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Human Polyclonal PKLR Primary Antibody für IHC, IHC (p) - ABIN4345879
Kowalski, Nocon, Gamian, Kołodziej, Rakus: Association of C-terminal region of phosphoglycerate mutase with glycolytic complex regulates energy production in cancer cells. in Journal of cellular physiology 2012
Rabbit Polyclonal PKLR Primary Antibody für IHC (p), IHC - ABIN269613
Jindal, Merchant, Balschi, Zhangand, Koren: Proteomic analyses of transgenic LQT1 and LQT2 rabbit hearts elucidate an increase in expression and activity of energy producing enzymes. in Journal of proteomics 2012
AMPD3 deficiency increases the level of ATP in erythrocytes, but does not improve anemia due to pyruvate kinase deficiency and leads to erythrocyte dysfunction.
Pyruvate kinase deficiency in mice protects against malaria
Gene copy number variation (CNV) of the PKLR, FCGR2A (zeige FCGR2A Antikörper), FCGR2C, and FCGR3 (zeige CD16 Antikörper) genes is associated with malaria severity, and our results provide evidence for a role of CNV in host responses to malaria.
Genotype-phenotype correlations for the novel missense mutations found in the PKLR gene in PK deficiency among Tunisian cases were investigated by three-dimensional structure analysis.
Data show that pyruvate kinase (PK) activity was decreased in the GATA1 (zeige GATA1 Antikörper) hemizygous state and PKLR c.1284delA variant.
An update of PKLR gene mutation database has been presented. (Review)
Two Novel Missense Mutations and a 5bp Deletion in the Erythroid-Specific Promoter of the PKLR Gene in Two Unrelated Patients With Pyruvate Kinase Deficient Transfusion-Dependent Chronic Nonspherocytic Hemolytic Anemia.
PKLR promotes colorectal cancer liver colonization through induction of glutathione synthesis.
Pyruvate kinase variants modulate malaria phenotypes in a Thai population.
661G>A and 1528C>T mutations of PKLR gene are associated with pyruvate kinase deficiency.
Case Report: unknown mutation in the pyruvate kinase gene (PKLR) identified from a neonate with severe jaundice.
This study determined which interactions in the fructose 1,6-bisphosphate binding site of human liver pyruvate kinase contribute to allostery.
The existence of mitochondrial Pyruvate kinase was confirmed by immunological analysis in pig liver mitochondria.
The protein encoded by this gene is a pyruvate kinase that catalyzes the transphosphorylation of phohsphoenolpyruvate into pyruvate and ATP, which is the rate-limiting step of glycolysis. Defects in this enzyme, due to gene mutations or genetic variations, are the common cause of chronic hereditary nonspherocytic hemolytic anemia (CNSHA or HNSHA). Multiple transcript variants encoding different isoforms have been found for this gene.
pyruvate kinase isozymes R/L
, pyruvate kinase, liver and RBC
, Pyruvate kinase isozyme R
, pyruvate kinase isozymes R/L-like
, pyruvate kinase PKLR
, pyruvate kinase isozymes L/R
, R-type/L-type pyruvate kinase
, pyruvate kinase 1
, pyruvate kinase isozyme R/L
, pyruvate kinase type L
, pyruvate kinase, liver and blood cell
, red cell/liver pyruvate kinase
, Pyruvate kinase isozymes R/L
, pyruvate kinase, liver and red blood cell