The N-terminal fragment of human islet amyloid polypeptide is non-fibrillogenic in the presence of membranes and does not cause leakage of bilayers of physiologically relevant lipid composition.

[1]  A. Jayaprakash,et al.  Liposome Damage and Modeling of Fragments of Human Islet Amyloid Polypeptide (IAPP) Support a Two-Step Model of Membrane Destruction , 2010, International Journal of Peptide Research and Therapeutics.

[2]  Maarten F. M. Engel,et al.  The role of the disulfide bond in the interaction of islet amyloid polypeptide with membranes , 2010, European Biophysics Journal.

[3]  J. Brender,et al.  Induction of negative curvature as a mechanism of cell toxicity by amyloidogenic peptides: the case of islet amyloid polypeptide. , 2009, Journal of the American Chemical Society.

[4]  Amedeo Caflisch,et al.  Amyloid aggregation on lipid bilayers and its impact on membrane permeability. , 2009 .

[5]  Kevin Hartman,et al.  A single mutation in the nonamyloidogenic region of islet amyloid polypeptide greatly reduces toxicity. , 2008, Biochemistry.

[6]  E. Dufourc,et al.  Surfactin-triggered small vesicle formation of negatively charged membranes: a novel membrane-lysis mechanism. , 2008, Biophysical journal.

[7]  S. Jayasinghe,et al.  Structure of α-Helical Membrane-bound Human Islet Amyloid Polypeptide and Its Implications for Membrane-mediated Misfolding* , 2008, Journal of Biological Chemistry.

[8]  Maarten F. M. Engel,et al.  Recent Insights in Islet Amyloid Polypeptide-Induced Membrane Disruption and Its Role in β-Cell Death in Type 2 Diabetes Mellitus , 2008, Experimental diabetes research.

[9]  J. Brender,et al.  Amyloid fiber formation and membrane disruption are separate processes localized in two distinct regions of IAPP, the type-2-diabetes-related peptide. , 2008, Journal of the American Chemical Society.

[10]  Maarten F. M. Engel,et al.  Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane , 2008, Proceedings of the National Academy of Sciences.

[11]  K. Beyer.  Mechanistic aspects of Parkinson’s disease: α-synuclein and the biomembrane , 2007, Cell Biochemistry and Biophysics.

[12]  M. Horowitz,et al.  Amylin , 2006 .

[13]  Maarten F. M. Engel,et al.  Islet amyloid polypeptide inserts into phospholipid monolayers as monomer. , 2006, Journal of molecular biology.

[14]  S. Jayasinghe,et al.  Lipid membranes modulate the structure of islet amyloid polypeptide. , 2005, Biochemistry.

[15]  Ian Parker,et al.  Calcium Dysregulation and Membrane Disruption as a Ubiquitous Neurotoxic Mechanism of Soluble Amyloid Oligomers*♦ , 2005, Journal of Biological Chemistry.

[16]  R. Rydel,et al.  Nucleation-Dependent Polymerization Is an Essential Component of Amyloid-Mediated Neuronal Cell Death , 2005, The Journal of Neuroscience.

[17]  Maarten F. M. Engel,et al.  Islet amyloid polypeptide‐induced membrane leakage involves uptake of lipids by forming amyloid fibers , 2004, FEBS letters.

[18]  A. Miranker,et al.  Phospholipid catalysis of diabetic amyloid assembly. , 2004, Journal of molecular biology.

[19]  N. Sreerama,et al.  On the analysis of membrane protein circular dichroism spectra , 2004, Protein science : a publication of the Protein Society.

[20]  E. Gazit,et al.  The human islet amyloid polypeptide forms transient membrane-active prefibrillar assemblies. , 2003, Biochemistry.

[21]  P. Westermark,et al.  Islet amyloid polypeptide inhibits glucagon release and exerts a dual action on insulin release from isolated islets , 2003, Regulatory Peptides.

[22]  A. Geliebter,et al.  Amylin, food intake, and obesity. , 2002, Obesity research.

[23]  R. Liskamp,et al.  Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides. , 2002, Chemistry.

[24]  A. Miranker,et al.  Islet amyloid: phase partitioning and secondary nucleation are central to the mechanism of fibrillogenesis. , 2002, Biochemistry.

[25]  E. Air,et al.  Inhibition of central amylin signaling increases food intake and body adiposity in rats. , 2001, Endocrinology.

[26]  M. Kirkitadze,et al.  Identification and characterization of key kinetic intermediates in amyloid beta-protein fibrillogenesis. , 2001, Journal of molecular biology.

[27]  C. Yip,et al.  Amyloid-beta peptide assembly: a critical step in fibrillogenesis and membrane disruption. , 2001, Biophysical journal.

[28]  B. Ahrén,et al.  Islet amyloid and type 2 diabetes mellitus. , 2000, The New England journal of medicine.

[29]  Y. Shai,et al.  Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by alpha-helical antimicrobial and cell non-selective membrane-lytic peptides. , 1999, Biochimica et biophysica acta.

[30]  D. Harrison,et al.  The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. , 1999, Diabetes.

[31]  H. Shao,et al.  Solution structures of micelle-bound amyloid beta-(1-40) and beta-(1-42) peptides of Alzheimer's disease. , 1999, Journal of molecular biology.

[32]  B. Kagan,et al.  Pore Formation by the Cytotoxic Islet Amyloid Peptide Amylin (*) , 1996, The Journal of Biological Chemistry.

[33]  S. Lenzen,et al.  Lipid composition of glucose-stimulated pancreatic islets and insulin-secreting tumor cells , 1994, Lipids.

[34]  Jing Zhang,et al.  Disulfide bond formation in peptides by dimethyl sulfoxide. Scope and applications , 1991 .

[35]  S. Fleischer,et al.  Two dimensional thin layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots , 1970, Lipids.

[36]  K. Beyer.  Mechanistic aspects of Parkinson's disease: alpha-synuclein and the biomembrane. , 2007, Cell biochemistry and biophysics.

[37]  H. Levine.  Quantification of beta-sheet amyloid fibril structures with thioflavin T. , 1999, Methods in enzymology.