ArticleThe protein journal2008
Modulation of the activity of newly synthesized human phenylalanine hydroxylase mutant proteins by low-molecular-weight compounds.
Article in The protein journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
7 citing papers in PubMed, 18 citations in OpenAlex.
- Distinct metabolic states of a cell guide alternate fates of mutational buffering through altered proteostasis.Nature communications · 2020Article
- Functional characterization and categorization of missense mutations that cause methylmalonyl-CoA mutase (MUT) deficiency.Human mutation · 2014Article
- Innovative strategies to treat protein misfolding in inborn errors of metabolism: pharmacological chaperones and proteostasis regulators.Journal of inherited metabolic disease · 2014Review
- A new model for allosteric regulation of phenylalanine hydroxylase: implications for disease and therapeutics.Archives of biochemistry and biophysics · 2013Article
- Chemical chaperones assist intracellular folding to buffer mutational variations.Nature chemical biology · 2012Article
- Phenylalanine hydroxylase misfolding and pharmacological chaperones.Current topics in medicinal chemistry · 2012Review
- Rescue of cystathionine beta-synthase (CBS) mutants with chemical chaperones: purification and characterization of eight CBS mutant enzymes.The Journal of biological chemistry · 2010Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phenylketonuria, the most frequent disorder of amino acid metabolism, is caused by a deficient activity of human phenylalanine hydroxylase (hPAH). Rescue of the enzyme activity of several recombinant hPAH mutant forms (I65T, R261Q, R270K and V388M) by low molecular weight compounds namely glycerol, trimethylamine N-oxide (TMAO) and sodium 4-phenylbutyrate (4-PB) was investigated using a prokaryotic expression model. The studied compounds were added to the culture medium, in a concentration dependent manner, simultaneously to induction of protein expression. Among the tested molecules glycerol and TMAO were able to increase the enzyme activity of the studied mutant proteins. Furthermore, a decrease in aggregates and a recovery of the active tetrameric and dimeric forms were detected. Since the addition of the studied compounds to the medium did not change the expression level of E. Coli molecular chaperones we postulate that glycerol and TMAO rescue results from a direct stabilizing effect of the newly synthesized mutant hPAH enzymes.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.