The rare disease Primary Hyperoxaluria Type I (PH1) results from the deficit of liver peroxisomal alanine:glyoxylate aminotransferase (AGT), as a consequence of inherited mutations on the AGXT gene frequently leading to protein misfolding. Pharmacological chaperone (PC) therapy is a newly developed approach for misfolding diseases based on the use of small molecule ligands able to promote the correct folding of a mutant enzyme. In this report, we describe the interaction of amino-oxyacetic acid (AOA) with the recombinant purified form of two polymorphic species of AGT, AGT-Ma and AGT-Mi, and with three pathogenic variants bearing previously identified folding defects: G41R-Ma, G170R-Mi, and I244T-Mi. We found that for all these enzyme AOA (...
Primary Hyperoxaluria Type I (PH1) is a disorder of glyoxylate metabolism caused by mutations in the...
The substitution of Ser187, a residue located far from the active site of human liver peroxisomal al...
Liver peroxisomal alanine:glyoxylate aminotransferase (AGT) (EC 2.6.1.44) catalyses the conversion o...
The rare disease Primary Hyperoxaluria Type I (PH1) results from the deficit of liver peroxisomal al...
The functional deficit of alanine:glyoxylate aminotransferase (AGT) in human hepatocytes leads to a ...
14 pags, 8 figs, 3 tabsPrimary hyperoxaluria type I (PH1) is a conformational disease which result i...
<div><p>Primary hyperoxaluria type I (PH1) is a conformational disease which result in the loss of a...
Primary hyperoxaluria 1 (PH1; Online Mendelian Inheritance in Man no. 259900), a typically lethal bi...
16 pags, 5 figsAlanine-glyoxylate aminotransferase catalyzes the transamination between L-alanine an...
Liver peroxisomal alanine:glyoxylate aminotransferase (AGT), a pyridoxal 5'-phosphate (PLP) enzyme, ...
Peroxisomal alanine:glyoxylate aminotransferase (AGT) is responsible for glyoxylate detoxification i...
G41 is an interfacial residue located within the alpha-helix 34-42 of alanine:glyoxylate aminotransf...
Peroxisomal alanine:glyoxylate aminotransferase (AGT) is responsible for glyoxylate detoxification i...
Protein misfolding is becoming one of the main mechanisms underlying inherited enzymatic deficits. T...
G41 is an interfacial residue located within the alpha-helix 34-42 of alanine:glyoxylate aminotransf...
Primary Hyperoxaluria Type I (PH1) is a disorder of glyoxylate metabolism caused by mutations in the...
The substitution of Ser187, a residue located far from the active site of human liver peroxisomal al...
Liver peroxisomal alanine:glyoxylate aminotransferase (AGT) (EC 2.6.1.44) catalyses the conversion o...
The rare disease Primary Hyperoxaluria Type I (PH1) results from the deficit of liver peroxisomal al...
The functional deficit of alanine:glyoxylate aminotransferase (AGT) in human hepatocytes leads to a ...
14 pags, 8 figs, 3 tabsPrimary hyperoxaluria type I (PH1) is a conformational disease which result i...
<div><p>Primary hyperoxaluria type I (PH1) is a conformational disease which result in the loss of a...
Primary hyperoxaluria 1 (PH1; Online Mendelian Inheritance in Man no. 259900), a typically lethal bi...
16 pags, 5 figsAlanine-glyoxylate aminotransferase catalyzes the transamination between L-alanine an...
Liver peroxisomal alanine:glyoxylate aminotransferase (AGT), a pyridoxal 5'-phosphate (PLP) enzyme, ...
Peroxisomal alanine:glyoxylate aminotransferase (AGT) is responsible for glyoxylate detoxification i...
G41 is an interfacial residue located within the alpha-helix 34-42 of alanine:glyoxylate aminotransf...
Peroxisomal alanine:glyoxylate aminotransferase (AGT) is responsible for glyoxylate detoxification i...
Protein misfolding is becoming one of the main mechanisms underlying inherited enzymatic deficits. T...
G41 is an interfacial residue located within the alpha-helix 34-42 of alanine:glyoxylate aminotransf...
Primary Hyperoxaluria Type I (PH1) is a disorder of glyoxylate metabolism caused by mutations in the...
The substitution of Ser187, a residue located far from the active site of human liver peroxisomal al...
Liver peroxisomal alanine:glyoxylate aminotransferase (AGT) (EC 2.6.1.44) catalyses the conversion o...