Results 201 to 210 of about 90,755 (258)

Myocardial Lipid Metabolism Imbalance: The Pathological Core and Novel Diagnostic‐Therapeutic Directions of Cardiovascular Diseases

Journal of Biochemical and Molecular Toxicology, Volume 40, Issue 8, August 2026.
In cardiac cells, Plin5/AMPK regulate lipid homeostasis; excess CD36‐mediated uptake drives lipotoxicity, mitochondrial dysfunction, and CVDs (e.g., heart failure). Biomarkers (ApoB/ApoA‐1) and therapies (SGLT2 inhibitors) target this cascade. ABSTRACT Cardiac lipid metabolism is fundamental to myocardial energy homeostasis, with fatty acid oxidation ...
Peiyun Xie, Qun Zeng, Hongrui Wang, Meihua She   +3 more
wiley   +1 more source

Beyond a Metabolite: Lactylation as a Pivotal Regulator of Colorectal Cancer Pathogenesis and Treatment Resistance

Journal of Biochemical and Molecular Toxicology, Volume 40, Issue 8, August 2026.
This review elucidates how lactylation, a novel histone modification driven by lactate, regulates colorectal cancer pathogenesis. We summarize its roles in tumor progression, metastasis, stemness, immunosuppression, and therapy resistance, and discusses the promising therapeutic strategies of targeting the lactylation pathway.
Shuilan Yao, Yun Liang, Xinwen Liang, Qisheng Su, Xiaohong Li   +4 more
wiley   +1 more source

Corrigendum to: Ebselen induces reactive oxygen species (ROS)-mediated cytotoxicity in Saccharomyces cerevisiae with inhibition of glutamate dehydrogenase being a target https://doi.org/10.1016/j.fob.2014.01.002. [PDF]

FEBS Open Bio
europepmc   +1 more source

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Studies of Glutamate Dehydrogenase

European Journal of Biochemistry, 1973
Specific interaction between α‐NADH and glutamate dehydrogenase is demonstrated by difference spectroscopy, circular dichroism and fluorescence measurements. Quantitative binding studies in the preparative ultracentrifuge yield six identical α‐NADH binding sites per oligomer with a dissociation constant of 20 μM.
R, Koberstein, J, Krause, H, Sund
openaire   +4 more sources

Glutamate dehydrogenase of Tetrahymena

Biochimica et Biophysica Acta (BBA) - Enzymology, 1974
Abstract Glutamate dehydrogenase [ l -glutamate: NAD(P) oxidoreductase (deaminating), EC 1.4.1.3] located in the mitochondria and able to utilize NAD, NADP, NADH or NADPH as substrate, has been purified 67-fold from Tetrahymena pyriformis . The activity with the four pyridine nucleotide substrates was catalyzed by a single enzyme as indicated by the
A B, Hooper, K R, Terry, K D, Kemp
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Glutamate dehydrogenase-malate dehydrogenase complex

Archives of Biochemistry and Biophysics, 1979
Abstract Kinetic and Sephadex gel filtration epxeriments indicate that in the presence of palmitoyl-CoA, glutamate dehydrogenase forms a complex with mitochondrial malate dehydrogenase. In this complex, palmitoyl-CoA is bound to glutamate dehydrogenase but is not bound to malate dehydrogenase.
L A, Fahien, E, Kmiotek, L, Smith
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Glutamate Dehydrogenase

2018
International ...
Tipton, K.F., Couée, Ivan
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Folates as inhibitors of glutamate dehydrogenase

Biochimica et Biophysica Acta (BBA) - Enzymology, 1976
Folates and tetrahydrofolates inhibit beef liver glutamate dehydrogenase (EC 1.4.1.2). Double reciprocal plats indicate a competitive inhibition for alpha-ketoglutarate-glutamate by folic acid and methotrexate and a complex or mixed type for NAD-NADH site. Pteroic acid is not inhibitory at the concentrations studied.
W E, White, L K, Yielding, C L, Krumdieck   +2 more
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Allosteric Transitions of Glutamate Dehydrogenase

Nature, 1968
L-GLUTAMATE dehydrogenase from beef liver, GDH (EC 1.4.1.3), has a molecular weight of 310,000 (referred to as the oligomer) consisting of six identical subunits1 and six active sites2.
A D, Malcolm, G K, Radda
openaire   +2 more sources