نتایج جستجو برای: gapdh

تعداد نتایج: 2656  

Journal: :Proceedings of the National Academy of Sciences of the United States of America 2015
Masataka Suzuki Jumpei Sasabe Yurika Miyoshi Kanako Kuwasako Yutaka Muto Kenji Hamase Masaaki Matsuoka Nobuaki Imanishi Sadakazu Aiso

D-Serine is an essential coagonist with glutamate for stimulation of N-methyl-D-aspartate (NMDA) glutamate receptors. Although astrocytic metabolic processes are known to regulate synaptic glutamate levels, mechanisms that control D-serine levels are not well defined. Here we show that d-serine production in astrocytes is modulated by the interaction between the D-serine synthetic enzyme serine...

Journal: :Infection and immunity 1998
D Gozalbo I Gil-Navarro I Azorín J Renau-Piqueras J P Martínez M L Gil

By immunoelectron microscopy with a polyclonal antibody against the cytosolic glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) from Candida albicans (anti-GAPDH PAb), the protein was clearly detected at the outer surface of the cell wall, particularly on blastoconidia, as well as in the cytoplasm. Intact blastoconidia were able to adhere to fibronectin and laminin immobilized ...

Journal: :Genetics and molecular research : GMR 2015
M C Rios W R T Silva A F Azevedo P L Santos S A Teixeira M N Muscará S M Thomazzi R P Almeida R P M Fernandes R Scher

Leishmania spp are the causative agents of a spectrum of diseases termed leishmaniasis that affect mammals, including humans and dogs. Although reactive nitrogen species are employed in the control of parasitism by the immune system, it is known that Leishmania can withstand this oxidative stress. As the mechanism by which these species are resistant to nitric oxide (NO) is poorly understood, t...

2016
Norbert Schormann Chapelle A Ayres Alexandra Fry Todd J Green Surajit Banerjee Glen C Ulett Debasish Chattopadhyay

Glyceraldehyde 3-phosphate dehydrogenase or GAPDH is an evolutionarily conserved glycolytic enzyme. It catalyzes the two step oxidative phosphorylation of D-glyceraldehyde 3-phosphate into 1,3-bisphosphoglycerate using inorganic phosphate and NAD+ as cofactor. GAPDH of Group B Streptococcus is a major virulence factor and a potential vaccine candidate. Moreover, since GAPDH activity is essentia...

1988
Nancy Schek Bruce Lee Olivera J. Finn

To identify and characterize genes, the products of which play a role in pancreatic adenocarcinoma, we constructed a complementary DNA (cDNA) library using inKN \ from the pancreatic adenocarcinoma cell line 111'\ I . grown as a nude mouse tumor. Through differential screening, we identified a cDNA clone, pIISB, that is homologous to an mRNA expressed at significantly higher levels in HPAF cell...

Journal: :European journal of biochemistry 2001
Y Liang J Li J Chen C C Wang

Thermodynamics of the refolding of denatured D-glyceraldehyde 3-phosphate dehydrogenase (GAPDH) assisted by protein disulfide isomerase (PDI), a molecular chaperone, has been studied by isothermal microcalorimetry at different molar ratios of PDI/GAPDH and temperatures using two thermodynamic models proposed for chaperone-substrate binding and chaperone-assisted substrate folding, respectively....

2013
Congcong Wang Chunzhou Han Tao Li Dehao Yang Xiaojiong Shen Yinxin Fan Yang Xu Wenli Zheng Chenzhong Fei Lifang Zhang Feiqun Xue

In mammalian cells, GAPDH (glyceraldehyde-3-phosphate dehydrogenase) has recently been shown to be implicated in numerous apoptotic paradigms, especially in neuronal apoptosis, and has been demonstrated to play a vital role in some neurodegenerative disorders. However, this phenomenon has not been reported in protists. In the present study, we report for the first time that such a mechanism is ...

Journal: :The Journal of biological chemistry 2009
Jenny Erales Sabrina Lignon Brigitte Gontero

A new role is reported for CP12, a highly unfolded and flexible protein, mainly known for its redox function with A(4) glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Both reduced and oxidized CP12 can prevent the in vitro thermal inactivation and aggregation of GAPDH from Chlamydomonas reinhardtii. This mechanism is thus not redox-dependent. The protection is specific to CP12, because other ...

Journal: :Biological chemistry 2015
Thomas Hildebrandt Johannes Knuesting Carsten Berndt Bruce Morgan Renate Scheibe

Cytosolic glyceraldehyde 3-phosphate dehydrogenase (GAPDH, E.C. 1.2.1.12) is present in all organisms and catalyzes the oxidation of triose phosphate during glycolysis. GAPDH is one of the most prominent cellular targets of oxidative modifications when reactive oxygen and nitrogen species are formed during metabolism and under stress conditions. GAPDH harbors a strictly conserved catalytic cyst...

Journal: :Microbiology 2001
M L Delgado J E O'Connor I Azorín J Renau-Piqueras M L Gil D Gozalbo

The authors show that the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) of Saccharomyces cerevisiae, previously thought to be restricted to the cell interior, is also present in the cell wall. GAPDH activity, proportional to cell number and time of incubation, was detected in intact wild-type yeast cells. Intact cells of yeast strains containing insertion mutations in each ...

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