Evidence map›Paper›PMID 24718418›Full record

ArticlePloS one2014

The domain-specific and temperature-dependent protein misfolding phenotype of variant medium-chain acyl-CoA dehydrogenase.

Johanna M Jank, Esther M Maier, Dunja D Reiβ, Martin Haslbeck, Kristina F Kemter, Marietta S Truger, Christian P Sommerhoff, Sacha Ferdinandusse, Ronald J Wanders, Søren W Gersting and 1 more

Erratum issuedOpen access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.9field-weighted citation impact, top 16% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

11 citing papers in PubMed, 24 citations in OpenAlex.

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  7. Defective hepatic bicarbonate production due to carbonic anhydrase VA deficiency leads to early-onset life-threatening metabolic crisis.Genetics in medicine : official journal of the American College of Medical Genetics · 2016
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4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

11 authors at 3 institutions in 2 countries.

Johanna M JankDepartment of Molecular Pediatrics, Dr. von Hauner Children's Hospital, Ludwig-Maximilians-University, Munich, Germany.
Esther M MaierDepartment of Molecular Pediatrics, Dr. von Hauner Children's Hospital, Ludwig-Maximilians-University, Munich, Germany.
Dunja D ReiβDepartment of Molecular Pediatrics, Dr. von Hauner Children's Hospital, Ludwig-Maximilians-University, Munich, Germany.
Martin HaslbeckDepartment of Chemistry, Technical University Munich, Garching, Germany.
Kristina F KemterDepartment of Molecular Pediatrics, Dr. von Hauner Children's Hospital, Ludwig-Maximilians-University, Munich, Germany.
Marietta S TrugerDepartment of Molecular Pediatrics, Dr. von Hauner Children's Hospital, Ludwig-Maximilians-University, Munich, Germany.
Christian P SommerhoffInstitute of Laboratory Medicine, Ludwig-Maximilians-University, Munich, Germany.
Sacha FerdinandusseDepartments of Laboratory Medicine and Pediatrics, Laboratory Genetic Metabolic Diseases, Academic Medical Center, Emma Children's Hospital, University of Amsterdam, Amsterdam, The Netherlands.
Ronald J WandersDepartments of Laboratory Medicine and Pediatrics, Laboratory Genetic Metabolic Diseases, Academic Medical Center, Emma Children's Hospital, University of Amsterdam, Amsterdam, The Netherlands.
Søren W GerstingDepartment of Molecular Pediatrics, Dr. von Hauner Children's Hospital, Ludwig-Maximilians-University, Munich, Germany.
Ania C MuntauDepartment of Molecular Pediatrics, Dr. von Hauner Children's Hospital, Ludwig-Maximilians-University, Munich, Germany.
Ludwig-Maximilians-Universität München · DEEmma Kinderziekenhuis · NLTechnical University of Munich · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The implementation of expanded newborn screening programs reduced mortality and morbidity in medium-chain acyl-CoA dehydrogenase deficiency (MCADD) caused by mutations in the ACADM gene. However, the disease is still potentially fatal. Missense induced MCADD is a protein misfolding disease with a molecular loss-of-function phenotype. Here we established a comprehensive experimental setup to analyze the structural consequences of eight ACADM missense mutations (p.Ala52Val, p.Tyr67His, p.Tyr158His, p.Arg206Cys, p.Asp266Gly, p.Lys329Glu, p.Arg334Lys, p.Arg413Ser) identified after newborn screening and linked the corresponding protein misfolding phenotype to the site of side-chain replacement with respect to the domain. With fever being the crucial risk factor for metabolic decompensation of patients with MCADD, special emphasis was put on the analysis of structural and functional derangements related to thermal stress. Based on protein conformation, thermal stability and kinetic stability, the molecular phenotype in MCADD depends on the structural region that is affected by missense-induced conformational changes with the central β-domain being particularly prone to structural derangement and destabilization. Since systematic classification of conformational derangements induced by ACADM mutations may be a helpful tool in assessing the clinical risk of patients, we scored the misfolding phenotype of the variants in comparison to p.Lys329Glu (K304E), the classical severe mutation, and p.Tyr67His (Y42H), discussed to be mild. Experiments assessing the impact of thermal stress revealed that mutations in the ACADM gene lower the temperature threshold at which MCAD loss-of-function occurs. Consequently, increased temperature as it occurs during intercurrent infections, significantly increases the risk of further conformational derangement and loss of function of the MCAD enzyme explaining the life-threatening clinical courses observed during fever episodes. Early and aggressive antipyretic treatment thus may be life-saving in patients suffering from MCADD.

Indexed as

Protein FoldingTemperatureAcyl-CoA DehydrogenaseAnimalsChlorocebus aethiopsCircular DichroismCOS CellsEnzyme ActivationFlavin-Adenine DinucleotideFluorescenceHot TemperatureHumansHydrophobic and Hydrophilic InteractionsKineticsModels, MolecularMutant ProteinsAcyl-CoA DehydrogenaseFlavin-Adenine DinucleotideMutant ProteinsProtein Aggregates

Identifiers

PMID24718418
PMCPMC3981736
OpenAlexW2016619949

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Registered trials

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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.