Evidence map›Paper›PMID 28076788›Full record

ArticleCell reports2017

Dynamin-2 Stabilizes the HIV-1 Fusion Pore with a Low Oligomeric State.

Daniel M Jones, Luis A Alvarez, Rory Nolan, Margarita Ferriz, Raquel Sainz Urruela, Xènia Massana-Muñoz, Hila Novak-Kotzer, Michael L Dustin, Sergi Padilla-Parra

Abstract read
In one paragraph

Article in Cell reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Article
  2. Dynole 34-2 and Acrylo-Dyn 2-30, Novel Dynamin GTPase Chemical Biology Probes.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
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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

9 authors.

Daniel M JonesDivision of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford OX3 7BN, UK.
Luis A AlvarezWellcome Trust Human Genetics, Cellular Imaging Core, University of Oxford, Oxford OX3 7BN, UK.
Rory NolanDivision of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford OX3 7BN, UK.
Margarita FerrizDivision of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford OX3 7BN, UK.
Raquel Sainz UrruelaWellcome Trust Human Genetics, Cellular Imaging Core, University of Oxford, Oxford OX3 7BN, UK.
Xènia Massana-MuñozDivision of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford OX3 7BN, UK.
Hila Novak-KotzerThe Kennedy Institute of Rheumatology, University of Oxford, Headington, Oxford OX3 7BN, UK.
Michael L DustinThe Kennedy Institute of Rheumatology, University of Oxford, Headington, Oxford OX3 7BN, UK.
Sergi Padilla-ParraDivision of Structural Biology, University of Oxford, The Henry Wellcome Building for Genomic Medicine, Headington, Oxford OX3 7BN, UK; Wellcome Trust Human Genetics, Cellular Imaging Core, University of Oxford, Oxford OX3 7BN, UK. Electronic address: spadilla@well.ox.ac.uk.

Funding

Wellcome TrustWellcome Trust 090532/Z/09/ZWellcome Trust 100262/Z/12/Z
6 · The paper itself

Abstract

One of the key research areas surrounding HIV-1 concerns the regulation of the fusion event that occurs between the virus particle and the host cell during entry. Even if it is universally accepted that the large GTPase dynamin-2 is important during HIV-1 entry, its exact role during the first steps of HIV-1 infection is not well characterized. Here, we have utilized a multidisciplinary approach to study the DNM2 role during fusion of HIV-1 in primary resting CD4 T and TZM-bl cells. We have combined advanced light microscopy and functional cell-based assays to experimentally assess the role of dynamin-2 during these processes. Overall, our data suggest that dynamin-2, as a tetramer, might help to establish hemi-fusion and stabilizes the pore during HIV-1 fusion.

Indexed as

Membrane FusionProtein MultimerizationCD4-Positive T-LymphocytesCell CountCell FusionDynamin IIFluorescence Resonance Energy TransferGenes, ReporterHEK293 CellsHIV-1HumansHydrazonesKineticsModels, BiologicalVirionVirus InternalizationDynamin IIHydrazonesN'-(3,4-dihydroxybenzylidene)-3-hydroxy-2-naphthahydrazideadvanced light imagingcell-cell fusionDynamin-2HIV-1 fusionnumber and brightness

Identifiers

PMID28076788
PMCPMC5263234

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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.