scispace - formally typeset
K

Kris Gevaert

Researcher at Ghent University

Publications -  476
Citations -  28249

Kris Gevaert is an academic researcher from Ghent University. The author has contributed to research in topics: Proteome & Proteomics. The author has an hindex of 83, co-authored 445 publications receiving 24088 citations. Previous affiliations of Kris Gevaert include Novo Nordisk & Flanders Institute for Biotechnology.

Papers
More filters
Journal ArticleDOI

Improved visualization of protein consensus sequences by iceLogo.

TL;DR: FASP method is described as “universal” for its ability to represent the proteome in an unbiased way, which was demonstrated by comparison to the transcriptome by demonstrating a disproportionate reduction in peptide ion current, peptide or protein identifications.
Journal ArticleDOI

Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides.

TL;DR: A diagonal method to isolate N-terminal peptides from in vivo blocked proteins based on diagonal electrophoresis and diagonal chromatography is described.
Journal ArticleDOI

PRIDE: The proteomics identifications database

TL;DR: The proteomics identifications (PRIDE) database is proposed as a means to finally turn publicly available data into publicly accessible data and offers a web‐based query interface, a user‐friendly data upload facility, and a documented application programming interface for direct computational access.
Journal ArticleDOI

Proteomics analyses reveal the evolutionary conservation and divergence of N-terminal acetyltransferases from yeast and humans

TL;DR: Although the COmbined FRActional DIagonal Chromatography technology was used to determine the N-terminal acetylation status of 742 human and yeast protein N termini, it was revealed that NatA from humans and yeast have identical or nearly identical specificities.
Journal ArticleDOI

Global Analysis of the Mitochondrial N-Proteome Identifies a Processing Peptidase Critical for Protein Stability

TL;DR: This work has identified the intermediate cleaving peptidase ICP55, which removes an amino acid from a characteristic set of MPP-generated N-termini, solving the controversial situation ofMPP specificity and suggesting that Icp55 converts instable intermediates into stable proteins.