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Data show that LINC00963 (MetaLnc9) interacted with the glycolytic kinase PGK1 and prevented its ubiquitination in non-small cell lung cancer (NSCLC) cells, leading to activation of the oncogenic AKT (show AKT1 Proteins)/mTOR (show FRAP1 Proteins) signaling pathway.
Acetylated PGK1 binds to and phosphorylates Beclin1 (show BECN1 Proteins) at S30 (show FAU Proteins), leading to activation of the VPS34 (show PIK3C3 Proteins)-Beclin1 (show BECN1 Proteins) complex to initiate autophagosomal formation.
Data suggest that, in breast cancer cells, MYC (show MYC Proteins) acts as an upstream regulator leading to PGK1 activation. (MYC (show MYC Proteins), proto-oncogene c-myc (show MYC Proteins); PGK1, phosphoglycerate kinase 1)
PGK1, a glycolytic enzyme catalyzing the conversion of 3-phosphoglycerate into 2-phosphoglycerate, has increased expression in synovial tissues and blood of rheumatoid arthritis, which may be involved in pro-inflammation and synovial hyperplasia of the disease
In neuroblastoma (show ARHGEF16 Proteins) cells, CAIX (show CA9 Proteins) and PGK1 expression is up regulated under hypoxia and correlates with response to targeted anti-proliferative treatment.
Mitochindrial PGK1 acts as a protein kinase in coordinating glycolysis and the tricarboxylic acid cycle, which is instrumental in cancer metabolism and tumorigenesis.
PI3K (show PIK3CA Proteins)/AKT (show AKT1 Proteins)/mTOR (show FRAP1 Proteins) pathway regulates HDAC3 (show HDAC3 Proteins) S424 phosphorylation, which promotes HDAC3 (show HDAC3 Proteins)-PGK1 interaction and PGK1 K220 deacetylation
Retinal dystrophy (show MERTK Proteins) may be one of the clinical manifestations of phosphoglycerate kinase deficiency.
Results show that PGK1 mRNA and protein expression were significantly increased in breast cancer tissues and can be considered as a prognostic biomarker of chemoresistance to paclitaxel treatment in breast cancer.
Suppression of PGK1 enhanced the radiosensitivity of U251 xenografts and suggest that PGK1 may serve as a useful target in the treatment of radioresistant glioma.
present in, and accounts for, glycolysis and glutamate (show GRIN2A Proteins) accumulation into synaptic vesicles
Pgk1 overexpression, or treatment with terazosin (an FDA-approved small molecule that binds and activates Pgk1), rescued motor axon phenotypes in SMA zebrafish. We conclude that global bioenergetics pa (show SMN1 Proteins)thways can be therapeutically manipulated to ameliorate SMA motor neuron phenotypes in vivo.
Phosphoglycerate kinase is a moonlighting protein that functions as both a glycolytic enzyme and a disulfide reductase (show GSR Proteins).
Purification and characterization of 3-phosphoglycerate kinase from Ehrlich ascites carcinoma cells
PGK domain movement and catalysis is regulated by a spring-loaded release mechanism
Results indicate that COX-2 suppression by PGK-1 is independent of its catalytic activity.
Together, these data suggest that PGK1 secreted by PCa (show ENPP1 Proteins) regulates bone formation at the metastatic site by increasing osteoblastic activity, decreasing osteoclastic function, and expressing an osteoblastic phenotype by PCa (show ENPP1 Proteins) cells.
Heterozygous for the X-linked pgk-1a and pgk-1b. Clonally heterotypic glands with inactive X-specific methylation were present in the adult murine stomach.
Pgk1 is strongly expressed in the developing tooth germ of the mouse lower first molar.
Findings indicate that overexpression of PGK-1 in LLC-1 reduces the COX-2 expression, and, in turn, affect PGE2, cell invasion, angiogenesis, and the immune functions, and finally inhibit the tumor progression.
targeting of a single bioenergetic protein, phosphoglycerate kinase 1 (Pgk1), was found to modulate motor neuron vulnerability in vivo. Knockdown of pgk1 alone was sufficient to partially mimic the SMA (show SMN1 Proteins) phenotype in wild-type zebrafish
PGK1 (phosphoglycerate kinase 1) interacts with AtFtsZ2 in planta, suggesting a possible role in FtsZ phosphorylation.
The protein encoded by this gene is a glycolytic enzyme that catalyzes the conversion of 1,3-diphosphoglycerate to 3-phosphoglycerate. The encoded protein may also act as a cofactor for polymerase alpha. This gene lies on the X-chromosome, while a related pseudogene also has been found on the X-chromosome and another on chromosome 19.
phosphoglycerate kinase 1
, PRP 2
, cell migration-inducing gene 10 protein
, primer recognition protein 2
, phosphoglycerate kinase