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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
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 
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 | PXD035647 | Pride
Cell expansion Lrr-receptor kinase Signaling cross-talk Signaling specificity Domain-swap chimera 
TranscriptomicsMOYO-S and MOYO-R responsive genes to dengue-2 infection at 3hr and 18hr post-infection times
We conducted a genome-wide survey of genes in Ae. aegypti females that are transcriptionally responsive upon challenge with dengue virus (serotype-2). The array was designed with 60-mer oligos specific to 16,092 gene transcripts of gene build AaegL1.1 (www. vectorbase.org). The hybridizations were p...
ORGANISM(S): Aedes aegypti 
2011-09-30 | GSE16563 | GEO
TranscriptomicsMOYO-S and MOYO-R responsive genes to dengue-2 infection at 3hr and 18hr post-infection times
We conducted a genome-wide survey of genes in Ae. aegypti females that are transcriptionally responsive upon challenge with dengue virus (serotype-2). The array was designed with 60-mer oligos specific to 16,092 gene transcripts of gene build AaegL1.1 (www. vectorbase.org). The hybridizations were p...
ORGANISM(S): Aedes aegypti 
2011-09-29 | E-GEOD-16563 | biostudies-arrayexpress
ProteomicsProteomic analysis of salivary glands of female Aedes aegypti Linn
Aedes aegypti is a major vector for dengue, chikungunya and yellow fever. Though salivary gland plays a crucial role in transmission of virus and vector life cycle, there is no global and unbiased published report on salivary gland proteome of Ae. aegypti. In this study, we have carried out mass spe...
ORGANISM(S): Aedes aegypti aegypti 
2017-02-28 | PXD002468 | Pride
Hypothetical proteins Saliva Ltq-velos mass spectrometer 
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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