Small-molecule inhibitors of islet amyloid polypeptide fibril formation.

[1]  E. Mandelkow,et al.  Rhodanine-based tau aggregation inhibitors in cell models of tauopathy. , 2007, Angewandte Chemie.

[2]  A. Cavalli,et al.  Insight Into the Kinetic of Amyloid β (1–42) Peptide Self‐Aggregation: Elucidation of Inhibitors’ Mechanism of Action , 2007, Chembiochem : a European journal of chemical biology.

[3]  A. Meister,et al.  Mechanism of islet amyloid polypeptide fibrillation at lipid interfaces studied by infrared reflection absorption spectroscopy. , 2007, Biophysical journal.

[4]  Boris Schmidt,et al.  Phenylthiazolyl-hydrazide and its derivatives are potent inhibitors of tau aggregation and toxicity in vitro and in cells. , 2007, Biochemistry.

[5]  S. Jayasinghe,et al.  Membrane interaction of islet amyloid polypeptide. , 2007, Biochimica et biophysica acta.

[6]  Chia-yu Lin,et al.  Toxic Human Islet Amyloid Polypeptide (h-IAPP) Oligomers Are Intracellular, and Vaccination to Induce Anti-Toxic Oligomer Antibodies Does Not Prevent h-IAPP–Induced β-Cell Apoptosis in h-IAPP Transgenic Mice , 2007, Diabetes.

[7]  R. Kayed,et al.  Small Molecule Inhibitors of Aggregation Indicate That Amyloid β Oligomerization and Fibrillization Pathways Are Independent and Distinct* , 2007, Journal of Biological Chemistry.

[8]  A. Kapurniotu,et al.  IAPP mimic blocks Abeta cytotoxic self-assembly: cross-suppression of amyloid toxicity of Abeta and IAPP suggests a molecular link between Alzheimer's disease and type II diabetes. , 2007, Angewandte Chemie.

[9]  Li‐Mei Yan,et al.  Ein IAPP‐Mimetikum blockiert die zytotoxische Aggregation von Aβ – die Kreuzunterdrückung der Amyloidtoxizität von Aβ und IAPP deutet auf einen molekularen Zusammenhang zwischen Alzheimer‐Krankheit und Typ‐II‐Diabetes hin , 2007 .

[10]  C. Dobson,et al.  Protein misfolding, functional amyloid, and human disease. , 2006, Annual review of biochemistry.

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

[12]  A. Kapurniotu,et al.  Design of a mimic of nonamyloidogenic and bioactive human islet amyloid polypeptide (IAPP) as nanomolar affinity inhibitor of IAPP cytotoxic fibrillogenesis , 2006, Proceedings of the National Academy of Sciences of the United States of America.

[13]  Ehud Gazit,et al.  Inhibition of Amyloid Fibril Formation by Polyphenols: Structural Similarity and Aromatic Interactions as a Common Inhibition Mechanism , 2006, Chemical biology & drug design.

[14]  Takeshi Iwatsubo,et al.  Inhibition of Heparin-induced Tau Filament Formation by Phenothiazines, Polyphenols, and Porphyrins* , 2005, Journal of Biological Chemistry.

[15]  E. Mandelkow,et al.  Anthraquinones Inhibit Tau Aggregation and Dissolve Alzheimer's Paired Helical Filaments in Vitro and in Cells* , 2005, Journal of Biological Chemistry.

[16]  R. Jansen,et al.  Amyloidogenic self-assembly of insulin aggregates probed by high resolution atomic force microscopy. , 2005, Biophysical journal.

[17]  M. R. Nilsson.  Techniques to study amyloid fibril formation in vitro. , 2004, Methods.

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

[19]  R. Jansen,et al.  Insulin forms amyloid in a strain‐dependent manner: An FT‐IR spectroscopic study , 2004, Protein science : a publication of the Protein Society.

[20]  C. Chirita,et al.  Ligand-dependent inhibition and reversal of tau filament formation. , 2004, Biochemistry.

[21]  C. Dobson.  Protein folding and misfolding , 2003, Nature.

[22]  Fred E. Cohen,et al.  Therapeutic approaches to protein-misfolding diseases , 2003, Nature.

[23]  Carl W. Cotman,et al.  Common Structure of Soluble Amyloid Oligomers Implies Common Mechanism of Pathogenesis , 2003, Science.

[24]  C. Soto,et al.  Converting a peptide into a drug: strategies to improve stability and bioavailability. , 2002, Current medicinal chemistry.

[25]  S. Tatulian.  Toward understanding interfacial activation of secretory phospholipase A2 (PLA2): membrane surface properties and membrane-induced structural changes in the enzyme contribute synergistically to PLA2 activation. , 2001, Biophysical journal.

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

[27]  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.

[28]  R. Turner,et al.  Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[29]  D. W. Hayden,et al.  Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. , 1987, Proceedings of the National Academy of Sciences of the United States of America.

[30]  C. Betsholtz,et al.  Islet amyloid polypeptide: mechanisms of amyloidogenesis in the pancreatic islets and potential roles in diabetes mellitus. , 1992, Laboratory investigation; a journal of technical methods and pathology.

[31]  E. Zeiger,et al.  Salmonella mutagenicity tests: III. Results from the testing of 255 chemicals. , 1987, Environmental mutagenesis.