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The protein encoded by DPAGT1 is an enzyme that catalyzes the first step in the dolichol-linked oligosaccharide pathway for glycoprotein biosynthesis. De plus, nous expédions Dolichyl-Phosphate (UDP-N-Acetylglucosamine) N-acetylglucosaminephosphotransferase 1 (GlcNAc-1-P Transferase) Anticorps (53) et Dolichyl-Phosphate (UDP-N-Acetylglucosamine) N-acetylglucosaminephosphotransferase 1 (GlcNAc-1-P Transferase) Kits (4) et beaucoup plus de produits pour cette protéine.
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present work improves our knowledge of DPAGT1-CDG and provides bases for developing tailored splicing and folding therapies
Data suggest that N-acetylglucosaminyl 1-phosphate transferase is a breast cancer therapeutic target.
Studies show that cells coordinate DPAGT1 expression and protein N-glycosylation with canonical Wnt signaling and E-cadherin adhesion via positive and negative feedback mechanisms.
prominent limb-girdle weakness and minimal craniobulbar symptoms who harbour a novel mutation in DPAGT1
Patients with DPAGT1 CMS share similar clinical features with patients who have CMS caused by mutations in GFPT1, another recently identified CMS subtype.
Results indicate that the clinical spectrum of dolichyl-phosphate alpha-N-acetylglucosaminyltransferase (DPAGT1)-congenital disorders of glycosylation (CDG) is much broader than appreciated so far.
Data suggest that in oral squamous cell carcinoma (OSCC), dysregulation of canonical Wnt signaling and DPAGT1-dependent N-glycosylation induces CTHRC1, thereby driving OSCC cell migration and tumor spread.
suggest that the primary pathogenic mechanism of DPAGT1-associated CMS is reduced levels of AChRs at the endplate region. This finding demonstrates that impairment of the N-linked glycosylation pathway can lead to the development of CMS
Overexpression of DPAGT1 in human oral squamous cell carcinoma specimens is linked to aberrant activation of canonical Wnt signaling.
We identify DPAGT1 as a gene in which mutations cause a congenital myasthenic syndrome.
Mutations in DPAGT1 gene is associated with Congenital disorder of glycosylation type Ij.
up-regulation of DPAGT1 transcripts by Wnt3a led to altered N-glycosylation of E-cadherin.
REVIEW: Structure, expression, and regulation
Studies show for the first time that DPAGT1 is an upstream regulator of E-cadherin N-glycosylation status and adherens junction composition and suggest that dysregulation of DPAGT1 causes disturbances in intercellular adhesion in oral cancer.
The protein encoded by this gene is an enzyme that catalyzes the first step in the dolichol-linked oligosaccharide pathway for glycoprotein biosynthesis. This enzyme belongs to the glycosyltransferase family 4. This protein is an integral membrane protein of the endoplasmic reticulum. The congenital disorder of glycosylation type Ij is caused by mutation in the gene encoding this enzyme.
, N-acetylglucosamine-1-phosphate transferase
, UDP-N-acetylglucosamine lysosomal enzyme N-acetylglucosamine phosphotransferase
, UDP-N-acetylglucosamine--dolichyl-phosphate N-acetylglucosaminephosphotransferase
, dolichyl-phosphate alpha-N-acetylglucosaminephosphotransferase 2
, glcNAc-1-P transferase
, GlcNAc-1-P transferase
, uridine diphosphate N-acetyl D-glucosamine dolichol phosphate N-acetyl-glucosamine-1 phosphate transferase
, UDP-GlcNAc:dolichyl-phosphate N-acetylglucosaminephosphotransferase
, dolichyl-phosphate (UDP-N-acetylglucosamine) N-acetylglucosaminephosphotransferase 1 (GlcNAc-1-P tra
, dolichyl-phosphate alpha-N-acetylglucosaminyltransferase
, UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase