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CYB5R3 encodes cytochrome b5 reductase, which includes a membrane-bound form in somatic cells (anchored in the endoplasmic reticulum, mitochondrial and other membranes) and a soluble form in erythrocytes. Zusätzlich bieten wir Ihnen Cytochrome B5 Reductase 3 Antikörper (136) und Cytochrome B5 Reductase 3 Proteine (16) und viele weitere Produktgruppen zu diesem Protein an.
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Data suggest that cytochrome b5 (CYB5 (zeige CYB5A ELISA Kits)) and cytochrome b5 reductase 3 (CYB5R3) can reduce human cytoglobin (CYGB (zeige CYGB ELISA Kits)) and zebrafish cytoglobins at rates up to 250-fold higher than those reported for the known physiological substrates, hemoglobin (zeige HBB ELISA Kits) and myoglobin (zeige MB ELISA Kits); the three proteins (CYB5 (zeige CYB5A ELISA Kits)+CYB5R3+CYGB (zeige CYGB ELISA Kits)) appear to constitute a metabolon involved in generation of nitric oxide.
CYB5R3 promotes colonization and metastasis formation and is a prognostic marker of disease-free and overall survival in estrogen receptor (zeige ESR1 ELISA Kits)-negative breast cancer.
Variants in CYB5A (zeige CYB5A ELISA Kits) and CYB5R3 should be considered in the evaluation of breast cancer risk in African American women.
Genetic variation in CYB5R3 is associated with methemoglobin levels in preterm infants receiving nitric oxide therapy.
The results unveil a potential mechanism of action by which CYB5R3 deficiency contributes to the pathophysiological underpinnings of neurological disorders in RHM patients.
Dapsone-associated methemoglobinemia in a patient with slow NAT2*5B haplotype and impaired cytochrome b5 reductase activity
A comprehensive overview of the study of structure and function of human cytochrome b5 reductase.
Data indicate that mitochondrial amidoxime reducing components 1 and 2 together with the electron transport proteins NADH-cytochrome b5 reductase (CYB5R) and cytochrome b5 (CYB5 (zeige CYB5A ELISA Kits)) catalyze the reduction of N-hydroxylated compounds such as amidoximes.
Population frequency and age of c.806C > T mutation in CYB5R3 gene as cause of recessive congenital methemoglobinemia in Yakutia.
Novel large deletion c.22-1320_633+1224del in the CYB5R3 gene from patients with hereditary methemoglobinemia
Nucleation is achieved by a mechanism involving APC (zeige APC ELISA Kits)-B dimerization and recruitment of multiple actin monomers. Further, APC (zeige APC ELISA Kits)-B nucleation activity is synergistic with its in vivo binding partner, the formin (zeige FMN1 ELISA Kits) mDia1
an N-terminal domain spanning residues 129-369(DID) is sufficient for auto-inhibition, but alone is not sufficient for RhoA (zeige RHOA ELISA Kits) relief of auto-inhibition, suggesting that sequences N-terminal to DID are important to RhoA (zeige RHOA ELISA Kits) binding.
Dia1 is required for the formation of the actin coat around endosomes downstream of RhoB, connecting membrane trafficking with the regulation of actin dynamics.
Dia1 and IQGAP1 (zeige IQGAP1 ELISA Kits) interact in cell migration and phagocytic cup formation.
This gene encodes cytochrome b5 reductase, which includes a membrane-bound form in somatic cells (anchored in the endoplasmic reticulum, mitochondrial and other membranes) and a soluble form in erythrocytes. The membrane-bound form exists mainly on the cytoplasmic side of the endoplasmic reticulum and functions in desaturation and elongation of fatty acids, in cholesterol biosynthesis, and in drug metabolism. The erythrocyte form is located in a soluble fraction of circulating erythrocytes and is involved in methemoglobin reduction. The membrane-bound form has both membrane-binding and catalytic domains, while the soluble form has only the catalytic domain. Alternate splicing results in multiple transcript variants. Mutations in this gene cause methemoglobinemias.
NADH-cytochrome b5 reductase 3
, NADH-cytochrome b5 reductase 3 membrane-bound form
, NADH-cytochrome b5 reductase 3 soluble form
, Diaphorase (NADH) (cytochrome b-5 reductase)
, diaphorase 1
, diaphorase 1 (NADH)
, NADH-cytochrome b5 reductase
, cytochrome b5 reductase 3