نتایج جستجو برای: gapdh

تعداد نتایج: 2656  

Journal: :The Biochemical journal 1995
P Marin M Maus J Bockaert J Glowinski J Prémont

Nitric oxide (NO) induces a covalent modification of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from various tissues. This phenomenon, which has previously been interpreted as an auto-ADP-ribosylation, is in fact a covalent binding of NAD+ to the enzyme. In the present study, we show that 3-morpholino-sydnonimine (SIN-1) is much more efficient than sodium nitroprusside (SNP) in stimulatin...

Journal: :Journal of virology 2000
S Choudhary B P De A K Banerjee

We previously reported specific interaction of cellular glyceraldehyde 3-phosphate dehydrogenase (GAPDH), the key glycolytic enzyme, and La protein, the RNA polymerase III transcription factor, with the cis-acting RNAs of human parainfluenza virus type 3 (HPIV3) and packaging of these proteins within purified virions (B. P. De, S. Gupta, H. Zhao, J. Z. Drazba, and A. K. Banerjee, J. Biol. Chem....

Fani Maleki A Nazari F, Parham A

Background: Adipose tissue is a main source for isolation of equine mesenchymal stem cells (MSCs) at different ages. It seems that characteristics of adipose-derived MSCs especially gene expression profile are changing along with age increase. A proper reference gene is required for normalizing data in gene expression analysis by qRT-PCR. This study aimed to evaluate whether GAPDH has a stable ...

Journal: :Toxicological sciences : an official journal of the Society of Toxicology 2006
Balázs Németi Iván Csanaky Zoltán Gregus

The environmentally prevalent arsenate (AsV) is reduced in the body to the much more toxic arsenite (AsIII). Recently, we have demonstrated that the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyzes the reduction of AsV in the presence of glutathione, yet the role of GAPDH in AsV reduction in vivo is unknown. Therefore, we examined the effect of (S)-alpha-cholorhydrin...

2015
Sunhee Hwang Marie-Hélène Disatnik Daria Mochly-Rosen

Mitochondrial dysfunction is implicated in multiple neurodegenerative diseases. In order to maintain a healthy population of functional mitochondria in cells, defective mitochondria must be properly eliminated by lysosomal machinery in a process referred to as mitophagy. Here, we uncover a new molecular mechanism underlying mitophagy driven by glyceraldehyde-3-phosphate dehydrogenase (GAPDH) un...

Journal: :The Journal of biological chemistry 2003
Sandrine Lebreton Emmanuelle Graciet Brigitte Gontero

The activity of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) embedded in the phosphoribulokinase (PRK).GAPDH.CP12 complex was increased 2-3-fold by reducing agents. This occurred by interaction with PRK as the cysteinyl sulfhydryls (4 SH/subunit) of GAPDH within the complex were unchanged whatever the redox state of the complex. But isolated GAPDH was not activated. Alkylation plus mass spe...

2013
A. Katrin Helfer-Hungerbuehler Stefan Widmer Regina Hofmann-Lehmann

Quantitative real-time PCR (qPCR) is broadly used to detect and quantify nucleic acid targets. In order to determine cell copy number and genome equivalents, a suitable reference gene that is present in a defined number in the genome is needed, preferably as a single copy gene. For most organisms, a variable number of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) pseudogenes have been report...

Journal: :The Journal of clinical investigation 2003
Xueliang Du Takeshi Matsumura Diane Edelstein Luciano Rossetti Zsuzsanna Zsengellér Csaba Szabó Michael Brownlee

In this report, we show that hyperglycemia-induced overproduction of superoxide by the mitochondrial electron transport chain activates the three major pathways of hyperglycemic damage found in aortic endothelial cells by inhibiting GAPDH activity. In bovine aortic endothelial cells, GAPDH antisense oligonucleotides activated each of the pathways of hyperglycemic vascular damage in cells cultur...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2004
Chengguo Xing Jacob R LaPorte Joseph K Barbay Andrew G Myers

Saframycin A (SafA) is a member of a class of natural products with potent antiproliferative effects in leukemia- and tumor-derived cells. This activity is frequently conjectured to derive from the ability of saframycins to covalently modify duplex DNA. We used a DNA-linked affinity purification technique to identify GAPDH as a protein target of DNA-small molecule adducts of several members of ...

Journal: :Protein science : a publication of the Protein Society 2014
Bo Y Baker Wuxian Shi Benlian Wang Krzysztof Palczewski

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) catalyzes the oxidative phosphorylation of d-glyceraldehyde 3-phosphate (G3P) into 1,3-diphosphoglycerate (BGP) in the presence of the NAD cofactor. GAPDH is an important drug target because of its central role in glycolysis, and nonglycolytic processes such as nuclear RNA transport, DNA replication/repair, membrane fusion and cellular apoptosis....

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