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The data thus identify CHIP as a ubiquitin ligase essential for DALIS formation.
Thus, our results identify CHIP as an E3 ubiquitin ligase of α-syn and suggest a novel function for BAG5 as a modulator of CHIP E3 ubiquitin ligase activity with implications for CHIP-mediated regulation of α-syn oligomerization.
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To identify ChIP-Seq peaks, we used the MACS version 1.4.0 beta (Model based Analysis of ChIP-Seq) peak finding algorithm by using a p value threshold of enrichment of 1e-5 as a cut-off.
CENH3-binding domains were identified by comparing the ChIPed and input data using SICER (Zang et al. 2009), which is designed to identify ChIP-enriched signals that tend to form specific subdomains.
Replicate ChIP-seq experiments were merged in MM-ChIP, which estimates sample-specific shift-size of ChIP-seq tags with MACS modeling and then pools shifted tags from different samples to identify ChIP-peaks with a dynamic Poisson model [ 23].
Moreover, we identified CHIP (Carboxy terminus of Hsp70-Interacting Protein) as the E3 ligase that ubiquitinated HIF-1α in the presence of MGO.
Moreover, we have identified CHIP as the ubiquitin ligase that promotes proteasomal degradation of HIF-1α in the presence of MGO.
We identified CHIP (Carboxyl terminus of the Hsc70-Interacting Protein) as the ubiquitin ligase that targets HIF-1α for degradation in the presence of MGO, by a mechanism that requires prior recruitment of the molecular chaperones Hsp40 and Hsp70.
Our study identified CHIP as an E3 ligase for EndoG.
Although the GRE of Nctp has not been identified, ChIP shows GR occupancy at the proximal promoter of Nctp gene [ 79].
To analyze the positional distribution of FOXP3 TFBS in reference to the TSS in more detail, we annotated the identified ChIP regions with the Genomic Position Annotation Tool (GPAT) [ 18].
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