Myoglobin forms amyloid fibrils by association of unfolded polypeptide segments
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Christopher M Dobson | C. Dobson | S. Diekmann | M. Fändrich | V. Forge | Marcus Fändrich | Katrin Buder | Marlis Kittler | Stephan Diekmann | Vincent Forge | Katrin Buder | Marlis Kittler
[1] J Collinge,et al. Reversible conversion of monomeric human prion protein between native and fibrilogenic conformations. , 1999, Science.
[2] P. Flory,et al. The Role of Dipole Interactions in Determining Polypeptide Configurations , 1965 .
[3] Andreas Hoenger,et al. De novo designed peptide-based amyloid fibrils , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[4] 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.
[5] F. Teale,et al. Cleavage of the haem-protein link by acid methylethylketone. , 1959, Biochimica et biophysica acta.
[6] Christopher M Dobson,et al. The behaviour of polyamino acids reveals an inverse side chain effect in amyloid structure formation , 2002, The EMBO journal.
[7] L Serrano,et al. Protein engineering as a strategy to avoid formation of amyloid fibrils , 2000, Protein science : a publication of the Protein Society.
[8] S. Lindquist,et al. Investigating protein conformation-based inheritance and disease in yeast. , 2001, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.
[9] J. Kelly,et al. Transthyretin quaternary and tertiary structural changes facilitate misassembly into amyloid. , 1997, Advances in protein chemistry.
[10] G. Fasman,et al. Computed circular dichroism spectra for the evaluation of protein conformation. , 1969, Biochemistry.
[11] 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.
[12] Christopher M. Dobson,et al. Amyloid fibrils from muscle myoglobin , 2001, Nature.
[13] C. Masters,et al. Amyloid Fibril Protein Nomenclature - 2002 , 2002, Amyloid : the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis.
[14] C. Dobson,et al. Local cooperativity in the unfolding of an amyloidogenic variant of human lysozyme , 2002, Nature Structural Biology.
[15] T. Huppert,et al. Chain length dependence of apomyoglobin folding: structural evolution from misfolded sheets to native helices. , 2003, Biochemistry.
[16] D. Thirumalai,et al. Exploring protein aggregation and self‐propagation using lattice models: Phase diagram and kinetics , 2002, Protein science : a publication of the Protein Society.
[17] J M Thornton,et al. Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations. , 1996, Journal of molecular biology.
[18] O. Ptitsyn,et al. Sequential mechanism of refolding of carbonic anhydrase B , 1987, FEBS letters.
[19] Fred E. Cohen,et al. Folding of Prion Protein to Its Native α-Helical Conformation Is under Kinetic Control* , 2001, The Journal of Biological Chemistry.
[20] Thomas E. Creighton,et al. Protein structure : a practical approach , 1997 .
[21] E. Gratton,et al. Pressure-induced perturbation of apomyoglobin structure: fluorescence studies on native and acidic compact forms. , 1996, Biochemistry.
[22] Bengt Nölting,et al. Mechanism of protein folding , 2000, Proteins.
[23] M. Perutz,et al. Aggregation of proteins with expanded glutamine and alanine repeats of the glutamine-rich and asparagine-rich domains of Sup35 and of the amyloid β-peptide of amyloid plaques , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[24] L. Serpell,et al. X-ray fiber diffraction of amyloid fibrils. , 1999, Methods in enzymology.
[25] Christopher M. Dobson,et al. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis , 1997, Nature.
[26] C. Yu,et al. Amyloid-like Fibril Formation in an All β-Barrel Protein Involves the Formation of Partially Structured Intermediate(s)* , 2002, The Journal of Biological Chemistry.
[27] C. Dobson,et al. Dependence on solution conditions of aggregation and amyloid formation by an SH3 domain. , 2001, Journal of molecular biology.
[28] H. Dyson,et al. Molecular hinges in protein folding: the urea-denatured state of apomyoglobin. , 2002, Biochemistry.
[29] C M Dobson,et al. Designing conditions for in vitro formation of amyloid protofilaments and fibrils. , 1999, Proceedings of the National Academy of Sciences of the United States of America.
[30] M. Landon. Protein structure: A Practical Approach : Edited by T.E. Creighton; IRL Press; Oxford University Press; Oxford, 1989; xviii + 355 pages; £30.00 , 1990 .
[31] 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.
[32] S. Radford,et al. Structural properties of an amyloid precursor of β2-microglobulin , 2002, Nature Structural Biology.
[33] P E Wright,et al. Peptide models of protein folding initiation sites. 1. Secondary structure formation by peptides corresponding to the G- and H-helices of myoglobin. , 1993, Biochemistry.
[34] A. Fink,et al. Discrete intermediates versus molten globule models for protein folding: characterization of partially folded intermediates of apomyoglobin. , 1998, Folding & design.
[35] C. Blake,et al. From the globular to the fibrous state: protein structure and structural conversion in amyloid formation , 1998, Quarterly Reviews of Biophysics.
[36] G. Brayer,et al. Horse heart metmyoglobin. A 2.8-A resolution three-dimensional structure determination. , 1988, The Journal of biological chemistry.
[37] Christopher M. Dobson,et al. Kinetic partitioning of protein folding and aggregation , 2002, Nature Structural Biology.
[38] C. Dobson. The structural basis of protein folding and its links with human disease. , 2001, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.
[39] George D Rose,et al. Polyproline II structure in a sequence of seven alanine residues , 2002, Proceedings of the National Academy of Sciences of the United States of America.
[40] 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.