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ProteomicsSex-specific proteomic profiles and complement-C3-microglial axis drive depressive symptoms in Parkinson’s disease
In this study, hippocampal and cortical tissues were collected from mice and divided into four experimental groups: control (Con), traumatic brain injury (TBI), control with hydrogen sulfide treatment (Con + H₂S), and TBI with hydrogen sulfide treatment (TBI + H₂S). Each group included three biologi...
ORGANISM(S): Homo Sapiens 
PXD076542 |
ProteomicsSubcommissural organ (SCO) contributes to brain development via SCO-secreted peptides
To explore the role of SCO and its functional mechanism, we measure the SCO-derived peptide in CSF from C57B/6 mice and SCO-ablated mice.
ORGANISM(S): Mus Musculus 
2025-02-04 | PXD040641 |
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 |
ProteomicsPupylation sites on protein GFP-PupE
Characterization of GFP-Pup after Pupylation assays by mass spectrometry.
ORGANISM(S): Mycobacterium Tuberculosis H37rv_2009 
PXD026478 |
ProteomicsPupylation sites on SARS-CoV-2 N
As a test for the effectiveness of SPIDER with RNA-protein pairs, we examined SARS-CoV-2 Nucleoprotein. We used Nucleoprotein and specific biotin-RNA to validate the efficiency of spider capturing N and analysised the pupylation sites of N protein by mass spectrometry
ORGANISM(S): Severe Acute Respiratory Syndrome Coronavirus 2 
PXD026518 |
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