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UnknownThe cryo-EM structure of the CENP-A nucleosome in complex with the phosphorylated CENP-C: CENP-A nucleosome in complex with phosphorylated CENP-C C-terminal domain (601-864) and CENP-N N-terminal domain (1-211)
Not available
EMPIAR-10565 | biostudies-other
UnknownThe cryo-EM structure of the CENP-A nucleosome in complex with the phosphorylated CENP-C:: CENP-A nucleosome in complex with phosphorylated CENP-C C-terminal domain(601-864)
Not available
EMPIAR-10569 | biostudies-other
UnknownThe cryo-EM structure of the CENP-A nucleosome in complex with the phosphorylated CENP-C:: CENP-A nucleosome in complex with CENP-C motif (655-675) and CENP-N N-terminal domain (1-211)
Not available
EMPIAR-10571 | biostudies-other
ProteomicsBridgin connects the outer kinetochore to centromeric chromatin
In this project, 3XFlag-tagged protein affinity purifications were performed to identify the protein-protein interactors using Cryptococcus neoformans cell lysate. After fractionation with SDS-PAGE, peptide samples for nanoLC-MS/MS were prepared by in-gel digestion. Raw data from Orbotrap Velos pr...
ORGANISM(S): Cryptococcus Neoformans 
2020-09-23 | PXD021072 | JPOST Repository
ProteomicsCRISPR-assisted RNA-protein interaction detection (CARPID) combined with quantitative mass spectrometry was used to identify proteins interacting with the long non-coding RNA (lncRNA) Taurine Up-regulated 1 (TUG1) in HEK293T cells under physiological conditions and after Camptothecin (CPT) treatment.
This project utilized CRISPR-assisted RNA-protein interaction detection (CARPID) combined with mass spectrometry to identify proteins interacting with the long non-coding RNA (lncRNA) TUG1 in HEK293T cells. TUG1 preferentially interacts with known R-loop-associated proteins, particularly under Campt...
ORGANISM(S): Homo Sapiens (human) 
2025-07-17 | PXD049137 | JPOST Repository
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