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The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates

The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates

http://www.wikidata.org/entity/Q36519300

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Aromatic Cross-Strand Ladders Control the Structure and Stability of β-Rich Peptide Self-Assembly Mimics Converting the Highly Amyloidogenic Human Calcitonin into a Powerful Fibril Inhibitor by Three-dimensional Structure Homology with a Non-amyloidogenic Analogue Analysis of Synonymous Codon Usage Bias of Zika Virus and Its Adaption to the Hosts Aggregation propensity of the human proteome Complete phenotypic recovery of an Alzheimer's disease model by a quinone-tryptophan hybrid aggregation inhibitor Halogenation generates effective modulators of amyloid-Beta aggregation and neurotoxicity.CPAD, Curated Protein Aggregation Database: A Repository of Manually Curated Experimental Data on Protein and Peptide Aggregation.Prediction of amyloidogenic and disordered regions in protein chains Prediction of amyloid fibril-forming segments based on a support vector machine Rational design of aggregation-resistant bioactive peptides: reengineering human calcitonin.Computational and experimental approaches to reveal the effects of single nucleotide polymorphisms with respect to disease diagnostics Cooperativity among short amyloid stretches in long amyloidogenic sequences Inhibition study on insulin fibrillation and cytotoxicity by paclitaxel.A consensus method for the prediction of 'aggregation-prone' peptides in globular proteins."Janus" cyclic peptides: a new approach to amyloid fibril inhibition?Structure based descriptors for the estimation of colloidal interactions and protein aggregation propensities Butyrylcholinesterase attenuates amyloid fibril formation in vitro.Distinct position-specific sequence features of hexa-peptides that form amyloid-fibrils: application to discriminate between amyloid fibril and amorphous β-aggregate forming peptide sequences Identification of properties important to protein aggregation using feature selection.Anti-amyloidogenic properties of some phenolic compounds Structure-Based Peptide Design to Modulate Amyloid Beta Aggregation and Reduce Cytotoxicity Assessing the role of aromatic residues in the amyloid aggregation of human muscle acylphosphatase.Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences.Organism complexity anti-correlates with proteomic beta-aggregation propensity.More than meets the eye: conformational switching of a stacked dialkoxynaphthalene-naphthalenetetracarboxylic diimide (DAN-NDI) foldamer to an NDI-NDI fibril aggregate One-dimensional barrier-preserving free-energy projections of a beta-sheet miniprotein: new insights into the folding process.Intrinsically semi-disordered state and its role in induced folding and protein aggregation Self assembly of short aromatic peptides into amyloid fibrils and related nanostructures.Computational approaches to understanding protein aggregation in neurodegeneration.Prediction of amyloid aggregation in vivo.Interaction and inhibitory influence of the azo dye carmoisine on lysozyme amyloid fibrillogenesis.The cleverSuite approach for protein characterization: predictions of structural properties, solubility, chaperone requirements and RNA-binding abilities.The distribution of residues in a polypeptide sequence is a determinant of aggregation optimized by evolution.ccSOL omics: a webserver for solubility prediction of endogenous and heterologous expression in Escherichia coli Similarities in the thermodynamics and kinetics of aggregation of disease-related Abeta(1-40) peptides.Mutagenic exploration of the cross-seeding and fibrillation propensity of Alzheimer's beta-amyloid peptide variants.The roles of the conserved tyrosine in the β2-α2 loop of the prion protein.Thermodynamic analysis of the aggregation propensity of oxidized Alzheimer's beta-amyloid variants.Protein aggregation determinants from a simplified model: cooperative folders resist aggregation.Mutagenic analysis of the nucleation propensity of oxidized Alzheimer's beta-amyloid peptide.

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P2860

The role of aromaticity, exposed surface, and dipole moment in determining protein aggregation rates

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Protein Science

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The role of aromaticity, expos ...... ning protein aggregation rates

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Amedeo Caflisch

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Andrea Cavalli

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Riccardo Pellarin

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P2860

Protein misfolding, evolution and disease

Evaluation of a fast implicit solvent model for molecular dynamics simulations

Intrinsic beta-sheet propensities result from van der Waals interactions between side chains and the local backbone

Chain length dependence of apomyoglobin folding: structural evolution from misfolded sheets to native helices.

Amyloid fibrillogenesis: themes and variations.

A molecular model of Alzheimer amyloid beta-peptide fibril formation.

A possible role for pi-stacking in the self-assembly of amyloid fibrils.

Rationalization of the effects of mutations on peptide and protein aggregation rates.

Studies of the aggregation of mutant proteins in vitro provide insights into the genetics of amyloid diseases.

The role of side-chain interactions in the early steps of aggregation: Molecular dynamics simulations of an amyloid-forming peptide from the yeast prion Sup35.

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1939-1941

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10.1110/PS.04663504

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13

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Gian Gaetano Tartaglia

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2004-05-28T00:00:00Z

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8536669

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