GAP: towards almost 100 percent prediction for β-strand-mediated aggregating peptides with distinct morphologies

A serendipitous survey of prediction algorithms for amyloidogenicity

(2013) Bartholomew P. Roland et al.   BIOPOLYMERS

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

(2013) A Thangakani et al.   BMC BIOINFORMATICS

Identification of a novel ‘aggregation-prone’/‘amyloidogenic determinant’ peptide in the sequence of the highly amyloidogenic human calcitonin

(2013) Vassiliki A. Iconomidou et al.   FEBS LETTERS

A Consensus Method for the Prediction of ‘Aggregation-Prone’ Peptides in Globular Proteins

(2013) Antonios C. Tsolis et al.   PLoS One

Identification of efflux proteins using efficient radial basis function networks with position-specific scoring matrices and biochemical properties

(2013) Yu-Yen Ou et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS

On the Role of Aggregation Prone Regions in Protein Evolution, Stability, and Enzymatic Catalysis: Insights from Diverse Analyses

(2013) Patrick M. Buck et al.   PLoS Computational Biology

Physicochemical Strategies for Inhibition of Amyloid Fibril Formation: An Overview of Recent Advances

(2012) R. Liu et al.   CURRENT MEDICINAL CHEMISTRY

Amyloid neuropathies

(2012) David Adams et al.   CURRENT OPINION IN NEUROLOGY

The RCSB Protein Data Bank: new resources for research and education

(2012) Peter W. Rose et al.   NUCLEIC ACIDS RESEARCH

Prediction of amyloid aggregation in vivo

(2011) Mattia Belli et al.   EMBO REPORTS

Journal of Neurochemistry special issue on Alzheimer’s disease: ‘amyloid cascade hypothesis - 20 years on’

(2011) Frédéric Checler et al.   JOURNAL OF NEUROCHEMISTRY

Aggregation in Protein-Based Biotherapeutics: Computational Studies and Tools to Identify Aggregation-Prone Regions

(2011) Neeraj J. Agrawal et al.   JOURNAL OF PHARMACEUTICAL SCIENCES

Nanomechanics of functional and pathological amyloid materials

(2011) Tuomas P. J. Knowles et al.   Nature Nanotechnology

How do thermophilic proteins resist aggregation?

(2011) Anthony Mary Thangakani et al.   PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS

Exploring the sequence determinants of amyloid structure using position-specific scoring matrices

(2010) Sebastian Maurer-Stroh et al.   NATURE METHODS

Amyloids: Not Only Pathological Agents but Also Ordered Nanomaterials

(2008) Izhack Cherny et al.   ANGEWANDTE CHEMIE-INTERNATIONAL EDITION

ROC analysis: applications to the classification of biological sequences and 3D structures

(2008) P. Sonego et al.   BRIEFINGS IN BIOINFORMATICS