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ProteomicsAPPLE-MS: A modular affinity purification-mass spectrometry method assisted by PafA- mediated proximity labeling
While affinity purification-mass spectrometry (AP-MS) has significantly advanced protein-protein interaction (PPI) studies, its limitations in detecting weak, transient, and membrane-associated interactions remain. To address these challenges, we introduced an innovative proteomic method termed Affi...
ORGANISM(S): Homo sapiens (Human) Rattus norvegicus (Rat) 
2025-10-27 | PXD063145 | Pride
Ap-ms Proximity labeling Protein-protein interaction Interactome 
ProteomicsHe Xiang - BfrB - Systematic Identification of Mycobacterium tuberculosis Effectors Reveals that BfrB Suppresses Innate Immunity
To identify the macrophage binding partner of Mtb BfrB, we selected and purified BfrB tagged with GST, and incubated it with THP-1 lysates before performing GST Pullodwn. Then the eluted protein were examined by sliver stain. Using mass spectrometry, we identified a protein with an apparent molecula...
ORGANISM(S): Homo sapiens (Human) Mycobacterium tuberculosis 
2017-10-17 | PXD006929 | Pride
Bfrb rps3 
Proteomicsc-di-GMP affect the protein acetylation through CobB dependent deacetylation
To determine whether c-di-GMP could affect CobB-dependent deacetylation in a global setting, we applied Stable Isotope Labeling with Amino acids in Cell culture (SILAC) coupled with MS to quantitatively compare the levels of protein acetylation in WT, ΔcobB and ΔdgcZ cells.
ORGANISM(S): Escherichia coli 
2019-06-17 | PXD013292 | Pride
C-di-gmp cobb 
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 
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 
PXD026514 |
Proteomicsm6A binding proteins identified by SPIDER assay
To assess whether SPIDER could identify modified nucleic acids binding proteins within a complex environment, such as the cellular milieu, we sought to identify N6-methyladenosine (m6A) binding proteins within a total cell lysate. We performed SPIDER assay by incubating biotin-ssRNAs（with and withou...
ORGANISM(S): Homo Sapiens 
2022-11-02 | PXD026519 |
ProteomicsIntra-molecule pupylation of GFP-PupE identified by mass spectrometry
Characterization of GFP-Pup before or after pupylation assays by Thermo Exactive Plus EMR mass spectrometry coupled to Agilent 1100 HPLC system
ORGANISM(S): Mycobacterium Tuberculosis H37rv_2009 
PXD026527 |
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 |
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