Sort   by:  
 Page size 
MetabolomicsGolgi-IP, a tool for multimodal analysis of Golgi molecular content
The Golgi is a membrane-bound organelle that is essential for protein and lipid biosynthesis. It represents a central trafficking hub that sorts proteins and lipids to various destinations or for secretion from the cell. The Golgi has emerged as a docking platform for cellular signaling pathways inc...
2023-06-27 | MTBLS6511 | MetaboLights
MetabolomicsInositol triphosphate-triggered calcium release blocks lipid exchange at endoplasmic reticulum-Golgi contact sites
Vesicular traffic and membrane contact sites between organelles enable the exchange of proteins, lipids, and metabolites. Recruitment of membrane tethers to contact sites between the endoplasmic reticulum (ER) and the plasma membrane is often triggered by calcium. In contrast, we reveal here a funct...
2021-05-06 | MTBLS2444 | MetaboLights
ProteomicsTrans-Golgi protein TVP23B regulates host-microbe interactions via Paneth cell homeostasis and Goblet cell glycosylation
A key feature in intestinal immunity is the dynamic intestinal barrier, which separates the host from resident and pathogenic microbiota through a mucus gel impregnated with antimicrobial peptides. The mechanisms underlying the maintenance and function of this intestinal barrier are not completely ...
ORGANISM(S): Mus Musculus (ncbitaxon:10090) 
2022-12-12 | MSV000090883 | MassIVE
GenomicsDe novo Golgi biogenesis requires orchestrated transactivation of Golgi genes
De novo Golgi biogenesis requires orchestrated transactivation of Golgi genes
PRJNA1217352 | ENA
ProteomicsDissecting the secretory pathway with electrophoresis reveals intra-Golgi trafficking pathways and enables compilation of sub-Golgi and sub-ER proteomes.
The Golgi is the hub of the eukaryotic secretory pathway, trafficking proteins and lipids, as well as synthesizing complex sugars. Different biosynthetic reactions are associated with different compartments of its complex architecture. Although pre- and post-Golgi trafficking has been much studied...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) 
2019-09-11 | PXD004596 | Pride
Arabidopsis Free flow electrophoresis Proteomics Trans-membrane span Secretory pathway Polysaccharide Endoplasmic reticulum Trafficking Golgi Cisternae Immunogold 
ProteomicsGolgi-IP, a novel tool for multimodal analysis of Golgi molecular content
The Golgi plays an essential role in protein and lipid glycosylation. Golgi dysfunction is associated with a variety of diseases including cancer, neurodegeneration and cardiovascular disease. We developed a powerful immunoprecipitation technique to isolate the Golgi by tagging TMEM115. Golgi-immuno...
ORGANISM(S): Homo sapiens (Human) 
2023-04-24 | PXD038046 | Pride
Golgi-ip Proteomics Metabolomics Lipidomics Golgi apparatus 
ProteomicsMaize and Arabidopsis Golgi proteome
Comparative proteomics of ER-Golgi membranes from etiolated coleoptiles of maize (Zea mays) and young leaves of Arabidopsis (Arabidopsis thaliana) isolated by flotation centrifugation demonstrate differences in the complement of synthases and glycosyl transferases unique to the type of wall made. Ad...
ORGANISM(S): Arabidopsis thaliana (Mouse-ear cress) Zea mays (Maize) 
2019-04-11 | PXD007612 | Pride
Flotation centrifugation Lc-msms Golgi Triple tof Arabidopsis Maize Ffe Free-flow electrophoresis 
ProteomicsCOG complex-dependent Golgi-derived vesicles from hTERT-RPE1 cells EXP1
Intracellular trafficking relies on small vesicular intermediates, though their specific role in Golgi function is still debated. To clarify this, we induced acute dysfunction of the Conserved Oligomeric Golgi (COG) complex and analyzed vesicles from cis, medial, and trans-Golgi compartments. Proteo...
ORGANISM(S): Homo sapiens (Human) 
2026-08-31 | PXD057633 | Pride
Glycosylation Golgi Vesicle Cog complex Immunoprecipitation Human 
TranscriptomicsTranscription profiling of yeast expressing mouse major histocompatibility complex class I heavy chain H-2K(b)
To dissect the requirements of membrane protein degradation from the ER, we expressed the mouse major histocompatibility complex class I heavy chain H-2K(b) in yeast. Like other proteins degraded from the ER, unassembled H-2K(b) heavy chains are not transported to the Golgi but are degraded in a pro...
ORGANISM(S): Saccharomyces cerevisiae 
2005-06-28 | E-SMDB-1576 | biostudies-arrayexpress
TranscriptomicsUnfolded Protein Response
To dissect the requirements of membrane protein degradation from the ER, we expressed the mouse major histocompatibility complex class I heavy chain H-2K(b) in yeast. Like other proteins degraded from the ER, unassembled H-2K(b) heavy chains are not transported to the Golgi but are degraded in a pro...
ORGANISM(S): Saccharomyces cerevisiae 
2005-08-16 | E-GEOD-3130 | biostudies-arrayexpress
Sort   by:  
 Page size