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Dog (Canine) Polyclonal AGXT Primary Antibody für ELISA - ABIN451791
Hoshino, Kühne, Filjak, Kröger: Regulation and characterization of L-serine: pyruvate aminotransferase in rat liver cytosol and mitochondria. in Zeitschrift fur Naturforschung. Section C, Biosciences 1977
Human Polyclonal AGXT Primary Antibody für IHC, IHC (p) - ABIN4278741
Castello, Borzone, DAria, Annunziata, Piccolo, Brunetti-Pierri: Helper-dependent adenoviral vectors for liver-directed gene therapy of primary hyperoxaluria type 1. in Gene therapy 2016
AGXT1 may aid in diagnostic workup especially in conjunction with arginase-1 for HCCs that may otherwise defy conventional immunostaining patterns
Pyridoxine increases the metabolic efficiency of alanine:glyoxylate aminotransferase.
To the best of our knowledge, 2 novel variants of AGXT, p.Gly41Trp and p.Leu33Met, were first reported. Bioinformatics and functional analysis showed that only 7 mutations led to a reduced expression of alanine-glyoxylate amino transferase (AGT) at a protein level
one novel mutation, c.1015delG, and a common mutation, c.815_816insGA, of the AGXT gene among four unrelated families with Primary hyperoxaluria type 1, is reported.
Mutations at the dimer interface of alanine-glyoxylate aminotransferase alter enzyme structure/activity, leading to primary hyperoxaluria type I and determine the cellular response to vitamin B6.
two novel AGXT missense mutations (p.M49L and p.N72I), which will enrich the AGXT mutation database and provide a better comprehension of PH1 pathogenesis, were identified in a big Chinese PH1 family. Significant morphological and structural difference of kidney stones from two siblings with the same genotype observed in this study displays the heterogeneity of genotype-phenotype correlation
AGXT mutational analysis was performed to confirm the diagnosis of PH1.
this study identifies a novel AGXT gene mutation in primary hyperoxaluria after kidney transplantation failure in Tunisian patient
AGXT gene sequencing is now the choice of diagnosis of Primary hyperoxaluria type 1 (PH1)due to its non-invasive nature compared to liver enzyme assay. Early diagnosis and accurate treatment in PH1 is important for better patient outcomes.
Caenorhabditis elegans AGXT-1 is a mitochondrial and temperature-adapted ortholog of peroxisomal human AGT1.
Novel AGXT mutations in a Tunisian population with primary hyperoxaluria type 1.
The novel p.Gln137Hisfs*19 AGXT mutation detected in this study extends the spectrum of known primary hyperoxaluria type I AGXT gene mutations in Tunisia.
Data show that onomeric minor allele of human alanine glyoxylate aminotransferase (AGT-Mi) binds pyridoxal 5-phosphate (PLP) but does not display catalytic activity.
Letter/Case Report: novel missense AGXT gene mutation in a Sri Lankan family with primary hyperoxaluria type 1.
Primary hyperoxaluria type 1 (PH1) is due to a defect in the AGXT gene. The aim of our study was to analyze the mutations causing PH1 in the Moroccan population
In conclusion, this study of an unprecedented number of primary hyperoxaluria type 1 patients showed geno-phenotype associations that have not been previously reported.
The pathogenic mutation G47R causes misfolding of alanine:glyoxylate aminotransferase.
A review of the current knowledge of the biochemical properties of liver peroxisomal alanine:glyoxylate aminotransferase and of the molecular defects caused by single point mutations associated with Primary Hyperoxaluria Type 1.
S81L and G170R mutations of AGT is associated with Primary Hyperoxaluria type I in homozygosis and heterozygosis.
AGT missense mutations associated with Primary Hyperoxaluria Type 1, were characterized.
AGT-deficient mice showed decreased vascular permeability, a readout of in vivo histamine activity.
expressed wild-type human AGT1 was predominantly localized in mouse hepatocellular peroxisomes, whereas the most common mutant form of AGT1 (G170R) was localized predominantly in the mitochondria
This gene is expressed only in the liver and the encoded protein is localized mostly in the peroxisomes, where it is involved in glyoxylate detoxification. Mutations in this gene, some of which alter subcellular targetting, have been associated with type I primary hyperoxaluria.
L-alanine: glyoxylate aminotransferase 1
, alanine--glyoxylate aminotransferase
, hepatic peroxisomal alanine:glyoxylate aminotransferase
, serine--pyruvate aminotransferase
, serine-pyruvate aminotransferase
, serine:pyruvate aminotransferase
, alanine:glyoxylate aminotransferase
, angiotensin receptor 2
, serine--pyruvate aminotransferase, mitochondrial
, serine--pyruvate aminotransferase, peroxisomal
, serine:pyruvate aminotransferase SPT
, serine:pyruvate/alanine:glyoxylate aminotransferase
, alanine-glyoxylate aminotransferase 1
, LOW QUALITY PROTEIN: serine--pyruvate aminotransferase, mitochondrial
, alanine-glyoxylate aminotransferase
, putative alanine:glyoxylate aminotransferase
, alanine-glyoxylate aminotransferase b