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MetabolomicsDNA nanomachines reveal an adaptive energy mode in confinement-induced amoeboid migration powered by polarized mitochondrial distribution

Energy metabolism is highly interdependent with adaptive cell migration in vivo. Mechanical confinement is a critical physical cue that induces switchable migration modes of the mesenchymal-to-amoeboid transition (MAT). However, the energy states in distinct migration modes, especially a...

2024-03-25 | MTBLS9657 | MetaboLights
GenomicsGenome-Wide Association Studies in Upper Gastrointestinal Cancers (Asian)

This project aims to conduct genome-wide association studies (GWAS) in two anatomically different upper gastrointestinal (UGI) cancer sites in two populations with distinctly different disease rates and genetic profiles. One population has very high rates for both esophageal squamous cel...

phs000361.v1.p1 | EGA
ProteomicsThe silk gland proteome of Stenopsyche angustata provides insights into the underwater silk secretion
Caddisworms (Trichoptera) spin adhesive silks to construct a variety of underwater composite structures. Many studies have focused on the fibroin heavy chain of caddisworm silk and found that it contains heavy phosphorylation to maintain a stable secondary structure. Besides fibroins, recent studies...
ORGANISM(S): Stenopsyche Angustata 
PXD042275 |
ProteomicsGel-based LC-MSMS, the interactome of XAF1 in 293T cells
We utilized mass spectrometry to analyze the interacting proteins of XAF1 in 293T cells.
ORGANISM(S): Homo Sapiens 
2023-03-22 | PXD041021 |
ProteomicsmRNA-protein interactome of THP-1 cells
To investigate the effectiveness of SPIDER identifying the mRNA interactome, we carried out the SPIDER assay by incubating biotin-oligo(dT) or biotin control directly with cell lysates of THP-1 cells
ORGANISM(S): Homo Sapiens 
PXD026521 |
ProteomicsLenalidomide binding proteins identified by SPIDER assay
To assess whether SPIDER could capture protein-small molecule interaction in a complex environment, here we carried out the SPIDER assay by incubating biotin-Lenalidomide or a biotin control with HEK293T total lysate, followed by the use of biotin conjugated beads coupled with mass spectrometry to i...
ORGANISM(S): Homo Sapiens 
PXD026523 |
ProteomicsMass spectrometry to exam noval receptors of the The Omicron Variant of SARS-CoV-2 RBD captured by SPIDER
We used SPIDER to examine the cell-surface receptors for specific ligands while these receptors were in their native membranes within intact cells in culture. Here we coupled the SPIDER assay with biotinylated RBD of the Omicron Variant of SARS-CoV-2 and biotinylated RBD of SARS-CoV-2. Then we perfo...
ORGANISM(S): Homo Sapiens Chlorocebus Sabaeus 
2022-01-18 | PXD031035 |
ProteomicsCheA pupylation sites identified by SPIDER assay
We used CheAs and biotin-CheZ to validate the efficiency of SPIDER capturing protein-protein interaction. Pupylation sites on WT CheAs after SPIDER assay was identified by LC-MS/MS analysis, by searching for an additional mass of ~243 Da, which represents the three C-terminal residues of Pup, i. e.,...
ORGANISM(S): Escherichia Coli 
PXD026509 |
ProteomicsCobB interacting proteins identified by SPIDER assay
To assess whether SPIDER could detect transient interactions such as enzymes and their substrates, we examined the interactome of the E. coli protein deacetylase CobB. As the only member of the Sir2 family of deacetylases in E. coli, CobB is known to play a role in many different pathways but their ...
ORGANISM(S): Escherichia Coli 
PXD026514 |
ProteomicsSide-by-side comparison of AP-MS, Tri-functional affinity probe, BioID, PUP-IT and SPIDER to identify CheZ-interacting proteins
Comparison of CheZ interactors’ ratio of two replicate experiments using five different methods, i.e., Affinity-Purification, Tri-functional affinity probe Sulfo-SBED and proximity labeling methods BioID, SPIDER, PUP-IT
ORGANISM(S): Escherichia Coli 
2022-11-03 | PXD037952 |
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