Computational study of missense mutations in phenylalanine hydroxylase.

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Phenylketonuria Pathophysiology: on the Role of Metabolic Alterations Predicting Severity of Disease-Causing Variants.First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer

P2860

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P2860

Computational study of missense mutations in phenylalanine hydroxylase.

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http://www.wikidata.org/entity/Q41271157

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2015 nî lūn-bûn

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2015年の論文

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2015年論文

@yue

2015年論文

@zh-hant

2015年論文

@zh-hk

2015年論文

@zh-mo

2015年論文

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2015年论文

@wuu

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Computational study of missense mutations in phenylalanine hydroxylase.

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type

Item

label

Computational study of missense mutations in phenylalanine hydroxylase.

@en

prefLabel

Computational study of missense mutations in phenylalanine hydroxylase.

@en

P1476

Computational study of missense mutations in phenylalanine hydroxylase.

@en

P2093

Kamila Réblová

http://www.w3.org/2001/XMLSchema#string

Lenka Fajkusová

http://www.w3.org/2001/XMLSchema#string

Petr Kulhánek

http://www.w3.org/2001/XMLSchema#string

P2860

Predicting deleterious amino acid substitutions

Tetrahydrobiopterin biosynthesis, regeneration and functions

Hyperphenylalaninemia with high levels of 7-biopterin is associated with mutations in the PCBD gene encoding the bifunctional protein pterin-4a-carbinolamine dehydratase and transcriptional coactivator (DCoH).

Geometry of interplanar residue contacts in protein structures

Structural basis of autoregulation of phenylalanine hydroxylase

2.0A resolution crystal structures of the ternary complexes of human phenylalanine hydroxylase catalytic domain with tetrahydrobiopterin and 3-(2-thienyl)-L-alanine or L-norleucine...

Structural studies of p53 inactivation by DNA-contact mutations and its rescue by suppressor mutations via alternative protein-DNA interactions

Crystal structure of the catalytic domain of human phenylalanine hydroxylase reveals the structural basis for phenylketonuria

Structure of tetrameric human phenylalanine hydroxylase and its implications for phenylketonuria

VMD: visual molecular dynamics

P2888

s00894-015-2620-6

P304

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P31

scholarly article

P356

10.1007/S00894-015-2620-6

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P433

http://www.w3.org/2001/XMLSchema#string

P478

http://www.w3.org/2001/XMLSchema#string

P577

2015-03-07T00:00:00Z

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P5875

273324110

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P698

25750018

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Computational study of missense mutations in phenylalanine hydroxylase.

about

P2860

P2860

Computational study of missense mutations in phenylalanine hydroxylase.

description

name

type

label

prefLabel

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P5875

P698

P356

P1433

P1476

P2093

P2860

P2888

P304

P31

P356

P433

P478

P577

P5875

P698