MILAMP: Multiple Instance Prediction of Amyloid Proteins
- 22 August 2019
- journal article
- research article
- Published by Institute of Electrical and Electronics Engineers (IEEE) in IEEE/ACM Transactions on Computational Biology and Bioinformatics
- Vol. 18 (3) , 1142-1150
Abstract
Amyloid proteins are implicated in several diseases such as Parkinson's, Alzheimer's, prion diseases, etc. In order to characterize the amyloidogenicity of a given protein, it is important to locate the amyloid forming hotspot regions within the protein as well as to analyze the effects of mutations on these proteins. The biochemical and biological assays used for this purpose can be facilitated by computational means. This paper presents a machine learning method that can predict hotspot amyloidogenic regions within proteins and characterize changes in their amyloidogenicity due to point mutations. The proposed method called MILAMP (Multiple Instance Learning of AMyloid Proteins) achieves high accuracy for identification of amyloid proteins, hotspot localization and prediction of mutation effects on amyloidogenicity by integrating heterogenous data sources and exploiting common predictive patterns across these tasks through multiple instance learning. The paper presents comprehensive benchmarking experiments to test the predictive performance of MILAMP in comparison to previously published state of the art techniques for amyloid prediction. The python code for the implementation and webserver for MILAMP is available at the URL: http://faculty.pieas.edu.pk/fayyaz/software.html#MILAMP.Keywords
Funding Information
- IT and Telecom Endowment Fund
- Higher Education Commission Pakistan (5000 Indigenous Scholarship Program)
This publication has 41 references indexed in Scilit:
- A Consensus Method for the Prediction of ‘Aggregation-Prone’ Peptides in Globular ProteinsPLOS ONE, 2013
- SNPeffect 4.0: on-line prediction of molecular and structural effects of protein-coding variantsNucleic Acids Research, 2011
- Prediction of amyloid aggregation in vivoEMBO Reports, 2011
- Amyloidogenic sequences in native protein structuresProtein Science, 2009
- Amyloidogenic determinants are usually not buriedBMC Structural Biology, 2009
- The Zyggregator method for predicting protein aggregation propensitiesChemical Society Reviews, 2008
- AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptidesBMC Bioinformatics, 2007
- Prediction of sequence-dependent and mutational effects on the aggregation of peptides and proteinsNature Biotechnology, 2004
- Protein aggregation and neurodegenerative diseaseNature Medicine, 2004
- Cryo‐electron microscopy structure of an SH3 amyloid fibril and model of the molecular packingThe EMBO Journal, 1999