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Allan Stensballe

Researcher at Aalborg University

Publications -  161
Citations -  8408

Allan Stensballe is an academic researcher from Aalborg University. The author has contributed to research in topics: Proteome & Phosphorylation. The author has an hindex of 36, co-authored 152 publications receiving 7364 citations. Previous affiliations of Allan Stensballe include University of Southern Denmark & Technical University of Denmark.

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Journal ArticleDOI

Vesiclepedia: a compendium for extracellular vesicles with continuous community annotation

Hina Kalra, +55 more
- 18 Dec 2012 - 
TL;DR: Vesiclepedia is a community-annotated compendium of molecular data on extracellular vesicles that aims to provide a single authoritative source for information on vesicle structure and function.
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Large-scale Analysis of in Vivo Phosphorylated Membrane Proteins by Immobilized Metal Ion Affinity Chromatography and Mass Spectrometry

TL;DR: A scheme for two-dimensional peptide separation using strong anion exchange chromatography prior to IMAC that both decreases the complexity of IMAC-purified phosphopeptides and yields a far greater coverage of monophosphorylated peptides is presented.
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Phosphoproteomics of the Arabidopsis Plasma Membrane and a New Phosphorylation Site Database

TL;DR: A large-scale strategy for the isolation of phosphopeptides and identification by mass spectrometry is developed and more than 300 phosphorylation sites from Arabidopsis thaliana plasma membrane proteins are identified, revealing an unexpected complexity of regulation.
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A Mass Spectrometry-based Proteomic Approach for Identification of Serine/Threonine-phosphorylated Proteins by Enrichment with Phospho-specific Antibodies Identification of a Novel Protein, Frigg, as a Protein Kinase A Substrate

TL;DR: Several antibodies are described that recognize phosphoserine/phosphothreonine-containing proteins by Western blotting and can be used to enrich for proteins phosphorylated on serine/threonine residues by immunoprecipitation, as well.
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Characterization of phosphoproteins from electrophoretic gels by nanoscale Fe(III) affinity chromatography with off-line mass spectrometry analysis.

TL;DR: An optimized and sensitive procedure for alkaline phosphatase treatment of peptide mixtures was implemented, which in combination with nano‐scale Fe(III)‐IMAC and MALDI‐MS allowed unambiguous identification of phosphopeptides by observation of 80 Da mass shifts.