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ProteomicsLFQbench enables a multi-centered benchmark study demonstrating robust proteomic label-free quantification
The consistent and accurate quantification of proteins is a challenging task for mass spectrometry (MS)-based proteomics. SWATH-MS uses data-independent acquisition (DIA) for label-free quantification. Here we evaluated five software tools for processing SWATH-MS data: OpenSWATH, SWATH2.0, Skyline, ...
ORGANISM(S): Escherichia Coli (ncbitaxon:562) Homo Sapiens (ncbitaxon:9606) Saccharomyces Cerevisiae (ncbitaxon:4932) 
2017-04-27 | MSV000081024 | MassIVE
UnknownIn-depth mass spectrometric mapping of the human vitreous proteome.
Not available
S-EPMC3689628 | biostudies-literature
ProteomicsSpatiotemporal proximity labeling tools to track GlcNAc-modified functional protein hubs during cellular signaling
A fundamental mechanism that all eukaryotic cells use to adapt to their environment is dynamic protein modification with monosaccharide sugars. In humans, O-linked N-acetylglucosamine (O-GlcNAc) is rapidly added and removed on diverse protein sites as a response to fluctuating nutrient levels, stres...
ORGANISM(S): Homo sapiens (Human) 
2022-10-15 | PXD033026 | Pride
Glycosylation Insulin signaling Proximity labeling Nucleocytoplasmic O-glcnac 
ProteomicsSpatiotemporal proximity labeling tools to track GlcNAc-modified functional protein hubs during cellular signaling
A fundamental mechanism that all eukaryotic cells use to adapt to their environment is dynamic protein modification with monosaccharide sugars. In humans, O-linked N-acetylglucosamine (O-GlcNAc) is rapidly added and removed on diverse protein sites as a response to fluctuating nutrient levels, stres...
ORGANISM(S): Homo sapiens (Human) 
2022-10-15 | PXD033062 | Pride
Glycosylation Insulin signaling Proximity labeling Nucleocytoplasmic O-glcnac 
ProteomicsSpatiotemporal proximity labeling tools to track GlcNAc-modified functional protein hubs during cellular signaling
A fundamental mechanism that all eukaryotic cells use to adapt to their environment is dynamic protein modification with monosaccharide sugars. In humans, O-linked N-acetylglucosamine (O-GlcNAc) is rapidly added and removed on diverse protein sites as a response to fluctuating nutrient levels, stres...
ORGANISM(S): Homo sapiens (Human) 
2022-10-15 | PXD033063 | Pride
Glycosylation Insulin signaling Proximity labeling Nucleocytoplasmic O-glcnac 
ProteomicsSpatiotemporal proximity labeling tools to track GlcNAc-modified functional protein hubs during cellular signaling
A fundamental mechanism that all eukaryotic cells use to adapt to their environment is dynamic protein modification with monosaccharide sugars. In humans, O-linked N-acetylglucosamine (O-GlcNAc) is rapidly added and removed on diverse protein sites as a response to fluctuating nutrient levels, stres...
ORGANISM(S): Homo sapiens (Human) 
2022-10-15 | PXD033066 | Pride
Glycosylation Insulin signaling Proximity labeling Nucleocytoplasmic O-glcnac 
ProteomicsSpatiotemporal proximity labeling tools to track GlcNAc-modified functional protein hubs during cellular signaling
A fundamental mechanism that all eukaryotic cells use to adapt to their environment is dynamic protein modification with monosaccharide sugars. In humans, O-linked N-acetylglucosamine (O-GlcNAc) is rapidly added and removed on diverse protein sites as a response to fluctuating nutrient levels, stres...
ORGANISM(S): Homo sapiens (Human) 
2022-10-15 | PXD033043 | Pride
Glycosylation Insulin signaling Proximity labeling Nucleocytoplasmic O-glcnac 
ProteomicsSpatiotemporal proximity labeling tools to track GlcNAc-modified functional protein hubs during cellular signaling
A fundamental mechanism that all eukaryotic cells use to adapt to their environment is dynamic protein modification with monosaccharide sugars. In humans, O-linked N-acetylglucosamine (O-GlcNAc) is rapidly added and removed on diverse protein sites as a response to fluctuating nutrient levels, stres...
ORGANISM(S): Homo sapiens (Human) 
2022-10-15 | PXD033044 | Pride
Glycosylation Insulin signaling Proximity labeling Nucleocytoplasmic O-glcnac 
TranscriptomicsA proteomic view on the cell biology of Staphylococcus aureus proteome
The genome sequence is the “blue-print of life”, but proteomics is required to relate this blue-print of life to the actual physiology of living cells. Because of their low complexity – only about 2.000 proteins make a Staphylococcus aureus cell viable – bacteria are excellent model systems to ident...
ORGANISM(S): Staphylococcus aureus 
2009-11-11 | E-GEOD-15060 | biostudies-arrayexpress
UnknownA Cross-Linking-Aided Immunoprecipitation/Mass Spectrometry Workflow Reveals Extensive Intracellular Trafficking in Time-Resolved, Signal-Dependent Epidermal Growth Factor Receptor Proteome.
Not available
S-EPMC7532284 | biostudies-literature
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