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Mervi H Toivari et al.
Applied microbiology and biotechnology, 85(3), 731-739 (2009-08-28)
Phosphoglucose isomerase-deficient (pgi1) strains of Saccharomyces cerevisiae were studied for the production of D-ribose and ribitol from D-glucose via the intermediates of the pentose phosphate pathway. Overexpression of the genes coding for NAD(+)-specific glutamate dehydrogenase (GDH2) of S. cerevisiae or
Shanti Balasubramaniam et al.
Journal of pediatric endocrinology & metabolism : JPEM, 24(7-8), 573-577 (2011-09-22)
Hyperinsulinism-hyperammonemia syndrome (HI/HA) (OMIM 606762), the second most common form of congenital hyperinsulinism (CHI) is associated with activating missense mutations in the GLUD1 gene, which encodes the mitochondrial matrix enzyme, glutamate dehydrogenase (GDH). Patients present with recurrent symptomatic postprandial hypoglycemia
Cleanthe Spanaki et al.
Neurotoxicity research, 21(1), 117-127 (2011-11-01)
Glutamate dehydrogenase (GDH) catalyzes the reversible inter-conversion of glutamate to α-ketoglutarate and ammonia. High levels of GDH activity is found in mammalian liver, kidney, brain, and pancreas. In the liver, GDH reaction appears to be close-to-equilibrium, providing the appropriate ratio
Jaekyoung Son et al.
Nature, 496(7443), 101-105 (2013-03-29)
Cancer cells have metabolic dependencies that distinguish them from their normal counterparts. Among these dependencies is an increased use of the amino acid glutamine to fuel anabolic processes. Indeed, the spectrum of glutamine-dependent tumours and the mechanisms whereby glutamine supports
Lia Rosso et al.
PLoS genetics, 4(8), e1000150-e1000150 (2008-08-09)
Many new gene copies emerged by gene duplication in hominoids, but little is known with respect to their functional evolution. Glutamate dehydrogenase (GLUD) is an enzyme central to the glutamate and energy metabolism of the cell. In addition to the
Susan M Hutson et al.
Neurochemistry international, 59(4), 518-524 (2011-05-31)
Branched-chain amino acids (BCAAs) catabolism follows sequential reactions and their metabolites intersect with other metabolic pathways. The initial enzymes in BCAA metabolism, the mitochondrial branched-chain aminotransferase (BCATm), which deaminates the BCAAs to branched-chain α-keto acids (BCKAs); and the branched-chain α-keto
Michisuke Yuzaki
The European journal of neuroscience, 32(2), 191-197 (2010-07-22)
Several C1q family members, especially the Cbln and C1q-like subfamilies, are highly and predominantly expressed in the central nervous system. Cbln1, a member of the Cbln subfamily, plays two unique roles at parallel fiber (PF)-Purkinje cell synapses in the cerebellum:
Jaclyn Bailey et al.
The FEBS journal, 278(17), 3140-3151 (2011-07-14)
Bovine glutamate dehydrogenase is potently inhibited by zinc and the major impact is on V(max) suggesting a V-type effect on catalysis or product release. Zinc inhibition decreases as glutamate concentrations decrease suggesting a role for subunit interactions. With the monocarboxylic
Kazuyoshi Aso et al.
Osaka city medical journal, 57(1), 1-9 (2011-11-24)
Congenital hyperinsulinism and hyperammonemia (CHH) is caused by gain of function of glutamate dehydrogenase (GDH). The genetic abnormalities are known to be located in three specific regions on the GDH protein. We describe here three different missense mutations identified in
K E Snider et al.
The Journal of clinical endocrinology and metabolism, 98(2), E355-E363 (2013-01-01)
Hypoglycemia due to congenital hyperinsulinism (HI) is caused by mutations in 9 genes. Our objective was to correlate genotype with phenotype in 417 children with HI. Mutation analysis was carried out for the ATP-sensitive potassium (KATP) channel genes (ABCC8 and
Andreas Plaitakis et al.
European journal of human genetics : EJHG, 18(3), 336-341 (2009-10-15)
Parkinson's disease (PD), a common neurodegenerative disorder characterized by progressive loss of dopaminergic neurons and their terminations in the basal ganglia, is thought to be related to genetic and environmental factors. Although the pathophysiology of PD neurodegeneration remains unclear, protein
Morgan E Roberts et al.
Biochemistry, 52(50), 8969-8971 (2013-12-04)
MitoNEET is a protein that was identified as a drug target for diabetes, but its cellular function as well as its role in diabetes remains elusive. Protein pull-down experiments identified glutamate dehydrogenase 1 (GDH1) as a potential binding partner. GDH1
Cleanthe Spanaki et al.
The Journal of biological chemistry, 285(22), 16748-16756 (2010-03-03)
Mammalian glutamate dehydrogenase (GDH) is an allosterically regulated enzyme that is expressed widely. Its activity is potently inhibited by GTP and thought to be controlled by the need of the cell for ATP. In addition to this housekeeping human (h)
Konstantinos Kanavouras et al.
Journal of neurochemistry, 109 Suppl 1, 167-173 (2009-05-07)
Glutamate dehydrogenase (GDH) in human exists in GLUD1 and GLUD2 gene-encoded isoforms (hGDH1 and hGDH2, respectively), differing in their regulation and tissue expression pattern. Whereas hGDH1 is subject to GTP control, hGDH2 uses for its regulation, a novel molecular mechanism
Hyperinsulinism and hyperammonaemia syndrome and severe myoclonic epilepsy of infancy.
F Pérez Errazquin et al.
Neurologia (Barcelona, Spain), 26(4), 248-252 (2010-12-18)
Cleanthe Spanaki et al.
Neurochemistry international, 61(4), 470-481 (2012-06-05)
Mammalian glutamate dehydrogenase (GDH) is a housekeeping mitochondrial enzyme (hGDH1 in the human) that catalyses the reversible inter-conversion of glutamate to α-ketoglutarate and ammonia, thus interconnecting amino acid and carbohydrate metabolism. It displays an energy sensing mechanism, which permits enzyme
Manish Verma et al.
Biochimica et biophysica acta, 1827(1), 38-49 (2012-10-10)
The sustained opening of the mitochondrial permeability transition pore (PTP) is a decisive event in the onset of irreversible cell injury. The PTP is modulated by numerous exogenous and endogenous effectors, including mitochondrial membrane potential, ions and metabolites. Mitochondrial sirtuins
Dimitra Kotzamani et al.
Neurochemistry international, 61(4), 463-469 (2012-06-20)
Human glutamate dehydrogenase (hGDH) exists in two highly homologous isoforms with a distinct regulatory and tissue expression profile: a housekeeping hGDH1 isoprotein encoded by the GLUD1 gene and an hGDH2 isoenzyme encoded by the GLUD2 gene. There is evidence that
Charles A Stanley
Neurochemistry international, 59(4), 465-472 (2010-12-07)
Glutamate dehydrogenase (GDH) has recently been shown to be involved in two genetic disorders of hyperinsulinemic hypoglycemia in children. These include the hyperinsulinism/hyperammonemia syndrome caused by dominant activating mutations of GLUD1 which interfere with inhibitory regulation by GTP and hyperinsulinism
Ioannis Zaganas et al.
Neurochemistry international, 55(1-3), 52-63 (2009-05-12)
In all mammals, glutamate dehydrogenase (GDH), an enzyme central to the metabolism of glutamate, is encoded by a single gene (GLUD1 in humans) which is expressed widely (housekeeping). Humans and other primates also possess a second gene, GLUD2, which encodes
Ioannis Zaganas et al.
Neurochemistry international, 61(4), 455-462 (2012-06-20)
Glutamate dehydrogenase (GDH), a mitochondrial enzyme with a key metabolic role, exists in the human in hGDH1 and hGDH2 isoforms encoded by the GLUD1 and GLUD2 genes, respectively. It seems that GLUD1 was retroposed to the X chromosome where it
Mehran Karimi et al.
Seminars in thrombosis and hemostasis, 35(4), 426-438 (2009-07-15)
Factor XIII (FXIII) is a tetrameric zymogen (FXIII-A (2)B (2)) that is converted into an active transglutaminase (FXIIIa) by thrombin and Ca (2+) in the terminal phase of the clotting cascade. By cross-linking fibrin chains and alpha (2) plasmin inhibitor
Glutamic dehydrogenase.
H J STRECKER
Archives of biochemistry and biophysics, 46(1), 128-140 (1953-09-01)
Generalized dystonia in a patient with a novel mutation in the GLUD1 gene.
Ryosuke Miyamoto et al.
Movement disorders : official journal of the Movement Disorder Society, 27(9), 1198-1199 (2012-06-26)
Nayla Munawar et al.
Extremophiles : life under extreme conditions, 16(3), 463-476 (2012-04-25)
Enzymes produced by halophilic archaea are generally heat resistant and organic solvent tolerant, and accordingly important for biocatalytic applications in 'green chemistry', frequently requiring a low-water environment. NAD(+)-dependent glutamate dehydrogenase from an extremely halophilic archaeon Halobacterium salinarum strain NRC-36014 was
Minfeng Ying et al.
Redox biology, 46, 102065-102065 (2021-07-23)
Although glucose, through pentose phosphate pathway (PPP), is the main source to generate NADPH, solid tumors are often deprived of glucose, hence alternative metabolic pathways to maintain NADPH homeostasis in cancer cells are required. Here, we report that lactate and
The crystallization and characterization of L-glutamic acid dehydrogenase.
J A OLSON et al.
The Journal of biological chemistry, 197(1), 67-79 (1952-05-01)
Duo You et al.
Chinese journal of cancer research = Chung-kuo yen cheng yen chiu, 33(3), 308-322 (2021-07-30)
α-ketoglutarate (α-KG) is the substrate to hydroxylate collagen and hypoxia-inducible factor-1α (HIF-1α), which are important for cancer metastasis. Previous studies have shown that the upregulation of collagen prolyl 4-hydroxylase in breast cancer cells stabilizes the expression of HIF-1α by depleting
Flavio Faletra et al.
Gene, 521(1), 160-165 (2013-03-20)
Congenital hyperinsulinism (CHI) is a genetic disorder characterized by profound hypoglycemia related to an inappropriate insulin secretion. It is a heterogeneous disease classified into two major subgroups: "channelopathies" due to defects in ATP-sensitive potassium channel, encoded by ABCC8 and KCNJ11
Andreas Plaitakis et al.
Neurochemistry international, 59(4), 495-509 (2011-03-23)
Whereas glutamate dehydrogenase in most mammals (hGDH1 in the human) is encoded by a single functional GLUD1 gene expressed widely, humans and other primates have acquired through retroposition an X-linked GLUD2 gene that encodes a highly homologous isoenzyme (hGDH2) expressed
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