Evidence map›Paper›PMID 29064083›Full record

ArticleJournal of computer-aided molecular design2017

New insights into flavivirus biology: the influence of pH over interactions between prM and E proteins.

Edson R A Oliveira, Ricardo B de Alencastro, Bruno A C Horta

Abstract read
PubMed Publisher
In one paragraph

Article in Journal of computer-aided molecular design, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.7field-weighted citation impact, top 14% 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

11 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Mechanisms of Zika astrocyte infection and neuronal toxicity.NeuroImmune pharmacology and therapeutics · 2023
    Article
  3. Review
  4. An overview of Zika virus genotypes and their infectivity.Revista da Sociedade Brasileira de Medicina Tropical · 2022
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
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.

Edson R A OliveiraInstituto de Química - Universidade Federal do Rio de Janeiro, Av. Athos da Silveira Ramos, 149 Centro de Tecnologia, Bloco A, Sala 609, Cidade Universitária, Rio de Janeiro, RJ, CEP: 21941-909, Brazil.
Ricardo B de AlencastroInstituto de Química - Universidade Federal do Rio de Janeiro, Av. Athos da Silveira Ramos, 149 Centro de Tecnologia, Bloco A, Sala 609, Cidade Universitária, Rio de Janeiro, RJ, CEP: 21941-909, Brazil.
Bruno A C HortaInstituto de Química - Universidade Federal do Rio de Janeiro, Av. Athos da Silveira Ramos, 149 Centro de Tecnologia, Bloco A, Sala 609, Cidade Universitária, Rio de Janeiro, RJ, CEP: 21941-909, Brazil. bruno@iq.ufrj.br.ORCID http://orcid.org/0000-0002-3952-1474
Universidade Federal do Rio de Janeiro · BR

Funding

Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro E-26/010.002420/2016Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro E-26/201.258/2015Fundação Carlos Chagas Filho de Amparo à Pesquisa do Estado do Rio de Janeiro E-26/203.198/2016
6 · The paper itself

Abstract

Diseases caused by flaviviruses, such as dengue and zika, are globally recognized as major threats. During infection, a critical point in their replicative cycle is the maturation step, which occurs throughout the cellular exocytic pathway. This step is a pH-dependent process that involves the modification of the viral envelope by converting prM (pre-membrane) into M (membrane) proteins with the release of a "pr peptide". After this reaction, the pr peptides remain bound to the viral envelope while the virions cross the acidic trans-Golgi network, and are released only at neutral pH after secretion of the virus particles. Despite this current knowledge, the molecular basis of the flavivirus maturation step is largely unknown. Here, based on the crystal structure of the dengue pr-E complex ("pr peptide" bound to virus envelope protein) and using molecular dynamics simulations, we found that the pH shift from acidic to neutral yields considerable structural changes in the system. Dynamic cross correlation maps and root mean square deviation analyses revealed that the pr-E junction is clearly unstable under neutral pH. Secondary structure analysis also revealed that the fusion loop region, present in the E protein, is sensitive to pH and tends to unstructure at a neutral environment. Moreover, we found that five residues present in the E protein, Gly

Indexed as

Molecular Dynamics SimulationBinding SitesDengue VirusHumansHydrogen-Ion ConcentrationProtein BindingProtein Structure, SecondaryViral Envelope ProteinsZika VirusprM protein, FlavivirusViral Envelope ProteinsEnvelopeFlavivirusMaturationMolecular dynamicsMolecular modelingPre-membrane

Identifiers

PMID29064083
OpenAlexW2765166360

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.