Evidence map›Paper›PMID 35064074›Full record

ArticleLife science alliance2022

Phenylbutyrate rescues the transport defect of the Sec61α mutations V67G and T185A for renin.

Mark Sicking, Martina Živná, Pratiti Bhadra, Veronika Barešová, Andrea Tirincsi, Drazena Hadzibeganovic, Kateřina Hodaňová, Petr Vyleťal, Jana Sovová, Ivana Jedličková and 7 more

Open access · goldAbstract read
In one paragraph

Article in Life science alliance, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
2.2field-weighted citation impact, top 13% 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, 16 citations in OpenAlex.

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  8. Editorial: The evolving picture of CaFrontiers in physiology · 2023
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

17 authors at 3 institutions in 3 countries.

Mark SickingDepartment of Medical Biochemistry and Molecular Biology, Saarland University, Homburg, Germany.
Martina ŽivnáResearch Unit for Rare Diseases, Department of Pediatrics and Metabolic Disorders, First Faculty of Medicine, Charles University, Prague, Czech Republic.
Pratiti BhadraCenter for Bioinformatics, Saarland University, Saarbrücken, Germany.
Veronika BarešováResearch Unit for Rare Diseases, Department of Pediatrics and Metabolic Disorders, First Faculty of Medicine, Charles University, Prague, Czech Republic.
Andrea TirincsiDepartment of Medical Biochemistry and Molecular Biology, Saarland University, Homburg, Germany.ORCID 0000-0002-0889-8340
Drazena HadzibeganovicDepartment of Medical Biochemistry and Molecular Biology, Saarland University, Homburg, Germany.
Kateřina HodaňováResearch Unit for Rare Diseases, Department of Pediatrics and Metabolic Disorders, First Faculty of Medicine, Charles University, Prague, Czech Republic.
Petr VyleťalResearch Unit for Rare Diseases, Department of Pediatrics and Metabolic Disorders, First Faculty of Medicine, Charles University, Prague, Czech Republic.
Jana SovováResearch Unit for Rare Diseases, Department of Pediatrics and Metabolic Disorders, First Faculty of Medicine, Charles University, Prague, Czech Republic.
Ivana JedličkováResearch Unit for Rare Diseases, Department of Pediatrics and Metabolic Disorders, First Faculty of Medicine, Charles University, Prague, Czech Republic.
Martin JungDepartment of Medical Biochemistry and Molecular Biology, Saarland University, Homburg, Germany.ORCID 0000-0002-1482-7020
Thomas BellDepartment of Chemistry, University of Nevada, Reno, NV, USA.
Volkhard HelmsCenter for Bioinformatics, Saarland University, Saarbrücken, Germany.ORCID 0000-0002-2180-9154
Anthony J BleyerResearch Unit for Rare Diseases, Department of Pediatrics and Metabolic Disorders, First Faculty of Medicine, Charles University, Prague, Czech Republic.
Stanislav KmochResearch Unit for Rare Diseases, Department of Pediatrics and Metabolic Disorders, First Faculty of Medicine, Charles University, Prague, Czech Republic.
Adolfo CavaliéExperimental and Clinical Pharmacology and Toxicology, Pre-clinical Center for Molecular Signaling (PZMS), Saarland University, Homburg, Germany.
Sven LangDepartment of Medical Biochemistry and Molecular Biology, Saarland University, Homburg, Germany sven.lang@uni-saarland.de.ORCID 0000-0003-1326-1851
Charles University · CZSaarland University · DEUniversity of Nevada, Reno · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human Sec61 complex is a widely distributed and abundant molecular machine. It resides in the membrane of the endoplasmic reticulum to channel two types of cargo: protein substrates and calcium ions. The

Indexed as

CalciumEndoplasmic ReticulumHEK293 CellsHumansKidney DiseasesMolecular ChaperonesMutation, MissensePhenylbutyratesPolycystic Kidney DiseasesProtein TransportReninSarcoplasmic Reticulum Calcium-Transporting ATPasesSEC Translocation Channels4-phenylbutyric acidATP2A2 protein, humanCalciumMolecular ChaperonesPhenylbutyratesReninSarcoplasmic Reticulum Calcium-Transporting ATPasesSEC61A1 protein, humanSEC Translocation Channels

Identifiers

PMID35064074
PMCPMC8807872
OpenAlexW4207035122

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.