Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity. - Wikidata - wikimedia - TriplyDB

Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity.

Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity.

http://www.wikidata.org/entity/Q33653452

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Mechanisms of islet amyloidosis toxicity in type 2 diabetes On the Environmental Factors Affecting the Structural and Cytotoxic Properties of IAPP Peptides Structure and membrane orientation of IAPP in its natively amidated form at physiological pH in a membrane environment Protein misfolding and aggregation in Alzheimer's disease and type 2 diabetes mellitus Inter-species cross-seeding: stability and assembly of rat-human amylin aggregates The therapeutic potential of metabolic hormones in the treatment of age-related cognitive decline and Alzheimer's disease.Rationally designed, nontoxic, nonamyloidogenic analogues of human islet amyloid polypeptide with improved solubility Short Peptides as Inhibitors of Amyloid Aggregation Misfolded proteins in Alzheimer's disease and type II diabetes.Islet Amyloid Polypeptide: Structure, Function, and Pathophysiology.Inhibition of Toxic IAPP Amyloid by Extracts of Common Fruits Lessons from two prevalent amyloidoses-what amylin and Aβ have in common Islet amyloid: from fundamental biophysics to mechanisms of cytotoxicity.Conformational Ensemble of hIAPP Dimer: Insight into the Molecular Mechanism by which a Green Tea Extract inhibits hIAPP Aggregation.IAPP aggregation and cellular toxicity are inhibited by 1,2,3,4,6-penta-O-galloyl-β-D-glucose.Regulation of the aggregation behavior of human islet amyloid polypeptide fragment by titanocene complexes.2DIR spectroscopy of human amylin fibrils reflects stable β-sheet structure.Myricetin Inhibits Islet Amyloid Polypeptide (IAPP) Aggregation and Rescues Living Mammalian Cells from IAPP Toxicity.A membrane-bound antiparallel dimer of rat islet amyloid polypeptide.Idealized models of protofilaments of human islet amyloid polypeptide Full length amylin oligomer aggregation: insights from molecular dynamics simulations and implications for design of aggregation inhibitors.Key aromatic/hydrophobic amino acids controlling a cross-amyloid peptide interaction versus amyloid self-assembly.

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P2860

Selection for nonamyloidogenic mutants of islet amyloid polypeptide (IAPP) identifies an extended region for amyloidogenicity.

http://www.wikidata.org/entity/Q33653452

description

2010 nî lūn-bûn

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2010 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Selection for nonamyloidogenic ...... d region for amyloidogenicity.

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Selection for nonamyloidogenic ...... d region for amyloidogenicity.

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Selection for nonamyloidogenic ...... d region for amyloidogenicity.

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Selection for nonamyloidogenic ...... d region for amyloidogenicity.

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Selection for nonamyloidogenic ...... d region for amyloidogenicity.

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Anastasia Calciano

http://www.w3.org/2001/XMLSchema#string

Ayano Fox

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Camille Errecart Casanova

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Luiza A Nogaj

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Thibaut Snollaerts

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P2860

Structures of rat and human islet amyloid polypeptide IAPP(1-19) in micelles by NMR spectroscopy

Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process

Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteins

Direct detection of transient alpha-helical states in islet amyloid polypeptide

Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation

De novo folding of GFP fusion proteins: high efficiency in eukaryotes but not in bacteria.

A comparative study of the relationship between protein structure and beta-aggregation in globular and intrinsically disordered proteins.

Mutations that reduce aggregation of the Alzheimer's Abeta42 peptide: an unbiased search for the sequence determinants of Abeta amyloidogenesis.

Combinatorial approaches to probe the sequence determinants of protein aggregation and amyloidogenicity.

A high-throughput screen for compounds that inhibit aggregation of the Alzheimer's peptide.

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scholarly article

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10.1021/BI100337P

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