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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Aug 2016.

Phosphoglycerate mutase 2

Phosphoglycerate Mutase, PGAM-M, muscle-specific phosphoglycerate mutase, PGAM2
Phosphoglycerate mutase (PGAM) catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway. The PGAM is a dimeric enzyme containing, in different tissues, different proportions of a slow-migrating muscle (MM) isozyme, a fast-migrating brain (BB) isozyme, and a hybrid form (MB). This gene encodes muscle-specific PGAM subunit. Mutations in this gene cause muscle phosphoglycerate mutase eficiency, also known as glycogen storage disease X. [provided by RefSeq, Sep 2009] (from NCBI)
Top mentioned proteins: ACID, CAN, fibrillin-1, HAD, Phosphofructokinase-1
Papers on Phosphoglycerate Mutase
Proteome basis for intramuscular variation in color stability of beef semimembranosus.
Rentfrow et al., Lexington, United States. In Meat Sci, Mar 2016
abundance of glycolytic enzymes (fructose-bisphosphate aldolase A, phosphoglycerate mutase 2, and beta-enolase) and phosphatidylethanolamine-binding protein 1 than their OSM counterparts.
Proteomics identification of PGAM1 as a potential therapeutic target for urothelial bladder cancer.
Liu et al., Chengdu, China. In J Proteomics, Mar 2016
Among them, phosphoglycerate mutase 1 (PGAM1), significantly up-regulated in UBC, was selected for detailed analysis.
The network of surface-displayed glycolytic enzymes in Mycoplasma pneumoniae and their interactions with human plasminogen.
Dumke et al., Dresden, Germany. In Infect Immun, Jan 2016
Eight glycolytic enzymes, pyruvate dehydrogenase A-C (PdhA-C), glyceraldehyde-3-phosphate dehydrogenase (GapA), lactate dehydrogenase (Ldh), phosphoglycerate mutase (Pgm), pyruvate kinase (Pyk) and transketolase (Tkt), were confirmed as surface-expressed and all are able to interact with plasminogen.
Monoclonal 1- and 3-Phosphohistidine Antibodies: New Tools to Study Histidine Phosphorylation.
Hunter et al., Los Angeles, United States. In Cell, Aug 2015
Assays based on the isomer-specific autophosphorylation of NME1 and phosphoglycerate mutase were used with immunoblotting and sequencing IgG variable domains to screen, select, and characterize anti-1-pHis and anti-3-pHis mAbs.
[Agrobacterium tumefaciens-mediated transformation of Aureobasidium pullulans and high-efficient screening for polymalic acid producing strain].
Zou et al., In Sheng Wu Gong Cheng Xue Bao, Jul 2015
A high-titer PMA mutant H27 was obtained, giving a good PMA production caused by the disruption of phosphoglycerate mutase, that increased by 24.5% compared with the control.
Dysregulated glycolysis as an oncogenic event.
Kondoh et al., Kyoto, Japan. In Cell Mol Life Sci, May 2015
Furthermore, several regulators of glycolysis have been recently identified as oncogene candidates, including the hypoxia-inducible factor pathway, sirtuins, adenosine monophosphate-activated kinase, glycolytic pyruvate kinase M2, phosphoglycerate mutase, and oncometabolites.
Kinetic and thermodynamic characterization of the interactions between the components of human plasma kinin-forming system and isolated and purified cell wall proteins of Candida albicans.
Rapala-Kozik et al., Kraków, Poland. In Acta Biochim Pol, 2014
Five of these fungal proteins, including agglutinin-like sequence protein 3 (Als3), triosephosphate isomerase 1 (Tpi1), enolase 1 (Eno1), phosphoglycerate mutase 1 (Gpm1) and glucose-6-phosphate isomerase 1 (Gpi1), were purified and characterized in terms of affinities to the human contact factors, using the surface plasmon resonance measurements.
The role of phosphoglycerate mutase 1 in tumor aerobic glycolysis and its potential therapeutic implications.
Ren et al., Tianjin, China. In Int J Cancer, 2014
A significant characteristic of cancer cell metabolism is the high level of aerobic glycolysis with high glucose consumption and lactate production.
Stress eating and tuning out: cancer cells re-wire metabolism to counter stress.
Dang et al., Philadelphia, United States. In Crit Rev Biochem Mol Biol, 2013
The key glycolytic enzymes phosphofructokinase-1 (PFK1), pyruvate kinase (PKM2) and phosphoglycerate mutase 1 (PGAM1) are regulated by upstream and downstream metabolites to balance glycolytic flux with flux through anabolic pathways.
Connections between various trigger factors and the RIP1/ RIP3 signaling pathway involved in necroptosis.
Liu et al., Bengbu, China. In Asian Pac J Cancer Prev, 2012
Necroptosis exhibits a unique signaling pathway that requires the involvement of receptor interaction protein kinases 1 and 3 (RIP1 and RIP3), mixed lineage kinase domain-like (MLKL), and phosphoglycerate mutase 5 (PGAM5) and can be specifically inhibited by necrostatins.
Advances in the proteomic discovery of novel therapeutic targets in cancer.
Wang et al., Atlanta, United States. In Drug Des Devel Ther, 2012
A number of potential drug targets, such as baculoviral inhibitor of apoptosis protein repeat-containing protein 6, macrophage inhibitory cytokine 1, phosphoglycerate mutase 1, prohibitin 1, fascin, and pyruvate kinase isozyme 2 were identified in the proteomic analysis of drug-resistant cancer cells, drug action, and differential disease state tissues.
Phosphoglycerate mutase 1 coordinates glycolysis and biosynthesis to promote tumor growth.
Chen et al., Atlanta, United States. In Cancer Cell, 2012
We found that the glycolytic enzyme phosphoglycerate mutase 1 (PGAM1), commonly upregulated in human cancers due to loss of TP53, contributes to biosynthesis regulation in part by controlling intracellular levels of its substrate, 3-phosphoglycerate (3-PG), and product, 2-phosphoglycerate (2-PG).
Evidence for an alternative glycolytic pathway in rapidly proliferating cells.
Cantley et al., Boston, United States. In Science, 2010
We demonstrate that phosphoenolpyruvate (PEP), the substrate for pyruvate kinase in cells, can act as a phosphate donor in mammalian cells because PEP participates in the phosphorylation of the glycolytic enzyme phosphoglycerate mutase (PGAM1) in PKM2-expressing cells.
Target discovery in small-molecule cell-based screens by in situ proteome reactivity profiling.
Cravatt et al., Los Angeles, United States. In Nat Biotechnol, 2005
In situ proteome reactivity profiling revealed that MJE3, but not other library members, covalently labeled the glycolytic enzyme phosphoglycerate mutase 1 (PGAM1), resulting in enzyme inhibition.
Human muscle phosphoglycerate mutase deficiency: newly discovered metabolic myopathy.
Friedman et al., In Science, 1981
Muscle phosphoglycerate mutase activity was decreased (5.7 percent of the lowest control value) in a 52-year-old man with intolerance for strenuous exercise and recurrent pigmenturia since adolescence.
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