scispace - formally typeset
B

Bart Hoorelbeke

Researcher at Ghent University

Publications -  8
Citations -  937

Bart Hoorelbeke is an academic researcher from Ghent University. The author has contributed to research in topics: Proteome & Chlamydophila pneumoniae. The author has an hindex of 6, co-authored 8 publications receiving 918 citations.

Papers
More filters
Journal ArticleDOI

Endonuclease G: a mitochondrial protein released in apoptosis and involved in caspase-independent DNA degradation

TL;DR: The ability of truncated Bid (tBid) to induce the release of a DNAse activity from mitochondria during apoptosis was confirmed in the liver from mice injected with agonistic anti-Fas antibody and is completely prevented in Bcl-2 transgenic mice.
Journal ArticleDOI

Chromatographic Isolation of Methionine-containing Peptides for Gel-free Proteome Analysis Identification Of More Than 800 Escherichia Coli Proteins

TL;DR: A novel gel-free proteomic technology was used to identify more than 800 proteins from 50 million Escherichia coli K12 cells in a single analysis, demonstrating the high dynamic range and the flexibility in the peptide sorting chemistry.
Journal ArticleDOI

Proteome analysis of the Chlamydia pneumoniae elementary body.

TL;DR: Proteome maps and a table of all identified proteins have been made available on the world wide web at www.gram.dk.au.
Journal ArticleDOI

Protein identification based on matrix assisted laser desorption/ionization‐post source decay‐mass spectrometry

TL;DR: The combination of peptide mass fingerprinting and PSD and analysis described here generally leads to unambiguous protein identification in the amount of material range generally encountered in most proteome studies.
Journal ArticleDOI

A matrix-assisted laser desorption ionization post-source decay (MALDI-PSD) analysis of proteins released from isolated liver mitochondria treated with recombinant truncated Bid.

TL;DR: It is demonstrated that a physiologically relevant concentration of tBid is sufficient to induce release of particular intermembrane mitochondrial proteins belonging to a broad molecular-mass range.