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The structure of calcium pumps found in the sarcoplasmic reticulum of skeletal muscle was elucidated in 2000 by Toyoshima, et al. using microscopy of tubular crystals and 3D microcrystals. The pump has a molecular mass of 110,000 amu , shows three well separated cytoplasmic domains , with a transmembrane domain consisting of ten alpha helices ...
Valproic acid has a black box warning for hepatotoxicity, pancreatitis, and fetal abnormalities. [4] There is evidence that valproic acid may cause premature growth plate ossification in children and adolescents, resulting in decreased height. [36] [37] [38] Valproic acid can also cause mydriasis, a dilation of the pupils. [39]
Liver failure; Pancreatitis (these two usually occur in first 6 months and can be fatal); Leukopenia (low white blood cell count); Neutropenia (low neutrophil count); Pure red cell aplasia
Calcium tends to have a slightly lower affinity for PMCA pumps than for SERCA pumps. [9] It is thought that the PMCA pump has 10 segments that cross the plasma membrane, with both C and N termini on the inside of the cell. [2] At the C terminus, there is a long "tail" of between 70 and 200 amino acids in length. [2]
Plasma membrane calcium-transporting ATPase 1 also known as Plasma membrane calcium pump isoform 1 is a plasma membrane Ca 2+ ATPase , an enzyme that in humans is encoded by the ATP2B1 gene . [ 5 ] [ 6 ] It's a transport protein , a translocase , a calcium pump EC 7.2.2.10 .
Rendered image of the Ca 2+ pump. Plasma membrane Ca 2+ ATPase (PMCA) is a transport protein in the plasma membrane of cells that serves to remove calcium (Ca 2+) from the cell. It is vital for regulating the amount of Ca 2+ within cells. [3] In fact, the PMCA is involved in removing Ca 2+ from all eukaryotic cells. [4]
Minor limb malformations seen after valproate exposure. Fetal valproate spectrum disorder (FVSD), previously known as fetal valproate syndrome (FVS), is a rare disease caused by prenatal exposure to valproic acid (VPA), a medication commonly used to treat epilepsy, bipolar disorder, and migraines.
The P-type ATPases, also known as E 1-E 2 ATPases, are a large group of evolutionarily related ion and lipid pumps that are found in bacteria, archaea, and eukaryotes. [1] P-type ATPases are α-helical bundle primary transporters named based upon their ability to catalyze auto- (or self-) phosphorylation (hence P) of a key conserved aspartate residue within the pump and their energy source ...