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The results suggest that this N-glycan of POFUT1 is not required for its proper enzymatic function, and that the p.Ser162Leu mutation of POFUT1 likely causes global developmental delay, microcephaly with vascular and cardiac defects.
Our findings suggested that overexpression of Pofut1 and activated Notch1 (zeige NOTCH1 Proteine) signaling may be associated with a poor prognosis in breast cancer.
POFUT1 gene expression in gastric cancer
POFUT1, POGLUT1 (zeige POGLUT1 Proteine) and ADAM10 (zeige ADAM10 Proteine) are processing enzymes that are involved in different steps of Notch (zeige NOTCH1 Proteine) receptor activation in the epidermis; the roles of these unique enzymes in a single pathway may explain both the overlapping and distinct clinical features of DDD (zeige KRT5 Proteine) and RAK (zeige FRK Proteine) patients
High expression of POFUT1 correlates with aggressive clinicopathological characteristics and poor prognosis of hepatocellular carcinoma patients.
The upregulation of poFUT1 by LIF (zeige LIF Proteine) facilitated trophoblast cell migration and invasion through activating the PI3K (zeige PIK3CA Proteine)/Akt (zeige AKT1 Proteine) signaling pathway.
Silencing of Pofut1 expression exerted antiproliferative and antiadhesive effects on hepatocytes.
Only a novel 1-bp deletion (c.246+5delG) in POFUT1 was found in a Chinese family with Dowling-Degos disease (DDD (zeige KRT5 Proteine)). No other novel mutation or this deletion was detected in POFUT1 in a second DDD (zeige KRT5 Proteine) family and a sporadic DDD (zeige KRT5 Proteine) case by Sanger Sequencing.
Identification of six pathogenic POFUT1 mutations in Dowling-Degos disease patients of different ethnic origin.
POFUT1 expression can contribute to cancer progression and that POFUT1 may serve as a diagnostic marker and a therapeutic target for OSCCs.
POFUT1 inactivation disrupts angiogenic signaling events and results in excessive angiogenic cell proliferation and plexus formation, leading to anomalous coronary arteries, myocardial infarction and heart failure.
both wild-type and mutant Pofut1 proteins were degraded through lysosome dependent machinery. Pofut1 protein loss in the point mutant embryos caused the same phenotypes as those observed in Pofut1 null embryos
The POFUT1 binds EGF (zeige EGF Proteine)-like domains of the hEGF type and that the highly correlated presence of POFUT1 and fucosylatable hEGFs has accompanied animal evolution.
Loss of Pofut1 expression is associated with Muscle Aging-Related Phenotypes.
results demonstrated that POFUT1-mediated O-fucosylation of NOTCH (zeige NOTCH1 Proteine) receptors regulates myogenic cell differentiation and affects postnatal muscle growth in mice
results establish the critical role of Pofut1 on Notch (zeige NOTCH1 Proteine) pathway activation during myogenic differentiation
mDLL1 O-fucosylation by POFUT1 is dispensable for ligand function
Loss of Pofut1 is associated with myeloid hyperplasia and impaired lymphopoiesis.
Pofut1 and O-fucose have roles in mammalian Notch (zeige NOTCH1 Proteine) signaling
Pofut1 is required for Notch (zeige NOTCH1 Proteine) signaling upstream of NICD1.
This gene encodes a member of the glycosyltransferase O-Fuc family. This enzyme adds O-fucose through an O-glycosidic linkage to conserved serine or threonine residues in the epidermal growth factor-like repeats of a number of cell surface and secreted proteins. O-fucose glycans are involved in ligand-induced receptor signaling. Alternative splicing of this gene results in two transcript variants encoding different isoforms.
GDP-fucose protein O-fucosyltransferase 1
, putative protein-O-fucosyltransferase
, peptide-O-fucosyltransferase 1
, protein-O-fucosyltransferase 1
, protein O-fucosyltransferase 1
, o-fucosyltransferase protein