Loss of function in phenylketonuria is caused by impaired molecular motions and conformational instability - Wikidata - wikimedia - TriplyDB

Loss of function in phenylketonuria is caused by impaired molecular motions and conformational instability

Loss of function in phenylketonuria is caused by impaired molecular motions and conformational instability

http://www.wikidata.org/entity/Q36744649

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Activation of phenylalanine hydroxylase induces positive cooperativity toward the natural cofactor Protein misfolding is the molecular mechanism underlying MCADD identified in newborn screening Characterization of two pathogenic mutations in cystathionine beta-synthase: different intracellular locations for wild-type and mutant proteins A new model for allosteric regulation of phenylalanine hydroxylase: implications for disease and therapeutics Structural and mechanistic basis of the interaction between a pharmacological chaperone and human phenylalanine hydroxylase Protein homeostasis disorders of key enzymes of amino acids metabolism: mutation-induced protein kinetic destabilization and new therapeutic strategies.Folding dynamics of phenylalanine hydroxylase depends on the enzyme's metallation state: the native metal, iron, protects against aggregate intermediates.Molecular basis of classic galactosemia from the structure of human galactose 1-phosphate uridylyltransferase.Novel pharmacological chaperones that correct phenylketonuria in mice.Dynamic regulation of phenylalanine hydroxylase by simulated redox manipulation Phenylalanine hydroxylase misfolding and pharmacological chaperones.Linking genotypes database with locus-specific database and genotype-phenotype correlation in phenylketonuria The domain-specific and temperature-dependent protein misfolding phenotype of variant medium-chain acyl-CoA dehydrogenase Types and effects of protein variations.Up to date knowledge on different treatment strategies for phenylketonuria.Cystathionine beta-synthase mutants exhibit changes in protein unfolding: conformational analysis of misfolded variants in crude cell extracts.First structure of full-length mammalian phenylalanine hydroxylase reveals the architecture of an autoinhibited tetramer Genotype-phenotype associations in French patients with phenylketonuria and importance of genotype for full assessment of tetrahydrobiopterin responsiveness Testing for tetrahydrobiopterin responsiveness in patients with hyperphenylalaninemia due to phenylalanine hydroxylase deficiency.Phenylalanine hydroxylase: function, structure, and regulation.Tetrahydrobiopterin, its mode of action on phenylalanine hydroxylase, and importance of genotypes for pharmacological therapy of phenylketonuria.Innovative strategies to treat protein misfolding in inborn errors of metabolism: pharmacological chaperones and proteostasis regulators.Clinical therapeutics for phenylketonuria.Genetics of Phenylketonuria: Then and Now.Expression analysis revealing destabilizing mutations in phosphomannomutase 2 deficiency (PMM2-CDG): expression analysis of PMM2-CDG mutations.Structural basis for ligand-dependent dimerization of phenylalanine hydroxylase regulatory domain.Computational study of missense mutations in phenylalanine hydroxylase.Biophysical analysis of the effect of chemical modification by 4-oxononenal on the structure, stability, and function of binding immunoglobulin protein (BiP).Mapping the functional landscape of frequent phenylalanine hydroxylase (PAH) genotypes promotes personalised medicine in phenylketonuria.Functional studies of tyrosine hydroxylase missense variants reveal distinct patterns of molecular defects in Dopa-responsive dystonia.Structural features of the regulatory ACT domain of phenylalanine hydroxylase.Functional and structural characterization of novel mutations and genotype-phenotype correlation in 51 phenylalanine hydroxylase deficient families from Southern Italy.Prevalence of tetrahydrobiopterine (BH4)-responsive alleles among Austrian patients with PAH deficiency: comprehensive results from molecular analysis in 147 patients.Tetrahydrobiopterin treatment reduces brain L-Phe but only partially improves serotonin in hyperphenylalaninemic ENU1/2 mice.Towards the identification of the allosteric Phe-binding site in phenylalanine hydroxylase.Experimental and computational evidence on conformational fluctuations as a source of catalytic defects in genetic diseases

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P2860

Loss of function in phenylketonuria is caused by impaired molecular motions and conformational instability

http://www.wikidata.org/entity/Q36744649

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Loss of function in phenylketo ...... and conformational instability

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Loss of function in phenylketo ...... and conformational instability

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Loss of function in phenylketo ...... and conformational instability

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Loss of function in phenylketo ...... and conformational instability

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Loss of function in phenylketo ...... and conformational instability

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J.AJHG.2008.05.013

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American Journal of Human Genetics

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Loss of function in phenylketo ...... and conformational instability

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Adelbert A Roscher

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Ania C Muntau

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Christian P Sommerhoff

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Dunja D Messing

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Florian B Lagler

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Kristina F Kemter

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Marta K Danecka

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Michael Staudigl

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Søren W Gersting

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P2860

Expression of recombinant human phenylalanine hydroxylase as fusion protein in Escherichia coli circumvents proteolytic degradation by host cell proteases. Isolation and characterization of the wild-type enzyme

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...

Structure of phenylalanine hydroxylase from Colwellia psychrerythraea 34H, a monomeric cold active enzyme with local flexibility around the active site and high overall stability

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

SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modeling

The human phenome project

Probing protein structure by limited proteolysis.

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5317785

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18538294

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phenylketonuria

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2443833

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