Evidence map›Paper›PMID 29694437›Full record

ArticlePloS one2018

A molecular dynamics study of adenylyl cyclase: The impact of ATP and G-protein binding.

Elisa Frezza, Juliette Martin, Richard Lavery

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

16 citing papers in PubMed, 24 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

3 authors at 1 institution in 1 country.

Elisa FrezzaMMSB, Univ. Lyon I / CNRS UMR 5086, Institut de Biologie et Chimie des Protéines, Lyon, France.ORCID 0000-0003-0122-7859
Juliette MartinMMSB, Univ. Lyon I / CNRS UMR 5086, Institut de Biologie et Chimie des Protéines, Lyon, France.ORCID 0000-0002-4787-0885
Richard LaveryMMSB, Univ. Lyon I / CNRS UMR 5086, Institut de Biologie et Chimie des Protéines, Lyon, France.ORCID 0000-0001-9901-6640
Université Claude Bernard Lyon 1 · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adenylyl cyclases (ACs) catalyze the biosynthesis of cyclic adenosine monophosphate (cAMP) from adenosine triphosphate (ATP) and play an important role in many signal transduction pathways. The enzymatic activity of ACs is carefully controlled by a variety of molecules, including G-protein subunits that can both stimulate and inhibit cAMP production. Using homology models developed from existing structural data, we have carried out all-atom, microsecond-scale molecular dynamics simulations on the AC5 isoform of adenylyl cyclase and on its complexes with ATP and with the stimulatory G-protein subunit Gsα. The results show that both ATP and Gsα binding have significant effects on the structure and flexibility of adenylyl cyclase. New data on ATP bound to AC5 in the absence of Gsα notably help to explain how Gsα binding enhances enzyme activity and could aid product release. Simulations also suggest a possible coupling between ATP binding and interactions with the inhibitory G-protein subunit Gαi.

Indexed as

Adenosine TriphosphateAdenylyl CyclasesAnimalsBinding SitesGTP-Binding ProteinsMiceModels, MolecularMolecular Dynamics SimulationProtein BindingStructural Homology, ProteinAdenosine TriphosphateAdenylyl Cyclasesadenylyl cyclase type VGTP-Binding Proteins

Identifiers

PMID29694437
PMCPMC5918993
OpenAlexW2801612845

What OpenQuestion holds

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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.