Evidence map›Paper›PMID 19506851›Full record

ArticleEuropean biophysics journal : EBJ2010

Structural implications of mutations assessed by molecular dynamics: Vpu1-32 from HIV-1.

J Krüger, Wolfgang B Fischer

Abstract read
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In one paragraph

Article in European biophysics journal : EBJ, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

6 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Viral channel forming proteins - modeling the target.Biochimica et biophysica acta · 2011
    Review
  5. Article
  6. 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

2 authors.

J KrügerInstitute of Biophotonics, School of Biomedical Science and Engineering, National Yang-Ming University, 155, Sec. 2, Li-Nong St., Taipei, 112, Taiwan.
Wolfgang B Fischer

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural pore models are generated for Vpu(1-32)WT from HIV-1 as well as for three mutants W23L, S24L and R31V. A computational methodology is employed which samples the whole conformational space of the pentameric assemblies of Vpu. The analysis of the related energy landscape reveals a small set of reasonable pore models, which are thoroughly investigated regarding their structural properties as well as their putative stability under native-like conditions. The models are also discussed in respect of earlier experimental findings about their channel activities. The study proposes functional pores reflecting the experimentally found conductance states of Vpu and its mutants.

Indexed as

Molecular Dynamics SimulationMutation, MissenseHIV-1Human Immunodeficiency Virus ProteinsKineticsLipid BilayersPhosphatidylcholinesProtein ConformationProtein Structure, SecondaryViral Regulatory and Accessory ProteinsViroporin Proteins1-palmitoyl-2-oleoylphosphatidylcholineHuman Immunodeficiency Virus ProteinsLipid BilayersPhosphatidylcholinesViral Regulatory and Accessory ProteinsViroporin Proteinsvpu protein, Human immunodeficiency virus 1

Identifiers

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.