Chinese medical journal, 124(17), 2611-2615 (2011-11-02)
Site A132Arg mutations potentially impair the affinity of isocitrate dehydrogenase 1 (IDH1) for its substrate isocitrate (ICT), consequently reducing the production of α-ketoglutarate and leading to tumor growth through the induction of the hypoxia-inducible factor-1 (HIF-1) pathway. However, given that
Yeast NAD(+)-specific isocitrate dehydrogenase is an allosterically regulated octameric enzyme composed of four heterodimers of a catalytic IDH2 subunit and a regulatory IDH1 subunit. Despite structural predictions that the enzyme would contain eight isocitrate binding sites, four NAD(+) binding sites
Journal of AOAC International, 93(3), 956-965 (2010-07-16)
Sugar and nonvolatile acid analyses were conducted on 52 samples of blackberries (Rubus spp), the objective being to develop a compositional database for evaluating authenticity and quality. Brix ranged from 6.88 to 16.83, with a mean of 10.82. Titratable acidity
Metabolism, gliomas, and IDH1.
Jan Smeitink
The New England journal of medicine, 362(12), 1144-1145 (2010-03-26)
The Journal of biological chemistry, 283(16), 10872-10880 (2008-02-08)
Mitochondrial NAD(+)-specific isocitrate dehydrogenases (IDHs) are key regulators of flux through biosynthetic and oxidative pathways in response to cellular energy levels. Here we present the first structures of a eukaryotic member of this enzyme family, the allosteric, hetero-octameric, NAD(+)-specific IDH
We describe here a rapid and sensitive method to separate and measure D-2-OHG and L-2-OHG enantiomers using high-resolution mass spectrometry (HRMS) detection.
Our team of scientists has experience in all areas of research including Life Science, Material Science, Chemical Synthesis, Chromatography, Analytical and many others.
