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ProteomicsDELTEX2 C-terminal domain recruits ADP-ribosylated DNA damage repair proteins for ubiquitination.
Crosstalk between ubiquitination and ADP-ribosylation regulates spatio-temporal recruitment of key players during DNA damage repair (DDR). The Deltex family of ubiquitin ligases (DTX1–4 and DTX3L), are characterized by a RING domain followed by a C-terminal domain (DTC) of unknown function; four Del...
ORGANISM(S): Homo sapiens (Human) 
2021-09-09 | PXD017807 | Pride
Par-binding domain Deltex c-terminal domain Parylation-dependent ubiquitination Dtx Dna damage 
TranscriptomicsStructural basis of YTH domain as m6A reader
The N6-methyladenosine (m6A) is the most abundant internal modification in almost all eukaryotic messenger RNAs, and is dynamically regulated. Therefore, identification of m6A readers is especially important in determining the cellular function of m6A. YTHDF2 has recently been characterized as the f...
ORGANISM(S): Homo sapiens 
2014-09-18 | E-GEOD-58352 | biostudies-arrayexpress
UnknownPar-4 secretion: stoichiometry of 3-arylquinoline binding to vimentin.
Not available
S-EPMC4681656 | biostudies-literature
TranscriptomicsTranscriptome-wide identification of RNA-binding protein and microRNA target sites by PAR-CLIP: QKI data
To assess whether the transcripts identified by PAR-CLIP are regulated by the RNA-binding protein (RBP) Quaking (QKI), we analyzed the mRNA levels of mock-transfected and QKI-specific siRNA-transfected cells with microarrays. Transcripts crosslinked to QKI were significantly upregulated upon siRNA t...
ORGANISM(S): Homo sapiens 
2010-05-27 | E-GEOD-21574 | biostudies-arrayexpress
UnknownBinding of Crumbs to the Par-6 CRIB-PDZ Module Is Regulated by Cdc42.
Not available
S-EPMC5433836 | biostudies-literature
TranscriptomicsMixture models and wavelet transforms reveal high confidence RNA-protein interaction sites in MOV10 PAR-CLIP data
The Photo-Activatable Ribonucleoside-enhanced CrossLinking and ImmunoPrecipitation (PAR-CLIP) method was recently developed for global identification of RNAs interacting with proteins. The strength of this versatile method results from induction of specific T to C transitions at sites of interaction...
ORGANISM(S): Homo sapiens 
2012-08-07 | E-GEOD-37524 | biostudies-arrayexpress
UnknownA Conserved PDZ-Binding Motif in aPKC Interacts with Par-3 and Mediates Cortical Polarity.
Not available
S-EPMC7104911 | biostudies-literature
UnknownOptimized PAR-2 RING dimerization mediates cooperative and selective membrane binding for robust cell polarity.
Not available
S-EPMC11294563 | biostudies-literature
OtherIdentification of PARP1-RNA binding in-vivo using PAR-CLiP Sequencing
Recent studies have implicated PARP1 in alternative splicing regulation. In addition, PARP1 has been shown to bind RNA in vivo suggesting that it is an RNA-binding protein (RBP). However, a detailed knowledge of the RNA-targets as well as the RNA binding region of PARP1 is unknown. We used Photoacti...
ORGANISM(S): Homo sapiens 
2018-02-14 | GSE95360 | GEO
GenomicsEpigenetic Repogramming by an Environmental Carcinogen Through Chromatin Domain Disruption
Histone modifications associated with gene silencing typically mark large contiguous regions of the genome forming repressive chromatin domain structures. Since the repressive domains exist in close proximity to active regions, maintenance of domain structure is critically important. This study show...
ORGANISM(S): Homo sapiens 
2014-09-24 | E-GEOD-56053 | biostudies-arrayexpress
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