist,et al. Nucleated conformational conversion and the replication of conformational information by a prion determinant. , 2000, Science.
[147] G. Vriend,et al. Amyloids protect the silkmoth oocyte and embryo , 2000, FEBS letters.
[148] D. Selkoe,et al. The oligomerization of amyloid beta-protein begins intracellularly in cells derived from human brain. , 2000, Biochemistry.
[149] L. Regan,et al. A systematic exploration of the influence of the protein stability on amyloid fibril formation in vitro. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[150] L. Serpell,et al. The protofilament substructure of amyloid fibrils. , 2000, Journal of molecular biology.
[151] D. Foguel,et al. The preaggregated state of an amyloidogenic protein: hydrostatic pressure converts native transthyretin into the amyloidogenic state. , 2000, Proceedings of the National Academy of Sciences of the United States of America.
[152] S. Müller,et al. Studies on the in Vitro Assembly of Aβ 1–40: Implications for the Search for Aβ Fibril Formation Inhibitors , 2000 .
[153] C M Dobson,et al. Mutational analysis of the propensity for amyloid formation by a globular protein , 2000, The EMBO journal.
[154] M. Hecht,et al. Nature disfavors sequences of alternating polar and non-polar amino acids: implications for amyloidogenesis. , 2000, Journal of molecular biology.
[155] L. Mucke,et al. Dopaminergic loss and inclusion body formation in alpha-synuclein mice: implications for neurodegenerative disorders. , 2000, Science.
[156] P. Lansbury,et al. Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid. , 2000, Biochemistry.
[157] L Serrano,et al. Protein engineering as a strategy to avoid formation of amyloid fibrils , 2000, Protein science : a publication of the Protein Society.
[158] C M Dobson,et al. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy , 2000, Protein science : a publication of the Protein Society.
[159] M. Schiffer,et al. Physicochemical consequences of amino acid variations that contribute to fibril formation by immunoglobulin light chains , 2008, Protein science : a publication of the Protein Society.
[160] C. Masters,et al. Soluble pool of Aβ amyloid as a determinant of severity of neurodegeneration in Alzheimer's disease , 1999, Annals of neurology.
[161] C. Ionescu-Zanetti,et al. Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[162] Dominic M. Walsh,et al. Protofibrillar Intermediates of Amyloid β-Protein Induce Acute Electrophysiological Changes and Progressive Neurotoxicity in Cortical Neurons , 1999, The Journal of Neuroscience.
[163] Gary Lynch,et al. Alterations in synaptic transmission and long-term potentiation in hippocampal slices from young and aged PDAPP mice , 1999, Brain Research.
[164] D. Selkoe,et al. Amyloid beta-protein fibrillogenesis. Structure and biological activity of protofibrillar intermediates. , 1999, The Journal of biological chemistry.
[165] L. Lue,et al. Soluble Amyloid β Peptide Concentration as a Predictor of Synaptic Change in Alzheimer’s Disease , 1999 .
[166] C. Dobson. Protein misfolding, evolution and disease. , 1999, Trends in biochemical sciences.
[167] J. Trojanowski,et al. The Levels of Soluble versus Insoluble Brain Aβ Distinguish Alzheimer's Disease from Normal and Pathologic Aging , 1999, Experimental Neurology.
[168] M. Tuite,et al. Translation termination efficiency can be regulated in Saccharomyces cerevisiae by environmental stress through a prion‐mediated mechanism , 1999, The EMBO journal.
[169] Veerle Baekelandt,et al. Early Phenotypic Changes in Transgenic Mice That Overexpress Different Mutants of Amyloid Precursor Protein in Brain* , 1999, The Journal of Biological Chemistry.
[170] Elena Orlova,et al. Cryo‐electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing , 1999, The EMBO journal.
[171] Bruce A. Yankner,et al. Aging renders the brain vulnerable to amyloid β-protein neurotoxicity , 1998, Nature Medicine.
[172] I D Campbell,et al. Amyloid fibril formation by an SH3 domain. , 1998, Proceedings of the National Academy of Sciences of the United States of America.
[173] S. Minoshima,et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism , 1998, Nature.
[174] J. Kelly,et al. The alternative conformations of amyloidogenic proteins and their multi-step assembly pathways. , 1998, Current opinion in structural biology.
[175] P. Lansbury,et al. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-beta protein. , 1997, Chemistry & biology.
[176] R. Wickner,et al. The prion model for [URE3] of yeast: spontaneous generation and requirements for propagation. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[177] V. Coustou,et al. The protein product of the het-s heterokaryon incompatibility gene of the fungus Podospora anserina behaves as a prion analog. , 1997, Proceedings of the National Academy of Sciences of the United States of America.
[178] D. Walsh,et al. Amyloid beta-protein fibrillogenesis. Detection of a protofibrillar intermediate. , 1997, The Journal of biological chemistry.
[179] U Aebi,et al. Polymorphic fibrillar assembly of human amylin. , 1997, Journal of structural biology.
[180] Peter T. Lansbury,et al. Observation of metastable Aβ amyloid protofibrils by atomic force microscopy , 1997 .
[181] Satoru Suzuki,et al. Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro , 1997 .
[182] C. Blake,et al. The structure of amyloid fibrils by electron microscopy and X-ray diffraction. , 1997, Advances in protein chemistry.
[183] M. Emmerling,et al. Morphology and Toxicity of Aβ-(1-42) Dimer Derived from Neuritic and Vascular Amyloid Deposits of Alzheimer's Disease* , 1996, The Journal of Biological Chemistry.
[184] S. Paushkin,et al. Propagation of the yeast prion‐like [psi+] determinant is mediated by oligomerization of the SUP35‐encoded polypeptide chain release factor. , 1996, The EMBO journal.
[185] C. Bergeron,et al. Copper/zinc superoxide dismutase expression in the human central nervous system. Correlation with selective neuronal vulnerability. , 1996, The American journal of pathology.
[186] U Aebi,et al. Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin. , 1995, Journal of structural biology.
[187] S. Squazzo,et al. Aggregation of Secreted Amyloid -Protein into Sodium Dodecyl Sulfate-stable Oligomers in Cell Culture (*) , 1995, The Journal of Biological Chemistry.
[188] P. Lansbury,et al. The core Alzheimer's peptide NAC forms amyloid fibrils which seed and are seeded by beta-amyloid: is NAC a common trigger or target in neurodegenerative disease? , 1995, Chemistry & biology.
[189] B. Yankner,et al. Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. , 1994, Proceedings of the National Academy of Sciences of the United States of America.
[190] H. Gertz,et al. Stability of cell size and nucleolar size in Lewy body containing neurons of substantia nigra in Parkinson's disease , 1994, Brain Research.
[191] Carl W. Cotman,et al. In vitro aging of ß-amyloid protein causes peptide aggregation and neurotoxicity , 1991, Brain Research.
[192] R. Doolittle,et al. A simple method for displaying the hydropathic character of a protein. , 1982, Journal of molecular biology.