Evidence map›Paper›PMID 29079932›Full record

ReviewNeurochemical research2019

Glutamate Dehydrogenase, a Complex Enzyme at a Crucial Metabolic Branch Point.

Hong Q Smith, Changhong Li, Charles A Stanley, Thomas James Smith

Abstract readReview
In one paragraph

Review in Neurochemical research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

62 citing papers in PubMed, 123 citations in OpenAlex.

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2 more citing papers are in PubMed but not listed here.

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

4 authors at 2 institutions in 1 country.

Hong Q SmithDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch at Galveston, Galveston, TX, USA.
Changhong LiDivision of Endocrinology, The Children's Hospital of Philadelphia, Philadelphia, PA, USA.
Charles A StanleyDivision of Endocrinology, The Children's Hospital of Philadelphia, Philadelphia, PA, USA.
Thomas James SmithDepartment of Biochemistry and Molecular Biology, University of Texas Medical Branch at Galveston, Galveston, TX, USA. thosmith@UTMB.EDU.ORCID http://orcid.org/0000-0002-0978-1494
Children's Hospital of Philadelphia · USThe University of Texas Medical Branch at Galveston · US

Funding

Neurological Phenotyping in Hyperinsulinism – Administrative Supplement to Islet dysregulation in Infants with Congenital HyperinsulinismR01DK056268 · NIDDK · CHILDREN'S HOSP OF PHILADELPHIA · PI DE LEON, DIVA D., GANGULY, ARUPA · 1999 to 2024
$9.1M
Islet Dysregulation in Infants with Congenital HyperinsulinismR37DK056268 · NIDDK · CHILDREN'S HOSP OF PHILADELPHIA · PI STANLEY, CHARLES ALFRED · 2009 to 2017
$6.0M
Insulin Secretion in Hyperinsulinism Human IsletsR01DK098517 · NIDDK · CHILDREN'S HOSP OF PHILADELPHIA · PI DE LEON, DIVA D. · 2013 to 2023
$4.5M
Mechanisms of glutamate dehydrogenase allosteryR01DK072171 · NIDDK · DONALD DANFORTH PLANT SCIENCE CENTER · PI SMITH, THOMAS JAMES. · 2005 to 2008
$1.4M
NIDDK NIH HHS R01 DK056268NIDDK NIH HHS R01 DK072171NIDDK NIH HHS R01 DK098517NIDDK NIH HHS R37 DK056268NIH HHS DK056268NIH HHS DK072171NIH HHS DK098517
6 · The paper itself

Abstract

In-vitro, glutamate dehydrogenase (GDH) catalyzes the reversible oxidative deamination of glutamate to α-ketoglutarate (α-KG). GDH is found in all organisms, but in animals is allosterically regulated by a wide array of metabolites. For many years, it was not at all clear why animals required such complex control. Further, in both standard textbooks and some research publications, there has been some controversy as to the directionality of the reaction. Here we review recent work demonstrating that GDH operates mainly in the catabolic direction in-vivo and that the finely tuned network of allosteric regulators allows GDH to meet the varied needs in a wide range of tissues in animals. Finally, we review the progress in using pharmacological agents to activate or inhibit GDH that could impact a wide range of pathologies from insulin disorders to tumor growth.

Indexed as

AnimalsEnergy MetabolismEnzyme InhibitorsGlutamate DehydrogenaseGlutamic AcidHumansMetabolic DiseasesProtein BindingProtein Structure, SecondaryEnzyme InhibitorsGlutamate DehydrogenaseGlutamic AcidAllosteryGlutamate dehydrogenaseInsulin

Identifiers

PMID29079932
PMCPMC5924581
OpenAlexW2766197379

What OpenQuestion holds

Textmetadata
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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.