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ProteomicsC-Man peptide pulldowns from Brain
Peptide pulldowns with C-man antibodies to demostrate the utelity of reagents for proteomic analysis. Using Murine brain samples Novel C-man sites are readily identifiable.
ORGANISM(S): Mus musculus (Mouse) 
2020-11-16 | PXD020336 | Pride
C-man Affinity pulldowns Glycopeptides 
ProteomicsBANC-seq to identify genome-wide transcription factor binding affinities to native chromatin
BANC-seq (Binding Affinities to Native Chromatin by sequencing) allows determination of absolute apparent binding affinites of transcription factors to native chromatin in a genome-wide manner. In this study, we establish the method and show that chromatin and DNA sequence define binding affinites o...
ORGANISM(S): Homo sapiens (Human) Mus musculus (Mouse) 
2023-02-09 | PXD038502 | Pride
Dna pulldowns Transcription factors Tmt Proteomes Binding affinity Absolute quantification 
ProteomicsSvf1-GFP pulldowns from Limar et al. 2023 JCB
Svf1-GFP pulldowns compared to untegged WT cells from SILAC labelled yeast cells. See Limar et al. 2023 JCB
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2023-03-06 | PXD039395 | Pride
Svf1-gfp pulldowns from yeast svf1 
GenomicsReciprocal interactions of human C10orf12 and C17orf96 with PRC2 revealed by BioTAP-XL crosslinking and affinity purification
Short-read sequencing of DNA fractions of the BioTAP-XL pull-downs on human EZH2 and interacting proteins. ChIP-seq-like pulldown/input samples
ORGANISM(S): Homo sapiens 
2014-02-01 | E-GEOD-53495 | biostudies-arrayexpress
ProteomicsEvaluation of peptide pulldown coupled to mass spectrometry approaches for investigation of motif-based protein-protein interactions
Eight different, SLiM-containing peptides were tested for pulldowns immobilized on magnetic beads, and the same sequences were used for PRISMA experiments. Double repeat of peptides were also used for higher local concentration of the motifs.
ORGANISM(S): Homo sapiens (Human) 
2023-03-07 | PXD037380 | Pride
Ap-ms Prisma Pulldown Slim Protein-protein interaction 
ProteomicsHigh Efficiency Enrichment by Saturating Nanoliters of Protein Affinity Media
Affinity-purification mass-spectrometry (AP-MS) is an established technique for identifying protein-protein interactions (PPIs). The basic technology involves immobilizing a high-specificity ligand to a solid phase support (e.g., an agarose or magnetic bead) to pull down protein(s) of interest from ...
ORGANISM(S): Homo sapiens (Human) Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus) 
2023-09-05 | PXD042936 | Pride
Bioid Magnetic beads Enrichment efficiency Affinity purification 
ProteomicsLimited-proteolysis coupled to mass spectrometry (LiP-MS) data on a serially filtered yeast lysate (the FLiP library) and on lysates of wild-type and Gcn5 mutant yeast strains grown under hydroxyurea stress and control conditions. Affinity purification mass spectrometry on Ada3 pulldowns from yeast grown under hydroxyurea stress and control conditions.
We applied serial ultrafiltration and limited proteolysis-coupled mass spectrometry (LiP-MS) to generate an atlas of peptides that act as markers for the formation or dissolution of protein-protein interactions (PPIs). Applied to Saccharomyces cerevisiae, the approach yielded 6,441 candidate PPI mar...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2024-10-17 | PXD055566 | Pride
Ap-ms Flip-ms Hydroxyurea Ada3 Lip-ms 
ProteomicsDetermining DNA-protein binding affinities and specificities from crude lysates using a combined SILAC/TMT labeling strategy
Gene expression is driven by the binding of transcription factors to regulatory elements in the genome, such as enhancers and promoters. A powerful technique to study DNA-protein interactions is affinity purification followed by mass spectrometry. Classic affinity purifications coupled to quantitati...
ORGANISM(S): Homo sapiens (Human) 
2023-10-08 | PXD041674 | Pride
Tmt Silac Dna pulldowns Paqman 
UnknownHigh-Efficiency Enrichment by Saturating Nanoliters of Protein Affinity Media.
Not available
S-EPMC11234515 | biostudies-literature
ProteomicsTeamwork of clustered low affinity κB sites and accessory factors regulates transcriptional strength of NF-κB RelA dimers
Non-consensus binding sites of transcription factors are often observed within the promoters and enhancers of various genes; however, their effect on transcriptional strength is unclear. Within the promoters and enhancers of NF-κB-responsive genes, we identified clusters of non- consensus κB DNA sit...
ORGANISM(S): Mus musculus (Mouse) 
2025-10-13 | PXD065004 | Pride
Transcription Cofactor Promoter Κb dna Nf-kappa b (nf-κb) 
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