FMO3 Antibody, FITC conjugated

1. Finally, understanding the binding mode of methimazole and indole could be advantageous for development of hFMO3 inhibitors, currently investigated as a possible treatment strategy for atherosclerosis PMID: 29959003
2. Report developmental regulation of hepatic FMO3 expression. PMID: 26839369
3. the involvement of flavin-containing monooxygenase-3 (FMO3) and cytochrome P450 enzymes (CYPs) in Busulphan metabolic pathway, is reported. PMID: 29121650
4. FMO3 protein abundance is significantly associated with age, gender, and genotype PMID: 28819071
5. FMO3 Variant is associated with chronic kidney disease. PMID: 27513517
6. The two FMO3 mutants were in close linkage disequilibrium and might play an important role in the pharmacokinetics of sulindac in Chinese healthy male volunteers. PMID: 28331852
7. mechanism of hFMO3 which could be valuable not only for screening of new chemical entities but more significantly for designing of novel inhibitors of this important Phase I drug metabolising enzyme. PMID: 27523475
8. Olanzapine clearance was not affected by CYP2D6 or FMO3 genotypes or smoking behavior as a single factor under the present conditions because olanzapine clearance is mediated by multiple enzymes involved in two major and one minor pathways PMID: 26856397
9. Oxidative stress-responsive transcription factor NRF2 is not indispensable for the human hepatic Flavin-containing monooxygenase-3 (FMO3) gene expression in HepG2 cells PMID: 26616280
10. FMO3 gene polymorphism E158K is a significant predictor of predisposition to chronic heart disease in women. PMID: 26519273
11. FMO3 is centrally involved in the pathogenesis of atherosclerosis by regulating cholesterol metabolism and insulin resistance. [Review] PMID: 26218418
12. FMO3 expression is increased in obese/insulin resistant patients. PMID: 25849138
13. These results suggest that genetic polymorphism in the human FMO3 gene may lead to changes of drug interactions for N- or S-oxygenations of xenobiotics and endogenous substances. PMID: 25760532
14. Effect of two-linked mutations of the FMO3 gene on itopride metabolism in Chinese healthy volunteers PMID: 25224784
15. Three polymorphisms were found in intronic regions of FMO3 in a child with trimethylaminuria and in her parents and a brother. The parents and brother showed no symptoms. PMID: 25288227
16. Comparisons of genotype and phenotype reveal that severe trimethylaminuria is caused by loss of function mutations in FMO3 PMID: 24028545
17. results show that FMO3 E158K and POR A503V polymorphisms are minor sources of nicotine metabolism variation, insufficient to appreciably alter smoking. PMID: 24448396
18. CYP3A4 and FMO3 are the major enzymes responsible for the metabolism of teneligliptin in humans. PMID: 23855261
19. FMO3 (rs2266780) was in complete linkage disequilibrium with FMO6. PMID: 24173915
20. single-nucleotide polymorphisms in the FMO3 gene is associated with chronic allograft dysfunction. PMID: 23350966
21. Novel variations in the FMO3 gene associated with trimethylaminuria. PMID: 23791655
22. provides fundamental, up-to-date information on the importance of human FMO3 in individual xenobiotic oxygenations, including those of new medicines and dietary-derived trimethylamine PMID: 23567996
23. FMO3 heterozygote genotypes increase the risk of stroke 6 times in hypertensives in Turkish population. PMID: 23510775
24. Polymorphisms in FMO3 influence nicotine clearance and that these genetic variants in turn influence cigarette consumption. PMID: 23211429
25. Genetic variations in the FMO3 gene in patients with trimethylaminuria do not always present with fish-like body odor. PMID: 23266626
26. Six novel variants of the FMO3 gene have been found responsible for trimethylaminuria in a Japanese population. PMID: 22819296
27. It was found that FMO3 158K, 257M and 308G alleles, demonstrate impaired metabolism toward many FMO3 substrates, were observed frequently in Turkish population similar to the other populations PMID: 22409263
28. patient heterozygous for 4 FMO3 mutations PMID: 21075259
29. This study is the first to demonstrate a gene-environment interaction in SIDS. The findings suggest that the common polymorphism G472A of FMO3 could act as an additional genetic SIDS risk factor in children whose mothers smoke. PMID: 20198379
30. These data suggest that birth is necessary, but not sufficient for the onset of FMO3 expression. A gender-independent increase in FMO3 expression was observed from 11 to 18 y of age. PMID: 11809920
31. two new polymorphisms, His132-FMO3 and Pro360-FMO3, were identified; the effect of the amino acid substitutions on the function of FMO3 was evaluated PMID: 12814961
32. Data show that the frequencies of FMO3 mutant alleles varied not only in different ethnic groups, but also in different populations that stemmed from the same ethnic group. PMID: 12903042
33. ..FMO3 appears to be the most important flavin-containing monoxygenase..in adult human liver. p. 574 ..human FMO3 appears to oxygenate nucleophilic heteroatom-containing substrates.." p. 576 PMID: 15203093
34. FMO3 displayed a significant, dominant liver-specific mRNA profile. PMID: 16183778
35. variants in the FMO3 gene do not predispose to essential hypertension in a cardiovascular disease population of 1649 individuals, 691(41.9%) of whom had a history of hypertension requiring drug treatment PMID: 16324215
36. Flavin-containing monooxygenase 3 (FMO3) is responsible for the majority of FMO-mediated xenobiotic metabolism in the adult human liver. PMID: 16481213
37. Genetic basis of trimethylaminuria is studied in Italian pedigrees and shows a spectrum of variation in the FM03 gene with 3 novel mutations: a de novo missense mutation, a deletion (G1182del) at codon 394 and a novel missense mutation (R238P). PMID: 16600650
38. The genotypes and allele frequencies of the MDR1/C3435T, FMO3/G488A, FMO3/A923G and CYP1A2/G-3860 A polymorphisms were not significantly different in cancer-free subjects and CRC patients. PMID: 16800822
39. The study is said to be the first report for significant single nucleotide polymorphisms of the FMO3 causing amino acid substitutions in Japanese trimethylaminuria patients. PMID: 16858129
40. As summarized in this review, FMO3 is apparently unique to the human, yet is the most abundant FMO family member in the adult human liver, whereas FMO1 dominates in most animal models. PMID: 16863467
41. Individuals homozygous for either of the nonsense mutations--Arg500Stop and/or Cys197Stop--alleles in the FMO3 gene can possess abnormal trimethylamine N-oxygenation. PMID: 16996766
42. results suggest that the effects of genetic variation of FMO3 could operate at the functional level for N- & S-oxygenation for typical FMO3 substrates PMID: 17142560
43. abnormal FMO3 capacity is caused by menstruation particularly in the presence, in homozygous form, of mild genetic variants such as [Glu158Lys; Glu308Gly] that cause a reduced FMO3 function PMID: 17257434
44. A homology model for FMO3 was constructed based on the crystal structure for yeast FMO which places the N61 residue alone, of the mutants analyzed here, in close proximity to the FAD catalytic center. PMID: 17531949
45. This review summarizes the current state of research on the genetic polymorphisms of FMO3, with a focus on their clinical implications in gastrointestinal diseases. PMID: 17559352
46. Mutations of the FMO3 gene were investigated in Japanese trimethylaminuria that showed low FMO3 metabolic capacity. PMID: 17584019
47. FMO3 is the primary human adult liver FMO enzyme, but is developmentally regulated PMID: 17786630
48. TG100435 and TG100855 were interconverted metabolically. FMO3 seem to be the major N-oxidizing enzyme, whereas cytochrome P450 reductase seems to be responsible for the retroreduction reaction. PMID: 17881660
49. The results provide evidence that FMO3 has been the subject of balancing selection. PMID: 17885620
50. Site-directed mutagenesis studies suggest that the putative hepatic nuclear factor-4 (HNF-4) binding site and CCAAT box could be responsible cis-acting elements of the FMO3 gene in a Japanese population. PMID: 18305374

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HGNC: 3771

OMIM: 136132

KEGG: hsa:2328

STRING: 9606.ENSP00000356729

UniGene: Hs.445350