Results 51 to 60 of about 171,288 (210)

A novel small-molecule inhibitor of 3-phosphoglycerate dehydrogenase. [PDF]

Mol Cell Oncol, 2016
Serine metabolism is likely to play a critical role in cancer cell growth. A recent study reports the identification of a novel small-molecule inhibitor of serine synthesis that targets 3-phosphoglycerate dehydrogenase (PHGDH), the first enzyme of the serine synthesis pathway, and selectively abrogates the proliferation of PHGDH overexpressing breast ...
Mullarky E, Lairson LL, Cantley LC, Lyssiotis CA.   +3 more
europepmc   +6 more sources

Phosphoglycerate dehydrogenase diverts glycolytic flux and contributes to oncogenesis [PDF]

Nature Genetics, 2011
Most tumors exhibit increased glucose metabolism to lactate, however, the extent to which glucose-derived metabolic fluxes are used for alternative processes is poorly understood. Using a metabolomics approach with isotope labeling, we found that in some cancer cells a relatively large amount of glycolytic carbon is diverted into serine and glycine ...
Locasale, Jason W., Grassian, Alexandra R., Melman, Tamar, Lyssiotis, Costas A., Mattaini, Katherine Ruth, Bass, Adam J., Heffron, Gregory J., Metallo, Christian M., Muranen, Taru, Sharfi, Hadar, Sasaki, Atsuo T., Anastasiou, Dimitrios, Mullarky, Edouard, Vokes, Natalie I., Sasaki, Mika, Beroukhim, Rameen, Stephanopoulos, Gregory, Ligon, Azra H., Meyerson, Matthew L., Richardson, Andrea L., Chin, Lynda, Wagner, Gerhard, Asara, John M., Brugge, Joan S., Cantley, Lewis C., Vander Heiden, Matthew G.   +25 more
openaire   +4 more sources

Proteomics analysis of antimalarial targets of Garcinia mangostana Linn.

Asian Pacific Journal of Tropical Biomedicine, 2014
Objective: To investigate possible protein targets for antimalarial activity of Garcinia mangostana Linn. (G. mangostana) (pericarp) in 3D7 Plasmodium falciparum clone using 2-dimensional electrophoresis and liquid chromatography mass-spectrometry (LC/MS/
Wanna Chaijaroenkul, Artitiya Thiengsusuk, Kanchana Rungsihirunrat, Stephen Andrew Ward, Kesara Na-Bangchang   +4 more
doaj   +1 more source

Inhibition of 3-phosphoglycerate dehydrogenase by l-serine [PDF]

Biochemical Journal, 1968
1. l-Serine was shown to be a highly specific inhibitor of 3-phosphoglycerate dehydrogenase. 2. 3-Phosphoglycerate dehydrogenase is cold-labile with respect to its catalytic activity and to sensitivity to serine. 3. l-Serine protects the catalytic site as well as the inhibitor site. 4. Glycerol protects the catalytic site as well as the inhibitor site.
J C, Slaughter, D D, Davies
openaire   +2 more sources

The malate-aspartate shuttle is important for de novo serine biosynthesis

Cell Reports, 2023
Summary: The malate-aspartate shuttle (MAS) is a redox shuttle that transports reducing equivalents across the inner mitochondrial membrane while recycling cytosolic NADH to NAD+.
Melissa H. Broeks, Nils W.F. Meijer, Denise Westland, Marjolein Bosma, Johan Gerrits, Hannah M. German, Jolita Ciapaite, Clara D.M. van Karnebeek, Ronald J.A. Wanders, Fried J.T. Zwartkruis, Nanda M. Verhoeven-Duif, Judith J.M. Jans   +11 more
doaj   +1 more source

Probing Subunit Interactions in 3‐Phosphoglycerate Dehydrogenase

The FASEB Journal, 2012
3‐Phosphoglycerate Dehydrogenase is a homotetramer with three types of subunit interfaces; between adjacent regulatory domains, cofactor domains, and across the central cavity of the tetramer. A single tryptophan per subunit lies at the cofactor interface and crosses over between adjacent subunits.
Falk, Bradley, Bell, Ellis
openaire   +1 more source

The isolation and characterization of 3-phosphoglycerate dehydrogenase from peas [PDF]

Biochemical Journal, 1968
1. 3-Phosphoglycerate dehydrogenase was purified 400-fold from crude extracts of etiolated pea epicotyls. 2. Michaelis constants were determined for all four substrates. 3. Loss of sensitivity to inhibition by l-serine occurs on purification. 4. The purified enzyme is inhibited by thiol-group reagents and, with N-ethyl-maleimide, protection is afforded
J C, Slaughter, D D, Davies
openaire   +2 more sources

Glycerol dehydrogenase: Structure, specificity, and mechanism of a family III polyol dehydrogenase [PDF]

, 2001
Background: Bacillus stearothermophilus glycerol dehydrogenase (GlyDH) (glycerol:NAD+ 2-oxidoreductase, EC 1.1.1.6) catalyzes the oxidation of glycerol to dihydroxyacetone (1,3-dihydroxypropanone) with concomitant reduction of NAD+ to NADH.
Baker PJ, Sveta Sedelnikova, Taylor R, Sedelnikova S, Baker, Patrick J., Rice DW, Muir, Nicola M., Gore, Michael G., Burke J, David W. Rice, Ruzheinikov, Sergey N., Bullough, Per A., Sedelnikova, Sveta, Sergey N. Ruzheinikov, Per A. Bullough, Patrick J. Baker, Gore MG, Burke, Jacky, Michael G. Gore, Muir NM, Bullough PA, Nicola M. Muir, Rice, David W., Robert Taylor, Ruzheinikov SN, Jacky Burke, Taylor, Robert   +26 more
core   +1 more source

Proteomic Analysis of Responsive Proteins Induced in Japanese Birch Plantlet Treated with Salicylic Acid

Proteomes, 2014
The present study was performed to unravel the mechanisms of systemic acquired resistance (SAR) establishment and resistance signaling pathways against the canker-rot fungus (Inonotus obliquus strain IO-U1) infection in Japanese birch plantlet No.8 ...
Hiromu Suzuki, Yuya Takashima, Futoshi Ishiguri, Nobuo Yoshizawa, Shinso Yokota   +4 more
doaj   +1 more source

UFL1‐Mediated UFMylation of ENO1 Restrains Aerobic Glycolysis and Colorectal Cancer Progression

Advanced Science, EarlyView.
UFMylation restrains aerobic glycolysis and colorectal cancer progression by modifying the glycolytic enzyme ENO1. Pharmacological enhancement of the UFL1–ENO1 interaction by the FDA‐approved antibiotic torezolid promotes ENO1 UFMylation, suppresses tumor metabolism, and sensitizes colorectal cancer to chemotherapy, revealing an actionable metabolic ...
Xiuqing Ma, Rui Wan, Yueyuan Zhong, Ziyang Cui, Xuan Zhang, Xiaoqiang He, Rong Wang, Lei Huang, Wan‐Yang Sun, Rong‐Rong He, Yang Zhou, Jianshuang Li, Li Shen, Shao‐Hua Wang, Tongzheng Liu   +14 more
wiley   +1 more source