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UnknownOsteopontin knockdown suppresses the growth and angiogenesis of colon cancer cells.
Not available
S-EPMC4130851 | biostudies-literature
TranscriptomicsReal-time quantitative PCR analysis of microRNAs in human PBMC samples
A significant percentage of HIV-infected individuals experience a sharp decline in CD4+ T cell counts and progress to AIDS quickly after primary infection. Identification of biomarkers distinguishing rapid progressors (RPs) versus chronic progressors (CPs) is critical for early clinical intervention...
ORGANISM(S): Homo sapiens 
2013-05-01 | E-GEOD-44332 | biostudies-arrayexpress
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
GenomicsGenome wide association study of leprosy in Chinese population

Leprosy is a chronic infectious disease caused by Mycobacterium leprae (M. leprae). Due to M. leprae's narrow host range and an inability to be cultured in vitro, the biological investigation of this disease has been difficult. Host genetic factors have been ...

phs000217.v1.p1 | EGA
ProteomicsProteomic analysis hippocampus in TLE rats
iTRAQ coupled with LC-MS/MS was applied for proteomic analysis of hippocampus.
ORGANISM(S): Rattus Norvegicus 
2022-04-27 | PXD033481 |
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 |
ProteomicsPupylation sites on protein GFP-PupE
Characterization of GFP-Pup after Pupylation assays by mass spectrometry.
ORGANISM(S): Mycobacterium Tuberculosis H37rv_2009 
2021-06-04 | PXD026478 |
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 
2021-06-04 | PXD026514 |
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 
2021-06-04 | PXD026509 |
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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