ライフサイエンスコーパス: FAH

1 FAH(-/-) pigs were treated with the protective drug 2-(2

2 judiciously selected reductant [formic acid (FAH)] effectively minimizes iodide oxidation and cation

3 t the development and characterization of an FAH inhibitor, 4-(hydroxymethylphosphinoyl)-3-oxo-butano

4 sive disorders linked to the PAH, ABCC6, and FAH and HPD genes, respectively.

5 ovirus injections >90% of hepatocytes became FAH positive and liver function was restored to normal.

6 ome of these mutations are known to decrease FAH catalytic activity, but the mechanisms of FAH mutati

7 her fumarylacetoacetate hydrolase deficient (FAH(-/-)) pigs, a novel large-animal model of HT1, devel

8 iously proposed based on recently determined FAH crystal structures.

9 We also generated FAH(+) hepatocytes in the liver via lipid-nanoparticle-m

10 deficiency of fumarylacetoacetate hydrolase (FAH) and develop progressive hepatocellular dysfunction

11 deficiency of fumarylacetoacetate hydrolase (FAH) and homogentisic acid dioxygenase (HGD), respective

12 Fumarylacetoacetate hydrolase (FAH) catalyzes the hydrolytic cleavage of a carbon-carbo

13 gene encoding fumarylacetoacetate hydrolase (FAH) cause hereditary tyrosinemia type I (HT1), a metabo

14 for MAAI and fumarylacetoacetate hydrolase (FAH) died rapidly on a normal diet, indicating that MAA

15 Fumarylacetoacetate hydrolase (FAH) domain-containing proteins occur in both prokaryote

16 ansferred the fumarylacetoacetate hydrolase (FAH) gene by LV vectors into FAH((-/-)) mice (n = 97) an

17 in the human fumarylacetoacetate hydrolase (FAH) gene that disrupt tyrosine catabolism.

18 Fumarylacetoacetate hydrolase (FAH) is the last enzyme in tyrosine catabolism, and muta

19 member of the fumarylacetoacetate hydrolase (FAH) superfamily and implicated Glu-109 and Glu-111 as p

20 on of a human fumarylacetoacetate hydrolase (FAH) transgene in the porcine model of HT1.

21 deficiency of fumarylacetoacetate hydrolase (FAH), to determine whether in vivo selection of correcte

22 ng, generated fumarylacetoacetate hydrolase (FAH)-positive hepatocytes in the liver, and rescued weig

23 in the enzyme fumarylacetoacetate hydrolase (FAH).

24 the pathway, fumarylacetoacetate hydrolase (FAH).

25 elective repopulation of the liver occurs in FAH-deficient mice.

26 tate hydrolase (FAH) gene by LV vectors into FAH((-/-)) mice (n = 97) and performed serial hepatocyte

27 Under conditions of low-dose NTBC, FAH(-/-) pigs developed liver fibrosis and portal hypert

28 n had no effect on the enzymatic activity of FAH, but rather promoted the degradation of the mutant p

29 The analysis of FAH structures corresponding to different catalytic stat

30 ight into the structure-based development of FAH inhibitors.

31 and provides stable long-term expression of FAH in pigs with HT1.

32 We expect that the subsequent generation of FAH-null homozygote pigs will serve as a significant adv

33 n of the K10C2.4, which encodes a homolog of FAH.

34 ntial human metabolic function, with loss of FAH activity causing the fatal metabolic disease heredit

35 AH catalytic activity, but the mechanisms of FAH mutation-induced pathogenicity remain poorly underst

36 The crystal structure of FAH complexed with HMPOBA refined at 1.3-A resolution re

37 Because HGD is upstream of FAH in the tyrosine pathway, mice doubly mutant in both

38 ylpyruvate dioxygenase, which is upstream of FAH.

39 This led to reduced FAH protein levels and enzymatic activity in the liver a

40 o structural differences in their respective FAH domains; however, the precise relationship between s

41 ly repaired the deletion junction to restore FAH expression in liver.

42 nt of pharmacological chaperones that target FAH to tackle the severe disease HT1.

43 lity of the enzyme and always accelerate the FAH aggregation pathway.

44 In conclusion, the FAH(-/-) pig is a large-animal model of HT1 with clinica

45 oxy transition state intermediate during the FAH catalyzed reaction, and reveals a Mg(2+) bound in th

46 in tyrosine catabolism, and mutations in the FAH gene are associated with hereditary tyrosinemia type

47 injection of adult bone marrow cells in the FAH(-/-) mouse, an animal model of tyrosinemia type I, r

48 recise relationship between structure of the FAH domain and the associated enzyme function remains el

49 in vivo from a luciferase gene linked to the FAH gene.

50 In mammals, three FAH domain-containing proteins, FAHD1, FAHD2A, and FAHD2

51 er where they differentiated into areas with FAH and Albumin positive hepatocytes.

52 Conclusion: Coexpression with FAH is an effective technique for lifelong expression of

53 odules and total liver from the patient with FAH deficiency were compared with control donor liver.

54 ological temperatures and concentrations, WT FAH is in equilibrium between a catalytically active dim

55 of thermodynamic and kinetic stability in WT FAH and a representative set of 19 missense mutations id