Evidence map›Paper›PMID 25148702›Full record

ArticleBiochimica et biophysica acta2014

HIV-1 Tat membrane interactions probed using X-ray and neutron scattering, CD spectroscopy and MD simulations.

Kiyotaka Akabori, Kun Huang, Bradley W Treece, Michael S Jablin, Brian Maranville, Arthur Woll, John F Nagle, Angel E Garcia, Stephanie Tristram-Nagle

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2014. 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
1.4field-weighted citation impact, top 18% 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, 29 citations in OpenAlex.

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  12. Physics of HIV.Journal of physics D: Applied physics · 2018
    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 at 4 institutions in 1 country.

Kiyotaka AkaboriDepartment of Physics, Carnegie Mellon University, 5000 Forbes Avenue, Pittsburgh, PA, United States.
Kun HuangDepartment of Physics, Rensselaer Polytechnic Institute, 110 Eighth Street, Troy, NY 12180, United States.
Bradley W TreeceDepartment of Physics, Carnegie Mellon University, 5000 Forbes Avenue, Pittsburgh, PA, United States.
Michael S JablinDepartment of Physics, Carnegie Mellon University, 5000 Forbes Avenue, Pittsburgh, PA, United States.
Brian MaranvilleNIST Center for Neutron Research, 100 Bureau Drive, Stop 6102, Gaithersburg, MD 20899, United States.
Arthur WollCHESS, Cornell University, 161 Synchrotron Drive, Ithaca, NY 14853, United States.
John F NagleDepartment of Physics, Carnegie Mellon University, 5000 Forbes Avenue, Pittsburgh, PA, United States.
Angel E GarciaDepartment of Physics, Rensselaer Polytechnic Institute, 110 Eighth Street, Troy, NY 12180, United States.
Stephanie Tristram-NagleDepartment of Physics, Carnegie Mellon University, 5000 Forbes Avenue, Pittsburgh, PA, United States. Electronic address: stn@cmu.edu.
Carnegie Mellon University · USRensselaer Polytechnic Institute · USCornell University · USNIST Center for Neutron Research · US

Funding

STRUCTURE OF LIPID BILAYERSR01GM044976 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI NAGLE, JOHN F, TRISTRAM-NAGLE, STEPHANIE · 1990 to 2014
$3.1M
Simulation studies of the mechanism of translocation of cell penetrating peptidesR01GM086801 · NIGMS · RENSSELAER POLYTECHNIC INSTITUTE · PI GARCIA, ANGEL E · 2010 to 2013
$1.2M
NIGMS NIH HHS R01 GM044976NIGMS NIH HHS R01 GM086801
6 · The paper itself

Abstract

We report the effect on lipid bilayers of the Tat peptide Y47GRKKRRQRRR57 from the HIV-1 virus transactivator of translation (Tat) protein. Synergistic use of low-angle X-ray scattering (LAXS) and atomistic molecular dynamic simulations (MD) indicate Tat peptide binding to neutral dioleoylphosphocholine (DOPC) lipid headgroups. This binding induced the local lipid phosphate groups to move 3Å closer to the center of the bilayer. Many of the positively charged guanidinium components of the arginines were as close to the center of the bilayer as the locally thinned lipid phosphate groups. LAXS data for DOPC, DOPC/dioleoylphosphoethanolamine (DOPE), DOPC/dioleoylphosphoserine (DOPS), and a mimic of the nuclear membrane gave similar results. Generally, the Tat peptide decreased the bilayer bending modulus KC and increased the area/lipid. Further indications that Tat softens a membrane, thereby facilitating translocation, were provided by wide-angle X-ray scattering (WAXS) and neutron scattering. CD spectroscopy was also applied to further characterize Tat/membrane interactions. Although a mechanism for translation remains obscure, this study suggests that the peptide/lipid interaction makes the Tat peptide poised to translocate from the headgroup region.

Indexed as

Lipid bilayer structure cell-penetrating peptideLow-angle X-ray scattering (LAXS)Membrane poreMolecular dynamics (MD) simulationsPeptide translocationWide-angle X-ray scattering (WAXS)

Identifiers

PMID25148702
PMCPMC4610132
OpenAlexW2172180260

What OpenQuestion holds

Textmetadata
LicenceTDM
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.