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we detected ALDOA somatic promoter mutations in two cases
Low ALDOA expression promotes invasion of colorectal cancer.
Aldolase A (ALDOA) knockdown reduced cyclin D1 expression by regulating epidermal growth factor receptor/mitogen-activated protein kinase (EGFR/MAPK) pathway.
Results showed that ALDOA was upregulated in renal cell carcinoma (RCC) samples and cell lines and significantly associated with metastasis and survival. Overall, data revealed that ALDOA functions as a tumor promoter, plays a prominent role in proliferation, migration, and invasion of RCC cells with high expression, and may promote EMT and activate the Wnt/betacatenin signaling pathway.
The results indicate that ALDOA and PGK1 may indicate resistance to cisplatin in osteosarcoma
Knockdown of ALDOA in QBC939 and RBE cells attenuated the cell proliferation and induced a higher apoptosis rate.
Silencing aldolase A suppressed colon cancer cell proliferation and invasion and inhibited the epithelial-mesenchymal transition phenotype. Aldolase A protein expression in colon cancer was related to tumor location, tumor clinical stage and survival.
mir-122 and its targets G6PC3, ALDOA and CS play roles in the hypoxia responses that regulate glucose and energy metabolism and can serve as hypoxia biomarkers.
Aldolase A promotes lung cancer metastasis via PHD-mediated stabilization of HIF-1alpha and the subsequent activation of MMP9.
Findings show that ALDOA expression is up-regulated in colorectal cancer (CRC) and is a hypoxia-inducible prognostic factor that is closely related to CRC malignancy.
Overexpression of ALDOA is associated with colorectal cancer.
In vitro and in vivo results demonstrated that ALDOA was associated with proliferation and metastasis of pancreatic cancer cells.
Study shows that PI3K directly coordinates glycolysis with cytoskeletal dynamics in an AKT-independent manner. Growth factors or insulin stimulate the PI3K-dependent activation of Rac, leading to disruption of the actin cytoskeleton, release of filamentous actin-bound aldolase A, and an increase in aldolase activity.
Our results expand the clinical spectrum of aldolase A deficiency to isolated temperature-dependent rhabdomyolysis, and suggest that thermolability may be tissue specific. We also propose a treatment for this severe disease
Study provides evidence supporting a critical functional role of ALDOA in osteosarcoma progression, metastasis and perhaps chemoresistance.
ALDOC, Aldolase A (ALDOA) and Aldolase B (ALDOB) activate Wnt signaling.
ALDOA is highly expressed in lung squamous cell carcinoma (LSCC) and its expression level is correlated with LSCC metastasis, grades, differentiation status and poor prognosis.
The expression of ALDOA and/or SULT1A3 is significantly higher.
The results presented here point to ALDA as a factor involved in the regulation of cells proliferation.
The new prognostic biomarkers GRP78, Fructose-bisphosphate Aldolase A (ALDOA), Carbonic Anhydrase I (CA1) and Peptidyl-prolyl cis-trans isomerase A or Cyclophilin A (PPIA)) provided good survival prediction for TNM stage I-IV patients.
Aldolase inhibits WASP/Arp2/3-dependent actin polymerization in vitro
The lattice of muscle aldolase contacts corresponded to an increased number of interactions between high-entropy side chains that mitigate the lattice strain incurred upon cryocooling and accompanying mosaic spread increases.
kinetic and structural analyses of fructose-bisphosphate aldolase
The protein encoded by this gene, Aldolase A (fructose-bisphosphate aldolase), is a glycolytic enzyme that catalyzes the reversible conversion of fructose-1,6-bisphosphate to glyceraldehyde 3-phosphate and dihydroxyacetone phosphate. Three aldolase isozymes (A, B, and C), encoded by three different genes, are differentially expressed during development. Aldolase A is found in the developing embryo and is produced in even greater amounts in adult muscle. Aldolase A expression is repressed in adult liver, kidney and intestine and similar to aldolase C levels in brain and other nervous tissue. Aldolase A deficiency has been associated with myopathy and hemolytic anemia. Alternative splicing and alternative promoter usage results in multiple transcript variants. Related pseudogenes have been identified on chromosomes 3 and 10.
, fructose-bisphosphate aldolase A
, lung cancer antigen NY-LU-1
, muscle-type aldolase
, aldolase A, fructose-bisphosphate
, aldolase 1, A isoform
, aldolase C
, aldolase a, fructose-bisphosphate, b