Sort   by:  
 Page size 
Protein microarray analysis of ACAP1 interacting proteins
Here we report on the identification of two previously uncharacterized proteins as CP190 interacting proteins, that we have named Ibf1 and Ibf2. These proteins localize at insulator bodies and associate with chromatin at CP190-binding sites throughout the genome. We also show that Ibf1 and Ibf2 are ...
ORGANISM(S): Drosophila melanogaster 
Piwi-interacting RNAs (piRNAs) are essential for silencing of transposable elements in the germline but their biogenesis is poorly understood. Here we demonstrate that MOV10L1, a germ cell-specific putative RNA helicase, is associated with Piwi proteins. Genetic disruption of the MOV10L1 RNA helicas...
ORGANISM(S): Mus musculus 
Analysis of DDX39A and DDX56 interacting proteins
UFBP1 (UFM1-binding and PCI domain-containing protein 1, also called DDRGK domain-containing protein 1, Dashurin, or C20orf116) is a protein that also participates in the ufmylation conjugating systems besides the E1 ubiquitin-like modifier-activating enzyme 5 (UBA5), the E2, UFM1-conjugating enzyme...
ORGANISM(S): Homo sapiens (Human) 
2018-05-08 | PXD009051 | Pride
RNA Seq of rhabdomyosarcoma cells with sgRNA targeting oncofusion interacting proteins
Chemical profiling of DNA G-quadruplex-interacting proteins in live cells
The poly(A)+ and poly(A)− fractions of interacting and non-interacting cells were used for distinct library preparation of interacting and non-interacting prokaryotic pathogen and eukaryotic host cells by deepSuperSAGE. Sequencing was performed with the Illumina HiSeq 2000 platform, and one point of...
ORGANISM(S): Salmonella enterica 
Protein Ser/Thr kinase CK2 is involved in a myriad of cellular processes including cell growth and proliferation by phosphorylating hundreds of substrates, yet the regulation process of CK2 function is poorly understood. The CK2 catalytic subunit, CK2α, is phosphorylated at Thr344 and phosphorylati...
ORGANISM(S): synthetic construct 
Through previous studies, we found that PRMT5 is regulated by phosphorylation modification and thus participates in tumor drug resistance. To further explore the mechanism of PRMT5 resistance, we screened potential PRMT5 kinases by mass spectrometry of proteins interacting with PRMT5
ORGANISM(S): Homo sapiens (Human) 
2025-02-22 | PXD058763 | Pride
Sort   by:  
 Page size