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UnknownAccurate protein complex retrieval by affinity enrichment mass spectrometry (AE-MS) rather than affinity purification mass spectrometry (AP-MS).
Not available
S-EPMC4288248 | biostudies-literature
ProteomicsHighly accurate protein complex retrieval by affinity enrichment MS rather than affinity purification MS
Protein-protein interactions are fundamental to the understanding of biological processes. Affinity purification coupled to mass spectrometry (AP-MS) is one of the most promising methods for their investigation. Previously, complexes were purified as much as possible, frequently followed by identifi...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2015-03-26 | PXD000955 | Pride
Ap-ms Ae-ms Yeast Interaction proteomics Label-free quantification 
ProteomicsThe landscape of phospho-tyrosine mediated protein interactions of human receptor tyrosine kinases
Systematically profiling the interactome of 1,144 unique wild-type and mutant phosphotyrosine residues of receptor tyrosine kinases by affinity enrichment - mass spectrometry (AE-MS), followed by a subset of novel interactors validation by competition assay.
ORGANISM(S): Homo sapiens (Human) 
2022-10-06 | PXD015927 | Pride
Tyrosine phosphorylation Ptb domain Receptor tyrosine kinases Phosphotyrosine interacting domain Affinity enrichment-mass spectrometry Hot-spot mutation Cell signaling Protein-protein interaction Mutation‐gain tyrosine Sh2 domain Interactome 
ProteomicsAE-MS to profile SLO-human plasma protein interactome landscape; HDX-MS and XL-MS to study protein interaction and dynamics of PLG-SLO
Group A Streptococcus is known to exploit the human fibrinolysis system, particularly by targeting the plasminogen/plasmin pathway through redundant pathomechanisms. In this study, we began with affinity-enrichment mass spectrometry to map the interaction landscape between streptolysin O and human p...
ORGANISM(S): Homo sapiens (Human) Streptococcus pyogenes MGAS315 
2024-10-17 | PXD051261 | Pride
Ae-ms Human Streptolysin o Streptococcus pyogenes Xl-ms Hdx-ms Plasminogen Lc-ms/ms 
ProteomicsReceptor kinase signalling of BRI1 and SIRK1 is tightly balanced by their interactomes as revealed from domain-swap chimaera in AE-MS approaches.
Plants response to different external and internal stimulation by activation of signal transduction pathways. Receptor kinases are localized at plasma membrane and were characterized to be involved in perception of signals at the cell surface. Here we use affinity enrichment mass spectrometry acquis...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-05-06 | PXD044354 | Pride
Lrr-receptor kinase Supervised machine learning Signaling specificity Affinity enrichment mass-spectrometry (ae-ms) Domain-swap chimera 
ProteomicsIdentification of parvulin interactors by diazirine mediated cross-linking
In this project we aimed to identify the parvulin interactors by diazirine mediated cross-linking in conjunction with affinity enrichment mass spectrometry (AE-MS).
ORGANISM(S): Homo sapiens (Human) 
2025-10-27 | PXD016355 | Pride
Par14 Mass spectrometry Par17 Parvulins 
ProteomicsReceptor kinase signalling of BRI1 and SIRK1 is tightly balanced by their interactomes as revealed from domain-swap chimaera in AE-MS approaches.
Plants response to different external and internal stimulation by activation of signal transduction pathways. Receptor kinases are localized at plasma membrane and were characterized to be involved in perception of signals at the cell surface. Here we use affinity enrichment mass spectrometry acquis...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2025-05-06 | PXD035647 | Pride
Cell expansion Lrr-receptor kinase Signaling cross-talk Signaling specificity Domain-swap chimera 
ProteomicsIdentification of PWWP2A interactors using label-free quantitative affinity enrichment mass spectrometry
Chromatin structure and function is regulated by reader proteins recognizing histone modifications and/or histone variants. We recently identified PWWP2A as a binder for H2A.Z-containing nucleosomes (Pünzeler, S. et al., EMBO J 2017). Here, as part of a larger project trying to characterize PWWP2A, ...
ORGANISM(S): Homo sapiens (Human) 
2018-08-30 | PXD010202 | Pride
Ap-ms Ae-ms Mta1 Nurd Pwwp2a Interaction proteomics Histone variants Label-free quantification H2a.z 
ProteomicsIdentification of interactors of acetylated Ub
In this project we present the identification of interactors of mono-acetylated ubiquitin (Ub) variants from HEK293T whole cell extracts. Affinity enrichment coupled to high-resolution mass spectrometry followed by label-free quantification revealed the interactome of the respective mono-acetylated ...
ORGANISM(S): Homo sapiens (Human) 
2022-10-14 | PXD028797 | Pride
Acetylation Ub Interactome 
UnknownReceptor Kinase Signaling of BRI1 and SIRK1 Is Tightly Balanced by Their Interactomes as Revealed From Domain-Swap Chimaera in AE-MS Approaches.
Not available
S-EPMC11585773 | biostudies-literature
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