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PGAM1 correlates with spermatogenic dysfunction and affects the function of cell proliferation, apoptosis and migration.
9630033F20Rik (show C12orf5 ELISA Kits) may play an important role in muscle wasting and that it has a distinguished characterization of gene network.[9630033F20Rik (show C12orf5 ELISA Kits)]
histidine-phosphorylated PGAM1 correlated with expression of PKM2 in tumor tissues; decreased pyruvate kinase activity in PKM2-expressing cells allows PEP-dep (show PREP ELISA Kits)endent histidine phosphorylation of PGAM1 and may provide an alternate glycolytic pathway
PGAM1 may be associated with the grade of glioma and be involved in the biological behavior of glioma cells. PGAM1 might be a novel therapeutic target in glioma.
Our finding showed that PGAM1 might serve as a promising therapeutic target for UBC (show RPS27A ELISA Kits).
PGAM1 is highly expressed in clear cell renal cell carcinoma and correlated with clinicalpathological features, which may contribute to tumor formation and progression.
PGAM is acetylated at lysines 100/106/113/138 in its central region, and a member of the Sirtuin (show SIRT1 ELISA Kits) family (class III deacetylase), SIRT2 (show SIRT2 ELISA Kits), is responsible for its deacetylation.
Tyrosine26 phosphorylation represents an additional acute mechanism underlying phosphoglycerate mutase 1 upregulation.
Phosphoglycerate mutase 1 (PGAM1) contributes to biosynthesis regulation by controlling intracellular levels of its substrate, 3-phosphoglycerate (3-PG), and product, 2-phosphoglycerate (2-PG).
PGAM1 deacetylation and activity are directly controlled by Sirt1 (show SIRT1 ELISA Kits).
histidine-phosphorylated PGAM1 correlated with expression of PKM2 in cancer cell lines; decreased pyruvate kinase activity in PKM2-expressing cells allows PEP (show PAEP ELISA Kits)-dependent histidine phosphorylation of PGAM1 and may provide an alternate glycolytic pathway
Our studies suggested that PGAM1 plays an important role in hepatocarcinogenesis
Phosphoglyceric acid mutase (EC 22.214.171.124) is widely distributed in mammalian tissues where it catalyzes the reversible reaction of 3-phosphoglycerate (3-PGA) to 2-phosphoglycerate (2-PGA) in the glycolytic pathway (summary by Chen et al., 1974
phosphoglycerate mutase 1 (brain)
, phosphoglycerate mutase 1
, uncharacterized protein LOC706211
, BPG-dependent PGAM 1
, phosphoglycerate mutase isozyme B
, phosphoglycerate mutase A, nonmuscle form