Evidence map›Paper›PMID 27815499›Full record

ArticleThe Journal of biological chemistry2016

Evolution of Negative Cooperativity in Glutathione Transferase Enabled Preservation of Enzyme Function.

Alessio Bocedi, Raffaele Fabrini, Mario Lo Bello, Anna Maria Caccuri, Giorgio Federici, Bengt Mannervik, Athel Cornish-Bowden, Giorgio Ricci

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-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

13 citing papers in PubMed, 28 citations in OpenAlex.

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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

8 authors at 3 institutions in 3 countries.

Alessio BocediFrom the Department of Chemical Sciences and Technologies.
Raffaele FabriniFrom the Department of Chemical Sciences and Technologies.
Mario Lo BelloDepartment of Biology, and.
Anna Maria CaccuriDepartment of Experimental Medicine and Surgery, University of Rome, Tor Vergata, Rome 00133, Italy.
Giorgio FedericiFrom the Department of Chemical Sciences and Technologies.
Bengt MannervikDepartment of Neurochemistry, Stockholm University SE-10691 Stockholm, Sweden, and.
Athel Cornish-BowdenAix Marseille Université, CNRS, Bioénergétique et Ingénierie des Protéines, Institut de Microbiologie de la Méditerranée, 13009 Marseille, France.
Giorgio RicciFrom the Department of Chemical Sciences and Technologies, riccig@uniroma2.it.
University of Rome Tor Vergata · ITAix-Marseille Université · FRStockholm University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Negative cooperativity in enzyme reactions, in which the first event makes subsequent events less favorable, is sometimes well understood at the molecular level, but its physiological role has often been obscure. Negative cooperativity occurs in human glutathione transferase (GST) GSTP1-1 when it binds and neutralizes a toxic nitric oxide adduct, the dinitrosyl-diglutathionyl iron complex (DNDGIC). However, the generality of this behavior across the divergent GST family and its evolutionary significance were unclear. To investigate, we studied 16 different GSTs, revealing that negative cooperativity is present only in more recently evolved GSTs, indicating evolutionary drift in this direction. In some variants, Hill coefficients were close to 0.5, the highest degree of negative cooperativity commonly observed (although smaller values of n

Indexed as

Evolution, MolecularCrystallography, X-RayFerrous CompoundsGlutathioneGlutathione TransferaseHumansKineticsNitric Oxidedinitrosylbis(glutathione)iron(II)Ferrous CompoundsGlutathioneGlutathione TransferaseNitric Oxideenzymeenzyme inactivationenzyme kineticsenzyme mechanismenzyme structure

Identifiers

PMID27815499
PMCPMC5207182
OpenAlexW2548652796

What OpenQuestion holds

Textmetadata
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.