Evidence map›Paper›PMID 34510628›Full record

ArticleHuman mutation2021

Noncoding sequence variants define a novel regulatory element in the first intron of the N-acetylglutamate synthase gene.

Johannes Häberle, Marvin B Moore, Nantaporn Haskins, Véronique Rüfenacht, Dariusz Rokicki, Estela Rubio-Gozalbo, Mendel Tuchman, Nicola Longo, Mark Yandell, Ashley Andrews and 2 more

Abstract read
In one paragraph

Article in Human mutation, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

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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

12 authors.

Johannes HäberleDivision of Metabolism and Children's Research Center, University Children's Hospital, Zurich, Switzerland.ORCID 0000-0003-0635-091X
Marvin B MooreDepartment of Human Genetics, University of Utah Health Science Center, Salt Lake City, Utah, USA.
Nantaporn HaskinsCenter for Genetic Medicine Research, Children's National Hospital, Washington, District of Columbia, USA.
Véronique RüfenachtDivision of Metabolism and Children's Research Center, University Children's Hospital, Zurich, Switzerland.
Dariusz RokickiDepartment of Pediatrics, Nutrition and Metabolic Diseases, The Children's Memorial Health Institute, Warsaw, Poland.
Estela Rubio-GozalboDepartment of Pediatrics and Clinical Genetics, Maastricht University Medical Center, Maastricht, The Netherlands.
Mendel TuchmanCenter for Genetic Medicine Research, Children's National Hospital, Washington, District of Columbia, USA.
Nicola LongoDivision of Medical Genetics, Department of Pediatrics, University of Utah Health Science Center, Salt Lake City, Utah, USA.ORCID 0000-0002-3677-1216
Mark YandellEccles Institute of Human Genetics, University of Utah Health Science Center, Salt Lake City, Utah, USA.
Ashley AndrewsDivision of Medical Genetics, Pediatrics, University of Utah Health Science Center, Salt Lake City, Utah, USA.
Nicholas AhMewCenter for Genetic Medicine Research, Children's National Hospital, Washington, District of Columbia, USA.
Ljubica CaldovicCenter for Genetic Medicine Research, Children's National Hospital, Washington, District of Columbia, USA.ORCID 0000-0002-9140-5585

Funding

N-acetylglutamate Synthase: Structure, Function & DefectsR01DK064913 · NIDDK · CHILDREN'S RESEARCH INSTITUTE · PI CALDOVIC, LJUBICA MORIZONO · 2003 to 2017
$4.9M
NIDDK NIH HHS R01 DK064913
6 · The paper itself

Abstract

N-acetylglutamate synthase deficiency is an autosomal recessive urea cycle disorder caused either by decreased expression of the NAGS gene or defective NAGS enzyme resulting in decreased production of N-acetylglutamate (NAG), an allosteric activator of carbamylphosphate synthetase 1 (CPS1). NAGSD is the only urea cycle disorder that can be effectively treated with a single drug, N-carbamylglutamate (NCG), a stable NAG analog, which activates CPS1 to restore ureagenesis. We describe three patients with NAGSD due to four novel noncoding sequence variants in the NAGS regulatory regions. All three patients had hyperammonemia that resolved upon treatment with NCG. Sequence variants NM_153006.2:c.427-222G>A and NM_153006.2:c.427-218A>C reside in the 547 bp-long first intron of NAGS and define a novel NAGS regulatory element that binds retinoic X receptor α. Sequence variants NC_000017.10:g.42078967A>T (NM_153006.2:c.-3065A>T) and NC_000017.10:g.42078934C>T (NM_153006.2:c.-3098C>T) reside in the NAGS enhancer, within known HNF1 and predicted glucocorticoid receptor binding sites, respectively. Reporter gene assays in HepG2 and HuH-7 cells demonstrated that all four substitutions could result in reduced expression of NAGS. These findings show that analyzing noncoding regions of NAGS and other urea cycle genes can reveal molecular causes of disease and identify novel regulators of ureagenesis.

Indexed as

Amino-Acid N-AcetyltransferaseHyperammonemiaUrea Cycle Disorders, InbornHumansIntronsRegulatory Sequences, Nucleic AcidAmino-Acid N-AcetyltransferaseNAGS protein, humanintronmutation analysisN-acetylglutamateN-acetylglutamate synthaseN-acetylglutamate synthase deficiencynoncoding sequence variantsregulatory elementurea cycleurea cycle disorders

Identifiers

PMID34510628
PMCPMC8604755

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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.