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TranscriptomicsValidation experiment of copy number variations identified by next-generation sequencing in chickens (part 1)
Copy number variation (CNV) is important and widespread in the genome, and is a major cause of disease and phenotypic diversity. Herein, we perform a genome-wide analysis of CNVs in the 12 diversified chicken genomes based on next-generation sequencing. We apply aCGH experiments to confirm our predi...
ORGANISM(S): Gallus gallus 
2015-05-14 | E-GEOD-54117 | biostudies-arrayexpress
TranscriptomicsValidation experiment of copy number variations identified by next-generation sequencing in chickens (part 2)
Copy number variation (CNV) is important and widespread in the genome, and is a major cause of disease and phenotypic diversity. Herein, we perform a genome-wide analysis of CNVs in the 12 diversified chicken genomes based on next-generation sequencing. We apply aCGH experiments to confirm our predi...
ORGANISM(S): Gallus gallus 
2015-05-14 | E-GEOD-54118 | biostudies-arrayexpress
ProteomicsPancreatic cancer-associated proteome sequencing
In this study, 30 pancreatic tissues were retrieved, including 20 samples of pancreatic ductal cell carcinoma and 10 of adjacent healthy tissues. All pancreatic samples were obtained from the First Hospital of Lanzhou University from January 2016 to December 2020.
ORGANISM(S): Homo Sapiens 
PXD044500 |
Proteomicsm6A binding proteins identidified by RNA pull down.
Biotinyted nucleic acid probe assay for protein-m6A interaction
ORGANISM(S): Escherichia Coli 
2022-11-02 | PXD037881 |
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 |
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 |
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 |
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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