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Small molecule inhibitor of PRC1 E3 ligase activity induces differentiation of leukemia initiating cells

ABSTRACT: Small molecule inhibitor of PRC1 E3 ligase activity induces differentiation of leukemia initiating cells

PROVIDER: PRJNA510342 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR8291390.fastq.gz	Fastqsanger.gz
	SRR8291391.fastq.gz	Fastqsanger.gz
	SRR8291392.fastq.gz	Fastqsanger.gz
	SRR8291393.fastq.gz	Fastqsanger.gz
	SRR8291394.fastq.gz	Fastqsanger.gz

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Small molecule inhibitor of PRC1 E3 ligase activity induces differentiation of leukemia initiating cells [ChIP-seq]

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Small molecule inhibitor of PRC1 E3 ligase activity induces differentiation of leukemia initiating cells [RNA-Seq]

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Small molecule inhibitor of PRC1 E3 ligase activity induces differentiation of leukemia initiating cells [ChIP-seq]

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Small molecule inhibitor of PRC1 E3 ligase activity induces differentiation of leukemia initiating cells [RNA-Seq]

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Functional E3 ligase hotspots and resistance mechanisms to small-molecule degraders [Saturating mutagenesis]

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EGFR is a target of the tumor suppressor E3-ligase FBXW7

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The Hace1 E3 Ligase Modulates the Activity of Multiple Tumor Suppressive CRL E3 Ligases by binding to CAND1

Project description:The Hace1 E3 ligase is a tumor suppressor in stressed cells. Through unknown mechanisms, Hace1 indirectly targets the cyclin D1 proto-oncogene for proteasomal degradation during nutrient depletion. We now show that Hace1 targets HIF1alpha for VHL-dependent degradation during hypoxia. To better understand these diverse actions we performed mass spectrometry to identify Hace1-interacting proteins. We show that Hace1 interacts with cullin-associated NEDD8-dissociated protein 1 (CAND1) under nutrient depletion and hypoxia. CAND1 binds cullins and prevents their entry into cullin ring E3 ligase (CRL) complexes, thus blocking CRL activity. Hace1 binding releases CUL1/2 from CAND1, facilitating assembly of CRL complexes to degrade cyclin D1 and HIF1alpha, respectively. These findings suggest a broad role for Hace1 in regulating tumor suppressive CRL E3 ligases. In this study, we used gene expression profiling to characterize how Hace1 overexpression affect the transcriptional response to hypoxic stress Using Affymetrix exon-level microarrays, we compared the expression profile of HEK293 cells overexpressing either Hace1 or MSCV vector alone, under hypoxia or normoxia

2011-07-01 | E-GEOD-25452 | biostudies-arrayexpress

Small molecule inhibitor of PRC1 E3 ligase activity induces differentiation of leukemia initiating cells

Project description:This SuperSeries is composed of the SubSeries listed below.

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BRCT phosphoprotein recognition, but not E3 ligase activity, is essential for BRCA1 tumor suppression

Project description:It has been recognized that BRCA1, in the form of the BRCA1/BARD1 heterodimer, acting as an ubiquitin E3 ligase offered a possible mechanism to explain its pleiotrophic nature of BRCA1 activity. Our observation that mice lacking BRCA1 enzymatic activity are viable apart from male sterility was unexpected. Our results suggest that the E3 ligase activity of BRCA1 is largely dispensable for normal development and is not essential for all BRCA1 functions. Thus, many of the known and unknown functions of BRCA1 are likely to be mediated independent of its ability to catalyze ubiquitination. The genome copy number patterns were studied on the mice tumors that lacks E3 ubiqitin ligase activity of BRCA1 and were compared to copy number profile of mice lacking p53 and both brca1 and p53. Array CGH was performed using Agilent mouse CGH microarray 244K kit. Genomic DNA isolated from tumor tissue and its corresponding mouse tail were labelled with two different dyes and hybridized simultaneously on to microarray slides to perform comparitive genomic hybridization.

2011-08-25 | E-GEOD-31673 | biostudies-arrayexpress

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