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Article
Open AccessDIP-MS: ultra-deep interaction proteomics for the deconvolution of protein complexes
Most proteins are organized in macromolecular assemblies, which represent key functional units regulating and catalyzing most cellular processes. Affinity purification of the protein of interest combined with ...
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Article
Open AccessExogenous human α-Synuclein acts in vitro as a mild platelet antiaggregant inhibiting α-thrombin-induced platelet activation
α-Synuclein (αSyn) is a small disordered protein, highly conserved in vertebrates and involved in the pathogenesis of Parkinson’s disease (PD). Indeed, αSyn amyloid aggregates are present in the brain of patie...
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Article
PCprophet: a framework for protein complex prediction and differential analysis using proteomic data
Despite the availability of methods for analyzing protein complexes, systematic analysis of complexes under multiple conditions remains challenging. Approaches based on biochemical fractionation of intact, nat...
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Article
Open AccessMap** specificity, cleavage entropy, allosteric changes and substrates of blood proteases in a high-throughput screen
Proteases are among the largest protein families and critical regulators of biochemical processes like apoptosis and blood coagulation. Knowledge of proteases has been expanded by the development of proteomic ...
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Protocol
System-Wide Profiling of Protein Complexes Via Size Exclusion Chromatography–Mass Spectrometry (SEC–MS)
In living cells, most proteins are organized in stable or transient functional assemblies, protein complexes, which control a multitude of vital cellular processes such as cell cycle progression, metabolism, a...
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Article
Open AccessMulti-layered proteomic analyses decode compositional and functional effects of cancer mutations on kinase complexes
Rapidly increasing availability of genomic data and ensuing identification of disease associated mutations allows for an unbiased insight into genetic drivers of disease development. However, determination of ...
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Article
Open AccessASPP proteins discriminate between PP1 catalytic subunits through their SH3 domain and the PP1 C-tail
Serine/threonine phosphatases such as PP1 lack substrate specificity and associate with a large array of targeting subunits to achieve the requisite selectivity. The tumour suppressor ASPP (apoptosis-stimulati...
