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Isocitrate dehydrogenases catalyze the oxidative decarboxylation of isocitrate to 2-oxoglutarate. Additionally we are shipping IDH1 Antibodies (211) and IDH1 Kits (24) and many more products for this protein.
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Findings demonstrated that miR (show MLXIP Proteins)-148a promotes glioma cell invasion and tumorigenesis by downregulating GADD45A (show GADD45A Proteins). Findings provide novel insights into how GADD45A (show GADD45A Proteins) is downregulated by miR (show MLXIP Proteins)-148a in IDH1R132H glioma
Glioblastoma multiforme HIF1-alpha (show HIF1A Proteins) and serum VEGF (show VEGFA Proteins) levels were found to be significantly increased in IDH1-mutated tumor tissues.Mutated IDH1 may contribute to carcinogenesis via induction of HIF-1 alpha (show HIF1A Proteins) pathway in primary glioblastoma multiforme.
IDH1 mutation is associated with 1p19q co-deletion diffuse glioma.
DNA mutational analysis in IDH1 in acute myeloid leukemia (show BCL11A Proteins).
Authors conclude that PROX1 (show PROX1 Proteins) is a new prognostic biomarker for 1p19q non-codeleted high-grade astrocytomas that have progressed from pre-existing low-grade tumors and harbor IDH1 mutations.
In primary human acute myeloid leukemia (show BCL11A Proteins) samples, the 2-hydroxyglutarate levels observed in samples with mutant IDH1 or IDH2 (show IDH2 Proteins) status were higher than those observed in samples without an enzyme mutation, similar to what was observed in the original study (Figure 5C; Ward et al., 2010).
Results present a unique phenotype of isocitrate dehydrogenase-mutation primary de novo glioblastomas arising from insular cortex region, the molecular backgrounds of which are similar to secondary glioblastomas.
These findings suggest that IDH1 upregulation represents a common metabolic adaptation by glioblastoma to support macromolecular synthesis, aggressive growth, and therapy resistance.
Patients with low IDH1-R132H expression had a poor overall survival. Our data indicate that IDH1-R132H expression could be used as a predictive marker of prognosis for patients with gastrointestinal cancer.
ATRX (show ATRX Proteins) deficiency was mutually exclusive with LOH. Conversely, ATRX (show ATRX Proteins)-proficient tumours immunoreactive for R132H-mutant isocitrate dehydrogenase 1 (IDH1) showed a high rate (85%) of LOH.
Through the use of a conditional mutant mouse model that confers a less aggressive tumor phenotype, findings provide new insight into the effects of mutant Idh1 on a candidate cell of origin for glioma, mutant Idh1's role in disrupting the microenvironment from which gliomas arise, and mutant Idh1's effect on the course of glioma progression.
IDH1 mutations caused down-regulation of leukocyte chemotaxis, resulting in repression of the tumor-associated immune system.
Idh1(R132H) mutation in the major adult neurogenic stem cell niche causes a phenotype resembling gliomagenesis
Mutant IDH1 downregulates the DNA damage (DD) sensor ATM by altering histone methylation, leading to impaired DNA repair, increased sensitivity to DD, and reduced HSC self-renewal, independent of TET2.
Using whole RNA sequencing of bone marrow cells in iron-overloaded mice, it was observed that Idh1 and Aco1 (show ACO1 Proteins), enzymes involved in the TCA cycle, were elevated.
data suggest that mutant IDH1 contributes to malignancy in the T-cell lineage and may alter the metabolic profile of malignant T cells
The results suggest that Idh1 has a physiological function in protecting cells from oxidative stress by regulating the intracellular NADP(+)/NADPH ratio.
These results support the translational potential of immunotherapeutic targeting of gliomas carrying IDH1 mutations R132H.
MiR (show MLXIP Proteins)-181a regulates lipid metabolism via IDH1
revealed a role for IDH1 in the synthesis/turnover of phospholipids in developing astrocytes and highlight the lipid alterations resulting from the loss of wild-type IDH1 activity.
Data suggest that the expression of cytosolic NADP+-dependent isocitrate dehydrogenase in bovine mammary epithelium is modulated by regulators of differentiation including extracellular matrix and lactogenic hormones as well as metabolic effectors.
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 (show IDH2 Proteins) 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 cytoplasm and peroxisomes. It contains the PTS-1 peroxisomal targeting signal sequence. The presence of this enzyme in peroxisomes suggests roles in the regeneration of NADPH for intraperoxisomal reductions, such as the conversion of 2, 4-dienoyl-CoAs to 3-enoyl-CoAs, as well as in peroxisomal reactions that consume 2-oxoglutarate, namely the alpha-hydroxylation of phytanic acid. The cytoplasmic enzyme serves a significant role in cytoplasmic NADPH production.
isocitrate dehydrogenase 1 (NADP+), soluble
, isocitrate dehydrogenase [NADP] cytoplasmic-like
, NADP(+)-specific ICDH
, NADP-dependent isocitrate dehydrogenase, cytosolic
, NADP-dependent isocitrate dehydrogenase, peroxisomal
, isocitrate dehydrogenase [NADP] cytoplasmic
, oxalosuccinate decarboxylase
, cytosolic NADP-isocitrate dehydrogenase
, isocitrate dehydrogenase 1
, Isocitrate dehydrogenase 1, soluble
, NADPH-specific isocitrate dehydrogenase
, isocitrate dehydrogenase [NADP], mitochondrial