Results 91 to 100 of about 693,247 (202)

Partial purification and properties of isocitrate dehydrogenase kinase/phosphatase from Escherichia coli ML308

open access: yes, 1984
1. Isocitrate dehydrogenase kinase and isocitrate dehydrogenase phosphatase were purified over 1000‐fold from Escherichia coli ML308 by a procedure involving fractionation with (NH4)2SO4 and chromatography on DEAE‐cellulose, blue‐dextran‐Sepharose and ...
Nimmo, Gillian A.   +3 more
core   +1 more source

Energetic dysregulations in psychotic disorders: Targets for new therapeutics

open access: yesThe FEBS Journal, EarlyView.
The present review synthesizes literature documenting aberrant energy production and use, specifically related to mitochondrial and redox dysregulation, in psychotic disorders. Findings from different levels of investigation—genetic, cellular, and in vivo imaging—converge on aberrant energy metabolism as a hallmark of psychotic disorders.
Jacey Anderson   +10 more
wiley   +1 more source

Roles of Arg231 and Tyr284 of Thermus thermophilus isocitrate dehydrogenase in the coenzyme specificity [PDF]

open access: yes, 1994
The coenzyme binding site of isocitrate dehydrogenase from Thermus thermophilus was analyzed by site-directed mutagenesis. The mutation analysis revealed that Arg231 and Tyr284 are involved in the discrimination between NAD and NADP, suggesting that ...
Takuro Yaoi   +5 more
core   +1 more source

A comprehensive study on ferredoxin isoforms in the cyanobacterium Synechocystis sp. PCC 6803

open access: yesThe FEBS Journal, EarlyView.
Ferredoxins are small FeS cluster‐containing proteins that play a central role in distributing electrons within the cell. The cyanobacterium Synechocystis sp. PCC 6803 contains several ferredoxin isoforms and their biophysical properties (UV/Vis and EPR spectra, Em potential), expression patterns, and interactions with the electron donors photosystem I
Marko Boehm   +14 more
wiley   +1 more source

The PRIME trial: An investigator‐initiated, multicentre, phase II study of the poly(ADP‐ribose) polymerase inhibitor olaparib in isocitrate dehydrogenase (IDH)‐mutated relapsed/refractory acute myeloid leukaemia and myelodysplastic syndromes

open access: yes
British Journal of Haematology, EarlyView.
Rory M. Shallis   +18 more
wiley   +1 more source

Intratumoral IDH1 mutation status in intrahepatic cholangiocarcinoma is homogeneous

open access: yesHistopathology, EarlyView.
IDH1 mutations are spatially homogeneous in intrahepatic cholangiocarcinoma. Single‐sample molecular testing is sufficient for clinical decision‐making. Introduction IDH1 mutations occur in approximately 10%–20% of intrahepatic cholangiocarcinoma (iCCA) and constitute an established target for molecularly guided therapy.
Sharon Weidmann   +8 more
wiley   +1 more source

Isocitrate dehydrogenase inhibitors in acute myeloid leukemia

open access: yesBiomarker Research, 2019
Isocitrate dehydrogenase (IDH) is a key enzyme involved in the conversion of isocitrate to α-ketoglutarate (α-KG) in the tricarboxylic acid (TCA) cycle. IDH mutation produces a neomorphic enzyme, which can lead to the abnormal accumulation of R-2-HG and ...
Xiaoyan Liu, Yuping Gong
doaj   +1 more source

Light signaling controls chloroplast pyruvate metabolism through the STF1/2–PKP1 module in soybean

open access: yesJournal of Integrative Plant Biology, EarlyView.
In soybean, light‐responsive proteins switch on GmPKP1, which boosts chloroplast pyruvate production. This increases pigments, photosynthesis, seed oil, pod number, and yield, revealing a new way that light boosts crop productivity. ABSTRACT Light signaling coordinates plant development with metabolism, but the link between photoreceptors and ...
Faming Lin   +11 more
wiley   +1 more source

Cloning and characterization of the isocitrate dehydrogenase gene from oleaginous yeast Lipomyces starkeyi

open access: yes, 2008
Oleaginous yeast Lipomyces starkeyi can accumulate intracellular lipids over 65% of its cell dry weight [1]. Mitochondrial NAD+-specific isocitrate dehydrogenase (IDH) catalyzes the oxidative decarboxylation of isocitrare to α-ketoglutarate in eukaryotic
唐伟, 赵宗保, 张素芳, 谭海东
core  

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