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enzyme crucial for the metabolism of cysteine [RGD, Feb 2006].. Zusätzlich bieten wir Ihnen CDO1 Antikörper (47) und CDO1 Proteine (17) und viele weitere Produktgruppen zu diesem Protein an.
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Presented here are the results of O2-dependent 2-mercaptoaniline reaction using two different thiol dioxygenase enzymes mouse CDO and 3-mercaptopropionic acid dioxygenase isolated from Azotobacter vinelandii. Benzothiazoles are produced by the condensation of 2-mercaptoaniline with aldehydes formed by an off-pathway oxidation of primary alcohols added to aqueous reactions to solubilize the substrate.
Cdo is required for efficient cardiomyogenesis of pluripotent stem cells and an excellent target to improve the differentiation potential of stem cells for generation of transplantable cells to treat cardiomyopathies.
our findings indicate Cdo1 suppresses osteogenic differentiation of BMSCs, through a potential mechanism which involves in Wnt (zeige WNT2 ELISA Kits) signaling reduction concomitantly
We investigated the ontogeny of Cdo1 mRNA expression in mouse fetal and placental tissues, which showed increasing levels from embryonic day 10.5 and was localised to the decidua and several fetal tissues including nasal cavities and brain.
Cdo1 is required for adipogenesis.Cdo1 interacts with Ppar-gamma (zeige PPARG ELISA Kits) during adipogenesis.
In light of these results, the minimal substrate requirements for CDO catalysis and O-activation are discussed.
the timing of chemical steps in the CDO kinetic mechanism is investigated by pH/pD-dependent steady-state kinetics and solvent isotope effects on kcat, kcat/KM, and (O2/CSA) coupling
Cdo1 knockout mice show increased cysteine concentrations and higher rates of metabolism of cysteine to hydrogen sulfide and thiosulfate.
A critical function of CDO appears to be to remove cysteine by a pathway in which the sulfur atom is oxidized in the first step.
Data from kinetic, spectroscopic, and computational studies suggest that in cysteine dioxygenase (CDO) a covalently cross-linked cysteine-tyrosine pair (C93-Y157) plays a vital role in CDO-mediated catalysis.
Promoter NA methylation of CDO1 was demonstrated for the first time to be a cancer-associated methylation in primary gallbladder cancer(GBC), and it has the potential to be a prognostic biomarker of GBC for high-risk patients with stage II GBC.
CDO1 methylation could be a potent prognostic predictor in primary esophageal squamous cell carcinoma and have great potential as a prognostic factor to guide the treatment of patients who need adjuvant chemotherapy.
High methylation of CDO1 gene is responsible of the development of the esophageal adenocarcinoma.
CDO1 promoter methylation is involved in gene regulation and is a potential prognostic biomarker for BCR (zeige BCR ELISA Kits)-free survival in prostate cancer (PC) patients following radical prostatectomy. Further studies are needed to validate CDO1 methylation assays and to evaluate the clinical utility of CDO1 methylation for the management of PCa (zeige FLVCR1 ELISA Kits)
methylation of the CDO1 gene promoter could be strong prognostic indicator in primary BC without preoperative treatment.
CDO1 promoter methylation may not substitute common prognostic makers to predict ccRCC survival, but offers additional, relevant prognostic information, indicating that it might be a novel molecular marker to determine ccRCC prognosis
Decreased expression of CDO1 is associated with esophageal squamous cell carcinoma.
A structural role of the Cys (zeige DNAJC5 ELISA Kits)-Tyr (zeige TYR ELISA Kits) cofactor coordinates the ferrous iron in the active site of CDO1.
A high negative correlation between promoter DNA methylation and gene expression was observed for CDO1, ZNF331 and ZSCAN18 in gastrointestinal tumors.
TGF-b1 suppressed Cdo1 gene transcription through the MEK (zeige MAP2K1 ELISA Kits)/ERK (zeige EPHB2 ELISA Kits) pathway.
enzyme crucial for the metabolism of cysteine
cysteine dioxygenase, type I
, cysteine dioxygenase type 1
, cysteine dioxygenase type I
, cytosolic cysteine dioxygenase 1
, cysteine dioxygenase 1, cytosolic