Evidence map›Paper›PMID 20303810›Full record

ReviewMolecular genetics and metabolism2010

N-acetylglutamate synthase: structure, function and defects.

Ljubica Caldovic, Nicholas Ah Mew, Dashuang Shi, Hiroki Morizono, Marc Yudkoff, Mendel Tuchman

Open access · greenAbstract readReview
In one paragraph

Review in Molecular genetics and metabolism, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.6field-weighted citation impact, top 11% 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

29 citing papers in PubMed, 70 citations in OpenAlex.

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  15. Frontiers in veterinary science · 2022
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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

6 authors at 3 institutions in 1 country.

Ljubica CaldovicThe Children's Research Institute, Children's National Medical Center, The George Washington University, Washington, DC 20010, USA.
Nicholas Ah Mew
Dashuang Shi
Hiroki Morizono
Marc Yudkoff
Mendel Tuchman
Children's National · USChildren's Hospital of Philadelphia · USGeorge Washington University · US

Funding

Training (Career Development) ComponentU54HD061221 · NICHD · CHILDREN'S RESEARCH INSTITUTE · PI GROPMAN, ANDREA LYNNE · 2009 to 2023
$20.8M
NEUROIMAGING COREP30HD040677 · NICHD · CHILDREN'S RESEARCH INSTITUTE · PI VITTORIO GALLO, VITTORIO GALLO VITTORIO GALLO · 2001 to 2015
$15.9M
ZAP-70 EXPRESSION, CD38 EXPRESSION AND PROGNOSIS IN CHRONIC LYMPHOCYTIC LEUKEMIAM01RR020359 · NCRR · CHILDREN'S RESEARCH INSTITUTE · PI RAKHMANINA, NATELLA Y · 2005 to 2010
$13.8M
RARE DISEASES CRC: UREA CYCLE DISORDERSU54RR019453 · NCRR · CHILDREN'S RESEARCH INSTITUTE · PI BATSHAW, MARK L. · 2003 to 2008
$7.0M
N-acetylglutamate Synthase: Structure, Function & DefectsR01DK064913 · NIDDK · CHILDREN'S RESEARCH INSTITUTE · PI CALDOVIC, LJUBICA MORIZONO · 2003 to 2017
$4.9M
N-carbamylglutamate in the treatment of hyperammonemiaR01HD058567 · NICHD · CHILDREN'S RESEARCH INSTITUTE · PI TUCHMAN, MENDEL · 2008 to 2016
$4.4M
REGULATION OF 15N UREA ISOTOPOMERS PRODUCTIONR01DK053761 · NIDDK · CHILDREN'S HOSP OF PHILADELPHIA · PI NISSIM, ITZHAK · 1999 to 2013
$4.4M
The molecular bases of inherited urea cycle disorders and ureagenesis regulationR01DK047870 · NIDDK · UNIVERSITY OF MINNESOTA TWIN CITIES · PI TUCHMAN, MENDEL · 1995 to 2010
$3.4M
Structural Studies of NAGSK01DK067935 · NIDDK · CHILDREN'S RESEARCH INSTITUTE · PI SHI, DASHUANG · 2004 to 2006
$373k
Molecular Regulation of UreagenesisK01DK076846 · NIDDK · CHILDREN'S RESEARCH INSTITUTE · PI CALDOVIC, LJUBICA MORIZONO · 2008 to 2010
$323k
NCRR NIH HHS M01 RR020359NCRR NIH HHS M01RR020359NCRR NIH HHS U54 RR019453NCRR NIH HHS U54RR019453NICHD NIH HHS P30 HD040677NICHD NIH HHS P30HD2697NICHD NIH HHS P30HD40677NICHD NIH HHS R01 HD058567NICHD NIH HHS R01HD058567NICHD NIH HHS U54 HD061221NICHD NIH HHS U54HD061221NIDDK NIH HHS K01 DK067935NIDDK NIH HHS K01DK067935NIDDK NIH HHS K01 DK076846NIDDK NIH HHS K01DK076846NIDDK NIH HHS R01 DK047870NIDDK NIH HHS R01 DK053761NIDDK NIH HHS R01 DK064913NIDDK NIH HHS R01DK064913NIDDK NIH HHS R01DK47870NIDDK NIH HHS R01DK53761
6 · The paper itself

Abstract

N-acetylglutamate (NAG) is a unique enzyme cofactor, essential for liver ureagenesis in mammals while it is the first committed substrate for de novo arginine biosynthesis in microorganisms and plants. The enzyme that produces NAG from glutamate and CoA, NAG synthase (NAGS), is allosterically inhibited by arginine in microorganisms and plants and activated in mammals. This transition of the allosteric effect occurred when tetrapods moved from sea to land. The first mammalian NAGS gene (from mouse) was cloned in 2002 and revealed significant differences from the NAGS ortholog in microorganisms. Almost all NAGS genes possess a C-terminus transferase domain in which the catalytic activity resides and an N-terminus kinase domain where arginine binds. The three-dimensional structure of NAGS shows two distinctly folded domains. The kinase domain binds arginine while the acetyltransferase domain contains the catalytic site. NAGS deficiency in humans leads to hyperammonemia and can be primary, due to mutations in the NAGS gene or secondary due to other mitochondrial aberrations that interfere with the normal function of the same enzyme. For either condition, N-carbamylglutamate (NCG), a stable functional analog of NAG, was found to either restore or improve the deficient urea-cycle function.

Indexed as

Amino-Acid N-AcetyltransferaseAmino Acid SequenceAnimalsBiocatalysisEvolution, MolecularHumansMolecular Sequence DataUrea Cycle Disorders, InbornAmino-Acid N-Acetyltransferase

Identifiers

PMID20303810
PMCPMC2876818
OpenAlexW2006497160

What OpenQuestion holds

Textmetadata
LicenceTDM
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.