Evidence map›Paper›PMID 28511544›Full record

ArticleBiointerphases2017

Structural characterization of membrane-bound human immunodeficiency virus-1 Gag matrix with neutron reflectometry.

Rebecca Eells, Marilia Barros, Kerry M Scott, Ioannis Karageorgos, Frank Heinrich, Mathias Lösche

Abstract read
In one paragraph

Article in Biointerphases, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing 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

8 citing papers in PubMed.

  1. Cooperative Membrane Binding of HIV-1 Matrix Proteins.The journal of physical chemistry. B · 2024
    Article
  2. Article
  3. Article
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  5. Article
  6. Uncovering a membrane-distal conformation of KRAS available to recruit RAF to the plasma membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  7. Article
  8. Article
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

6 authors.

Rebecca EellsDepartment of Physics, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213.
Marilia BarrosMemorial Sloan Kettering Cancer Center, New York, New York 10065.
Kerry M ScottBiomolecular Measurement Division, National Institute of Standards and Technology, Gaithersburg, Maryland 20899 and Institute for Bioscience and Biotechnology Research, Rockville, Maryland 20850.
Ioannis KarageorgosBiomolecular Measurement Division, National Institute of Standards and Technology, Gaithersburg, Maryland 20899 and Institute for Bioscience and Biotechnology Research, Rockville, Maryland 20850.
Frank HeinrichDepartment of Physics, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213 and NIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland 20899.
Mathias LöscheDepartments of Physics and Biomedical Engineering, Carnegie Mellon University, Pittsburgh, Pennsylvania 15213 and NIST Center for Neutron Research, National Institute of Standards and Technology, Gaithersburg, Maryland 20899.

Funding

Training in the Molecular Biophysics and Structural BiologyT32GM088119 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI HINCK, ANDREW P · 2011 to 2020
$1.6M
Membrane Coupling and Dynamic Reorganization of Gag in Viral BuddingR01GM101647 · NIGMS · CARNEGIE-MELLON UNIVERSITY · PI LOESCHE, MATHIAS · 2012 to 2015
$1.2M
NIGMS NIH HHS R01 GM101647NIGMS NIH HHS T32 GM088119
6 · The paper itself

Abstract

The structural characterization of peripheral membrane proteins represents a tremendous challenge in structural biology due to their transient interaction with the membrane and the potential multitude of protein conformations during this interaction. Neutron reflectometry is uniquely suited to address this problem because of its ability to structurally characterize biological model systems nondestructively and under biomimetic conditions that retain full protein functionality. Being sensitive to only the membrane-bound fraction of a water-soluble peripheral protein, neutron reflectometry obtains a low-resolution average structure of the protein-membrane complex that is further refined using integrative modeling strategies. Here, the authors review the current technological state of biological neutron reflectometry exemplified by a detailed report on the structure determination of the myristoylated human immunodeficiency virus-1 (HIV-1) Gag matrix associated with phosphoserine-containing model membranes. The authors found that the HIV-1 Gag matrix is able to adopt different configurations at the membrane in a pH-dependent manner and that the myristate group orients the protein in a way that is conducive to PIP

Indexed as

LipoylationMembranes, ArtificialNeutron DiffractionCell Membranegag Gene Products, Human Immunodeficiency VirusHIV-1HumansPhosphoserinegag Gene Products, Human Immunodeficiency VirusMembranes, ArtificialPhosphoserine

Identifiers

PMID28511544
PMCPMC5433906

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.