نتایج جستجو برای: gapdh real

تعداد نتایج: 531958  

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 ...

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: :Journal of neuroscience methods 2010
Katherine Nelissen Karen Smeets Monique Mulder Jerome J A Hendriks Marcel Ameloot

Quantitative real time polymerase chain reaction (qPCR) has become a widely used tool to examine gene expression levels. Reliable quantification, however, depends on a proper normalization strategy. Normalization with multiple reference genes is becoming the standard, although the most suitable reference genes depend on the applied treatment as well as the tissue or cell type studied. In this s...

2015
Sung Han Kim Weon Seo Park Sang Jin Lee Moon Kyung Choi Seung Min Yeon Jeong Nam Joo Ara Ko Eun Sik Lee Jae Young Joung Ho Kyung Seo Jinsoo Chung Kang Hyun Lee

The study quantified the relative absolute PSCA level in relation to the glyceraldehyde 3-phosphate dehydrogenase (GAPDH) level in the peripheral blood of 478 hormone-naive prostate cancer (PC) patients who underwent radical prostatectomy from 2005 to 2012 and evaluated its prognostic significance as a risk factor for predicting biochemical recurrence (BCR), compared to known parameters. Nested...

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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