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Human PGAM1 Protein expressed in Wheat germ - ABIN1314779
Kimura, Sakurai, Koumura, Yamada, Hayashi, Tanaka, Hozumi, Tanaka, Takemura, Seishima, Inuzuka: High prevalence of autoantibodies against phosphoglycerate mutase 1 in patients with autoimmune central nervous system diseases. in Journal of neuroimmunology 2010
High PGAM1 expression is associated with Pancreatic Ductal Adenocarcinoma Metastasis.
conformation and dynamics of the C-terminal region in human phosphoglycerate mutase 1
When BPGM is knocked out, 1,3-BPG can directly phosphorylate PGAM1. In this case, PGAM1 phosphorylation and activity are decreased, but nevertheless sufficient to maintain normal glycolytic flux and cellular growth rate.
study provided the first evidence revealing a non-metabolic function of PGAM1 in promoting cell migration, and gained new insights into the role of PGAM1 in cancer progression.
Data show that tyrosine 26 phosphorylation enhances the binding of phosphoglycerate mutase 1 (PGAM1) to its substrates through generating electrostatic environment and structural features that are advantageous to the binding.
PGAM1 in promoting homologous recombination repair in tumor cell lines. Suggest potential therapeutic opportunity for PGAM1 inhibitors in combination with PARP inhibitors in cancer treatment.
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.
PGAM1 correlates with spermatogenic dysfunction and affects the function of cell proliferation, apoptosis and migration.
Our finding showed that PGAM1 might serve as a promising therapeutic target for UBC.
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 family (class III deacetylase), SIRT2, 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.
histidine-phosphorylated PGAM1 correlated with expression of PKM2 in cancer cell lines; decreased pyruvate kinase activity in PKM2-expressing cells allows PEP-dependent histidine phosphorylation of PGAM1 and may provide an alternate glycolytic pathway
Our studies suggested that PGAM1 plays an important role in hepatocarcinogenesis
This protein has been found differentially expressed in thalami from patients with schizophrenia.
Results identified phosphoglycerate mutase 1 that showed elevated levels of protein carbonyls in inferior parietal lobule (IPL) from subjects with early stage-Alzheimer's disease.
Cloning, purification, crystallization and preliminary crystallographic analysis of human phosphoglycerate mutase
Phosphoglycerate mutase may have a role in preventing non-spherocytic anemia [case report]
9630033F20Rik may play an important role in muscle wasting and that it has a distinguished characterization of gene network.[9630033F20Rik]
histidine-phosphorylated PGAM1 correlated with expression of PKM2 in tumor tissues; decreased pyruvate kinase activity in PKM2-expressing cells allows PEP-dependent histidine phosphorylation of PGAM1 and may provide an alternate glycolytic pathway
Phosphoglyceric acid mutase (EC 18.104.22.168) 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
BPG-dependent PGAM 1
, phosphoglycerate mutase 1
, phosphoglycerate mutase A, nonmuscle form
, phosphoglycerate mutase isozyme B
, phosphoglycerate mutase 1 (brain)
, uncharacterized protein LOC706211
, bisphosphoglycerate mutase 1a