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Philip E. Bourne

Researcher at University of Virginia

Publications -  357
Citations -  64294

Philip E. Bourne is an academic researcher from University of Virginia. The author has contributed to research in topics: Protein Data Bank & Structural genomics. The author has an hindex of 68, co-authored 331 publications receiving 54563 citations. Previous affiliations of Philip E. Bourne include University of Sheffield & University of California, Los Angeles.

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Book ChapterDOI

CASP and CAFASP experiments and their findings

TL;DR: This short introductory chapter is intended simply to introduce a sense of the progress, limitations, challenges, and likely future developments in the field of protein structure prediction through what seems to be a unique scientific process.
Journal ArticleDOI

Peptide Identification by Database Search of Mixture Tandem Mass Spectra

TL;DR: This work proposes a new database search tool (MixDB) that is able to identify mixture tandem mass spectra from more than one peptide, and shows that peptides can be reliably identified with up to 95% accuracy from mixture spectra.
Journal ArticleDOI

Toward effective software solutions for big biology

TL;DR: A bioinformatics manifesto is published as a practical guide for FOSS-style development that aims to provide process and architecture guidelines for early-career bioinformaticians and their supervisors.
Book ChapterDOI

The immune epitope database and analysis resource

TL;DR: The utility of the IEDB was recently demonstrated through a comprehensive analysis of all current information regarding antibody and T cell epitopes derived from influenza A and determining possible cross-reactivity among H5N1 avian flu and human flu viruses.
Journal ArticleDOI

Insights into the binding mode of MEK type-III inhibitors. A step towards discovering and designing allosteric kinase inhibitors across the human kinome

TL;DR: This work systematically studied the binding mode of MEK-targeted type-III inhibitors using structural systems pharmacology and molecular dynamics simulation, and hypothesize that the helix-folding activation loop is a hallmark allosteric binding site for type- III inhibitors.