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ProteomicsMetabolism of ethylene and epoxyethane by the methanotrophic bacterium Methylohalobius crimeensis
M. crimeensis contains an operon with a putative pathway for catabolic oxidation of epoxyethane to acetyl CoA. Proteomics was used to meausure the expression of the proteins encoded by this operon before and after ethylene exposure.
ORGANISM(S): Methylohalobius crimeensis 10Ki 
2024-12-09 | PXD051614 | Pride
Methylohalobius crimeensis Ethylene Epoxyethane 
UnknownEthylene and epoxyethane metabolism in methanotrophic bacteria: comparative genomics and physiological studies using <i>Methylohalobius crimeensis</i>.
Not available
S-EPMC11507031 | biostudies-literature
UnknownIdentification of polypeptides expressed in response to vinyl chloride, ethene, and epoxyethane in Nocardioides sp. strain JS614 by using peptide mass fingerprinting.
Not available
S-EPMC1932774 | biostudies-literature
GenomicsGenome-wide studies identify a novel interplay between AML1 and AML1/ETO in t(8;21) acute myeloid leukemia
The AML1/ETO fusion protein is essential to the development of acute myeloid leukemia (AML), and is well recognized for its dominant-negative effect on the co-existing wild-type protein AML1. However, the involvement of wild-type AML1 in AML1/ETO-driven leukemogenesis remains elusive. Through chroma...
ORGANISM(S): Homo sapiens 
2015-11-04 | E-GEOD-65427 | biostudies-arrayexpress
TranscriptomicsGene expression profile and DNA binding pattern of AML1/ETO in U937 cells
This SuperSeries is composed of the following subset Series: GSE10520: Genes regulated by AML1/ETO in U937 cells GSE10537: Gene expression profiling of AML1/ETO regulated genes and binding pattern on human promoters in U937 cells GSE10578: AML1/ETO, AML1, and HEB binding patterns on chromosme 19 GSE...
ORGANISM(S): Homo sapiens 
2010-06-24 | E-GEOD-10537 | biostudies-arrayexpress
TranscriptomicsDepletion of RUNX1/ETO in t(8;21) AML cells leads to genome-wide changes in chromatin structure and transcription factor binding [expression array data]
The t(8;21) translocation fuses the DNA binding domain of the hematopoietic master regulator RUNX1 to the ETO protein. The resultant RUNX1/ETO fusion protein is a leukemia-initiating transcription factor that interferes with RUNX1 function. The result of this interference is a block in differentiati...
ORGANISM(S): Homo sapiens 
2012-03-27 | E-GEOD-29223 | biostudies-arrayexpress
TranscriptomicsDepletion of RUNX1/ETO in t(8;21) AML cells leads to genome-wide changes in chromatin structure and transcription factor binding (Illumina expression)
The t(8;21) translocation fuses the DNA binding domain of the hematopoietic master regulator RUNX1 to the ETO protein. The resultant RUNX1/ETO fusion protein is a leukemia-initiating transcription factor that interferes with RUNX1 function. The result of this interference is a block in differentiati...
ORGANISM(S): Homo sapiens 
2012-03-27 | E-GEOD-34594 | biostudies-arrayexpress
TranscriptomicsAML1/ETO, AML1, and HEB binding patterns on chromosme 19
Approximately 20% of Acute Myelogenous Leukemia (AML) cases carry the t(8;21) translocation, which involves the AML1 and ETO genes, and express the resulting AML1/ETO fusion protein that functions as a transcriptional repressor by recruiting NCoR/SMRT/HDAC complexes to DNA. We used ChIP-chip to iden...
ORGANISM(S): Homo sapiens 
2008-11-27 | E-GEOD-10578 | biostudies-arrayexpress
GenomicsDepletion of RUNX1/ETO in t(8;21) AML cells leads to genome-wide changes in chromatin structure and transcription factor binding (ChIP-seq)
The t(8;21) translocation fuses the DNA binding domain of the hematopoietic master regulator RUNX1 to the ETO protein. The resultant RUNX1/ETO fusion protein is a leukemia-initiating transcription factor that interferes with RUNX1 function. The result of this interference is a block in differentiati...
ORGANISM(S): Homo sapiens 
2012-03-27 | E-GEOD-34540 | biostudies-arrayexpress
UnknownEpoxyalkane: coenzyme M transferase in the ethene and vinyl chloride biodegradation pathways of mycobacterium strain JS60.
Not available
S-EPMC193758 | biostudies-literature
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