Amyloidogenic hexapeptide fragment of medin: homology to functional islet amyloid polypeptide fragments
暂无分享,去创建一个
[1] Sharon Gilead,et al. Identification and characterization of a novel molecular-recognition and self-assembly domain within the islet amyloid polypeptide. , 2002, Journal of molecular biology.
[2] Ehud Gazit,et al. Global analysis of tandem aromatic octapeptide repeats: The significance of the aromatic-glycine motif , 2002, Bioinform..
[3] T. Thomas,et al. Aspirin and non-steroidal anti-inflammatory drugs inhibit amyloid-β aggregation , 2001 .
[4] P. Westermark,et al. Senile aortic amyloid. Evidence for two distinct forms of localized deposits. , 1992, The American journal of pathology.
[5] Ehud Gazit,et al. Analysis of the Minimal Amyloid-forming Fragment of the Islet Amyloid Polypeptide , 2001, The Journal of Biological Chemistry.
[6] W. Atkins,et al. Self-assembly and gelation of oxidized glutathione in organic solvents. , 2001, Journal of the American Chemical Society.
[7] P. Lansbury,et al. Amyloid fibrillogenesis: themes and variations. , 2000, Current opinion in structural biology.
[8] C. Blake,et al. From the globular to the fibrous state: protein structure and structural conversion in amyloid formation , 1998, Quarterly Reviews of Biophysics.
[9] R. Friedland,et al. Nicotine inhibits amyloid formation by the beta-peptide. , 1996, Biochemistry.
[10] Meital Reches,et al. Casting Metal Nanowires Within Discrete Self-Assembled Peptide Nanotubes , 2003, Science.
[11] G. Forloni,et al. Anti‐amyloidogenic activity of tetracyclines: studies in vitro , 2001, FEBS letters.
[12] P. Lansbury,et al. Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. , 1997, Annual review of biochemistry.
[13] R. Pickersgill,et al. The architecture of parallel β-helices and related folds , 2001 .
[14] P. Lansbury,et al. Seeding “one-dimensional crystallization” of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie? , 1993, Cell.
[15] Meital Reches,et al. Amyloid Fibril Formation by Pentapeptide and Tetrapeptide Fragments of Human Calcitonin* , 2002, The Journal of Biological Chemistry.
[16] J. Bernhagen,et al. Conformational transitions of islet amyloid polypeptide (IAPP) in amyloid formation in vitro. , 1999, Journal of molecular biology.
[17] B. Ahrén,et al. Islet amyloid and type 2 diabetes mellitus. , 2000, The New England journal of medicine.
[18] J. Bernhagen,et al. Identification of a penta- and hexapeptide of islet amyloid polypeptide (IAPP) with amyloidogenic and cytotoxic properties. , 2000, Journal of molecular biology.
[19] L. Tjernberg,et al. Charge Attraction and β Propensity Are Necessary for Amyloid Fibril Formation from Tetrapeptides* , 2002, The Journal of Biological Chemistry.
[20] C. Dobson. Protein misfolding, evolution and disease. , 1999, Trends in biochemical sciences.
[21] 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.
[22] D. Downing,et al. Amyloid fibrils may be assembled from beta-helical protofibrils. , 1998, Biochemistry.
[23] Eric J. Simon,et al. Structural model for the β-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide , 1995, Nature Structural Biology.
[24] Y. Cordeiro,et al. Modulation of Prion Protein Oligomerization, Aggregation, and β-sheet Conversion by 4,4′-Dianilino-1,1′-binaphthyl-5,5′-sulfonate (bis-ANS)* , 2004, Journal of Biological Chemistry.
[25] Ehud Gazit,et al. A possible role for π‐stacking in the self‐assembly of amyloid fibrils , 2002, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.
[26] D. Downing,et al. Fibril formation by amyloid-beta proteins may involve beta-helical protofibrils. , 1999, The journal of peptide research : official journal of the American Peptide Society.
[27] J. Sipe,et al. Review: history of the amyloid fibril. , 2000, Journal of structural biology.
[28] Ehud Gazit,et al. The "Correctly Folded" state of proteins: is it a metastable state? , 2002, Angewandte Chemie.
[29] V. Uversky,et al. Is Congo Red an Amyloid-specific Dye?* , 2001, The Journal of Biological Chemistry.
[30] R. Pickersgill,et al. The architecture of parallel beta-helices and related folds. , 2001, Progress in biophysics and molecular biology.
[31] L. Tjernberg,et al. Medin: an integral fragment of aortic smooth muscle cell-produced lactadherin forms the most common human amyloid. , 1999, Proceedings of the National Academy of Sciences of the United States of America.