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Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. Additionally we are shipping IDH2 Antibodies (112) and IDH2 Kits (14) and many more products for this protein.
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Leaf IDH activity reduced by 43% in mutant
TET2, ASXL1 (show ASXL1 Proteins), IDH1 (show IDH1 Proteins), and IDH2 Single Nucleotide Polymorphisms in Turkish Patients with Chronic Myeloproliferative Neoplasms.
IDH1/2 mutations induce a homologous recombination defect that renders tumor cells exquisitely sensitive to poly(adenosine 5'-diphosphate-ribose) polymerase inhibitors
To confirm this result, we analyzed survival data from 142 LGGs from TCGA with IDH1 (show IDH1 Proteins)/IDH2 mutations and no 1p19q codeletion. Despite the high rate of censured data, we found that CNLOH 17p, including the TP53 (show TP53 Proteins) locus, was associated with better outcome (OR = 0.27; p = .026)
6 cases of diffuse glioma that presented a diagnostic challenge due to conflicting IDH1 (show IDH1 Proteins)/IDH2, ATRX (show ATRX Proteins), and 1p/19q results.
In this review, we focus on three key areas in acute myeloid leukemia (show BCL11A Proteins) (AML (show RUNX1 Proteins)) developmental therapeutics: FLT3 (show FLT3 Proteins) inhibitors, IDH(IDH1 (show IDH1 Proteins) and IDH2 ) inhibitors, and drugs that may be particularly beneficial in secondary AML (show RUNX1 Proteins)
The role of mutant IDH1 (show IDH1 Proteins) and IDH2 inhibitors in the treatment of acute myeloid leukemia (show BCL11A Proteins).
olaparib and other PARP inhibitors killed cells in multiple cancer cell lines that harbor IDH1 (show IDH1 Proteins) and IDH2 mutations. In addition, glioma cell lines generated from patient tumors with IDH1 (show IDH1 Proteins) mutations were vulnerable to the investigational PARP inhibitor talazoparib . In mice, olaparib slowed the growth of implanted IDH1 (show IDH1 Proteins)-mutant tumors.
demonstrate the presence of the IDH2 p.R172K/S mutation in patients with cutaneous localizations of angioimmunoblastic T-cell lymphomas.
an IDH mutant-enriched subtype of cholangiocarcinoma with distinct molecular features including low expression of chromatin modifiers, elevated expression of mitochondrial genes, and increased mitochondrial DNA copy number, is reported.
IDH (show IDH1 Proteins) mutations define a distinct subtype of ICC, a malignancy that is largely refractory to current therapies. Our work demonstrates that IDHm ICC cells are hypersensitive to dasatinib and critically dependent on SRC (show SRC Proteins) activity for survival and proliferation, pointing to new therapeutic strategies against these cancers.
The disruption of IDH2 attenuates age-associated hepatic steatosis by the activation of p38 (show CRK Proteins)/cJun (show JUN Proteins) NH2-terminal kinase (JNK (show MAPK8 Proteins)) and p53 (show TP53 Proteins), presumably induced by the elevation of mitochondrial reactive oxygen species (ROS (show ROS1 Proteins)), which in turn resulted in the suppression of hepatic lipogenesis and inflammation via the upregulation of fibroblast growth factor 21 (FGF21 (show FGF21 Proteins)) and the inhibition of NFkappaB signaling pathways.
We propose that D2-HG promotes cardiac dysfunction by impairing alpha-ketoglutarate dehydrogenase (show alphaKGDHC Proteins) and induces histone modifications in an ACL (show APOC4 Proteins)-dependent manner.Combining mathematical modeling and in vivo as well as ex vivo studies, we found that increased amounts of the oncometabolite d-2-hydroxyglutarate (D2-HG), produced by IDH2 mutant leukemic cells, cause contractile dysfunction in the heart
Increased obesity resistance and insulin (show INS Proteins) sensitivity in mice lacking the IDH2 gene has been documented.
treatment with Mito-TEMPO, a mitochondrial-specific superoxide scavenger, recovered mitochondrial fission-fusion imbalance and blunted mitochondrial superoxide production, and reduced the IDH2 knockdown-induced decrease in MnSOD (show SOD2 Proteins) expression, eNOS (show NOS3 Proteins) phosphorylation and NO production in endothelial cells
Findings demonstrate that IDH2 contributes to degeneration of the DA neuron in the neurotoxin model of Parkinson's Disease.
IDH2 deficiency promotes mitochondrial dysfunction and cardiac hypertrophy in mice.
IDH2 and NPM1 (show GJA1 Proteins) mutations synergize in the development and maintenance of acute myeloid leukemia (show BCL11A Proteins) stem-like cells.
7-Ketocholesterol inhibits isocitrate dehydrogenase 2 expression and impairs endothelial function via microRNA-144 leading to atherosclerosis.
These data demonstrate the proto-oncogenic role of mutant IDH2.
The tumor tissue of B16F10 cells transfected with IDH2 antisense cDNA exhibited induction of apoptosis and downregulation of angiogenesis markers.
The enzyme is highly sensitive to Mg(2 (show MCOLN1 Proteins)+) concentration in the physiological range, pointing to a potential regulatory role of [Mg(2 (show MCOLN1 Proteins)+)] in mitochondrial energy metabolism.
Tyr140 and Lys212 are required for the catalytic activity of porcine NADP-dependent isocitrate dehydrogenase (show IDH3B Proteins)
analysis of the coenzyme binding site in the porcine mitochondrial NADP-dependent isocitrate dehydrogenase (show IDH3B Proteins)
These results suggest that IDPm plays an important protective role in cadmium-induced apoptosis by maintaining cellular redox status and by protection of Grx (show GRX1 Proteins) activity.
Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. These enzymes belong to two distinct subclasses, one of which utilizes NAD(+) as the electron acceptor and the other NADP(+). Five isocitrate dehydrogenases have been reported: three NAD(+)-dependent isocitrate dehydrogenases, which localize to the mitochondrial matrix, and two NADP(+)-dependent isocitrate dehydrogenases, one of which is mitochondrial and the other predominantly cytosolic. Each NADP(+)-dependent isozyme is a homodimer. The protein encoded by this gene is the NADP(+)-dependent isocitrate dehydrogenase found in the mitochondria. It plays a role in intermediary metabolism and energy production. This protein may tightly associate or interact with the pyruvate dehydrogenase complex.
, isocitrate dehydrogenase [NADP], mitochondrial
, oxalosuccinate decarboxylase
, NADP+-specific isocitrate dehydrogenase
, NADPH-specific isocitrate dehydrogenase
, isocitrate dehydrogenase 2 (NADP+), mitochondrial
, isocitrate dehydrogenase [NADP], mitochondrial-like