The V108M mutation decreases the structural stability of catechol O-methyltransferase.

The V108M mutation decreases the structural stability of catechol O-methyltransferase.

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http://www.wikidata.org/entity/Q46599695
The structural biology of oestrogen metabolismA Multi-scale Computational Platform to Mechanistically Assess the Effect of Genetic Variation on Drug Responses in Human Erythrocyte MetabolismA miniaturized technique for assessing protein thermodynamics and function using fast determination of quantitative cysteine reactivity.New Dynamic Rotamer Libraries: Data-Driven Analysis of Side-Chain Conformational Propensities.A hotspot of inactivation: The A22S and V108M polymorphisms individually destabilize the active site structure of catechol O-methyltransferase.Polymorphisms and disease: hotspots of inactivation in methyltransferasesDisruptive mRNA folding increases translational efficiency of catechol-O-methyltransferase variantComputational Investigation of the Interplay of Substrate Positioning and Reactivity in Catechol O-Methyltransferase.No association between germline variation in catechol-O-methyltransferase and colorectal cancer survival in postmenopausal women.One amino acid makes a difference-Characterization of a new TPMT allele and the influence of SAM on TPMT stability.The Val158Met polymorphism in COMT gene and cancer risk: role of endogenous and exogenous catechols.Catechol-O-Methyltransferase (COMT): An Update on Its Role in Cancer, Neurological and Cardiovascular Diseases.1H, 15N, 13C backbone resonance assignments of human soluble catechol O-methyltransferase in complex with S-adenosyl-L-methionine and 3,5-dinitrocatechol.A preliminary investigation of the impact of catechol-O-methyltransferase genotype on the absorption and metabolism of green tea catechins.Polymorphisms in the potential functional regions of the TGF-β 1 and TGF-β receptor genes and disease susceptibility in HBV-related hepatocellular carcinoma patients.In Vitro Protein Stability of Two Naturally Occurring Thiopurine S-Methyltransferase Variants: Biophysical Characterization of TPMT*6 and TPMT*8.
P2860

The V108M mutation decreases the structural stability of catechol O-methyltransferase.

Item
http://www.wikidata.org/entity/Q46599695
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh-hant
name
The V108M mutation decreases the structural stability of catechol O-methyltransferase.
@en
The V108M mutation decreases the structural stability of catechol O-methyltransferase.
@nl
type
label
The V108M mutation decreases the structural stability of catechol O-methyltransferase.
@en
The V108M mutation decreases the structural stability of catechol O-methyltransferase.
@nl
prefLabel
The V108M mutation decreases the structural stability of catechol O-methyltransferase.
@en
The V108M mutation decreases the structural stability of catechol O-methyltransferase.
@nl
P1433
P1476
P2093
P304
P31
P356
P433
P478
P50
P577
P698
P356
P1433
P1476
The V108M mutation decreases the structural stability of catechol O-methyltransferase
@en
P2093
P304
P31
P356
10.1016/J.BBAPAP.2008.04.006
P433
P478
P50
P577
P698