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MiR-135 targets phosphofructokinase-1 in the ancreatic ductal adenocarcinoma cells.
KLK6 may be the key protease involved in the proteolytic modification of PFK-M.
Data indicate that 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase3 (PFKFB3) and phosphofructokinase (PFK1) expression allows discrimination between induced pluripotent stem cells (iPS) and cancer stem cells (CSCs).
characterize three PFK1 mutations and show they have distinct effects on allosteric regulation of PFKP activity and lactate production.
Gene-based analysis identified an association between breast cancer and the phosphofructokinase-muscle (PFKM) gene on chromosome 12q13.11 that met the genome-wide gene-based threshold of 2.5 x 10(-6).
insulin/phosphofructokinase (PFKM), overlaps with an expression quantitative trait loci
Asp(543)Ala, a naturally occurring Tarui disease-causing mutation in the activating binding site, causes an increased efficacy of ATP at the inhibitory allosteric binding site.
Molecular genetic findings demonstrated the absence of specific genotype-phenotype correlations in PFKM gene mutations.
eukaryotic Pfk did not evolve from prokaryotic ancestors, reciprocal linkage of functionally opposed allosteric binding sites must have developed independently in prokaryotic and eukaryotic Pfk (convergent evolution).
Posttranslational modification of PFK1 enzyme might be the pivotal factor of deregulated glycolytic flux in tumors
Data indicate that substitution of residue at the citrate-binding site (D591V) of PFK-M resulted in the complete loss of activity.
Glycolytic efficiency, which is important for the survival of cancer cells, depends primarily on the preferential expression of PFK-L over the M and P isoforms.
Identification of novel PFK-M transcripts in the testis and embryo.
Two phosphofructokinase (PFK) chimeras were constructed by exchanging the N- and C-terminal halves of the mammalian M- and C-type isozymes.
Using shotgun mass spectrometry, we found this protein differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
insulin, the most known regulator of glucose consumption, specifically regulates the expression of PFKL and PFKM, which impact the regulation of glycolysis in the cell.
This study demonstrated that the reveal PFK-1 as an important regulator of neurogenesis.
These results reveal a novel role of NRX in the regulation of PFK1 activity and in the balance between glycolysis and the pentose phosphate pathway.
Posttranslational modification of PFK1 enzyme might be the pivotal factor of deregulated glycolytic flux in tumors.
HK1S is tethered in the principal piece region by PFKMS, which in turn is bound tightly to GSTM5 in the fibrous sheath of sperm.
Recombinant expression of caveolin-3 affects subcellular localization of PFK-M, by targeting PFK-M to plasma membrane and by trans-locating PFK-M to caveolae-enriched membrane domains. Strictly dependent on the concentration of extracellular glucose.
Sequence analysis of Pfkm gene introns and exons was performed.
The results suggest the importance of phosphofructokinase-M for insulin secretion, although glucokinase is the overall rate-limiting glucose sensor.
Thr-201 phosphorylation of Bad by JNK1 is required for PFK-1 activation
In skeletal muscle, the lack of PFK activity blocked glycolysis and resulted in considerable glycogen storage and low ATP content.
The tissue expression profiles of eGYS1, equine type II hexokinase (eHKII) and muscle-type phosphofructokinase (ePFKM) were determined by real-time PCR and western blot analysis.
Three phosphofructokinase isozymes exist in humans muscle, liver and platelet. These isozymes function as subunits of the mammalian tetramer phosphofructokinase, which catalyzes the phosphorylation of fructose-6-phosphate to fructose-1,6-bisphosphate. Tetramer composition varies depending on tissue type. This gene encodes the muscle-type isozyme. Mutations in this gene have been associated with glycogen storage disease type VII, also known as Tarui disease. Alternatively spliced transcript variants have been described.
, 6-phosphofructokinase, muscle type
, phosphofructo-1-kinase isozyme A
, phosphofructokinase 1
, phosphofructokinase, polypeptide X
, phosphofructokinase 4
, phosphofructokinase-1 A isozyme
, phosphofructokinase-M (connecting peptide)
, 6-phosphofructokinase muscle type
, muscle type phosphofructokinase
, muscle phosphofructokinase
, muscle-type phosphofructokinase
, ATP-dependent 6-phosphofructokinase, muscle type
, phosphofructokinase, muscle S homeolog