The parallel superpleated beta-structure as a model for amyloid fibrils of human amylin.
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[1] P. Lansbury,et al. Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. , 2002, Biochemistry.
[2] 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.
[3] R. Leapman,et al. Amyloid Fibril Formation by Aβ16-22, a Seven-Residue Fragment of the Alzheimer's β-Amyloid Peptide, and Structural Characterization by Solid State NMR† , 2000 .
[4] P E Fraser,et al. Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis. , 2001, Journal of molecular biology.
[5] D. W. Hayden,et al. Feline insular amyloid. Ultrastructural evidence for intracellular formation by nonendocrine cells. , 1981, Laboratory investigation; a journal of technical methods and pathology.
[6] E. Opie. THE RELATION OE DIABETES MELLITUS TO LESIONS OF THE PANCREAS. HYALINE DEGENERATION OF THE ISLANDS OE LANGERHANS , 1901, The Journal of experimental medicine.
[7] J. Thornton,et al. PROCHECK: a program to check the stereochemical quality of protein structures , 1993 .
[8] U Aebi,et al. Amyloid fibril formation from full-length and fragments of amylin. , 2000, Journal of structural biology.
[9] U. Aebi,et al. Full-length rat amylin forms fibrils following substitution of single residues from human amylin. , 2003, Journal of molecular biology.
[10] S. Steinbacher,et al. Crystal structure of P22 tailspike protein: interdigitated subunits in a thermostable trimer. , 1994, Science.
[11] H. King,et al. Global Burden of Diabetes, 1995–2025: Prevalence, numerical estimates, and projections , 1998, Diabetes Care.
[12] C. Betsholtz,et al. Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation. , 1990, Proceedings of the National Academy of Sciences of the United States of America.
[13] U. Aebi,et al. Watching amyloid fibrils grow by time-lapse atomic force microscopy. , 1999, Journal of molecular biology.
[14] E. D. de Koning,et al. Effect of pH and insulin on fibrillogenesis of islet amyloid polypeptide in vitro. , 1995, Biochemistry.
[15] D. Raleigh,et al. Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin. , 1999, Journal of molecular biology.
[16] J. M. Griffiths,et al. Rotational Resonance Solid-State NMR Elucidates a Structural Model of Pancreatic Amyloid , 1995 .
[17] J. Bernhagen,et al. Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro. , 1999, Journal of molecular biology.
[18] U Aebi,et al. Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin. , 1995, Journal of structural biology.
[19] A. Miranker,et al. Islet amyloid polypeptide: identification of long-range contacts and local order on the fibrillogenesis pathway. , 2001, Journal of molecular biology.
[20] L. Serpell,et al. Structural characterisation of islet amyloid polypeptide fibrils. , 2004, Journal of molecular biology.
[21] J. Critchley,et al. The islet amyloid polypeptide (amylin) gene S20G mutation in Chinese subjects: Evidence for associations with type 2 diabetes and cholesterol levels , 2001, Clinical endocrinology.
[22] Ralf Langen,et al. Identifying Structural Features of Fibrillar Islet Amyloid Polypeptide Using Site-directed Spin Labeling* , 2004, Journal of Biological Chemistry.
[23] A. Clark,et al. Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology. , 2001, Biochimica et biophysica acta.
[24] U Aebi,et al. Polymorphic fibrillar assembly of human amylin. , 1997, Journal of structural biology.
[25] M. Yoder,et al. New domain motif: the structure of pectate lyase C, a secreted plant virulence factor. , 1993, Science.
[26] A. Naito,et al. Structural diversity of amyloid fibril formed in human calcitonin as revealed by site‐directed 13C solid‐state NMR spectroscopy , 2004, Magnetic resonance in chemistry : MRC.
[27] E. Baker,et al. Hydrogen bonding in globular proteins. , 1984, Progress in biophysics and molecular biology.
[28] R J Fletterick,et al. Interactive program for visualization and modelling of proteins, nucleic acids and small molecules , 1986 .
[29] J. Permert,et al. Renal elimination of islet amyloid polypeptide. , 1997, Biochemical and biophysical research communications.
[30] E. Wilander,et al. The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus , 1978, Diabetologia.
[31] S. Wimalawansa,et al. Amylin, calcitonin gene-related peptide, calcitonin, and adrenomedullin: a peptide superfamily. , 1997, Critical reviews in neurobiology.
[32] B. Hansen,et al. Diabetes mellitus in Macaca mulatta monkeys is characterised by islet amyloidosis and reduction in beta-cell population , 1993, Diabetologia.
[33] P. Emsley,et al. Structure of Bordetella pertussis virulence factor P.69 pertactin , 1996, Nature.
[34] H. Eklund,et al. Crystal structure of plant pectin methylesterase , 2002, FEBS letters.
[35] A. Motta,et al. Modulating Calcitonin Fibrillogenesis , 2004, Journal of Biological Chemistry.
[36] L. Pauling,et al. Stable configurations of polypeptide chains , 1953, Proceedings of the Royal Society of London. Series B - Biological Sciences.
[37] U. Aebi,et al. Human Amylin Oligomer Growth and Fibril Elongation Define Two Distinct Phases in Amyloid Formation* , 2004, Journal of Biological Chemistry.