Evidence map›Paper›PMID 24674984›Full record

ReviewBiochimica et biophysica acta2014

Zooming in on disordered systems: neutron reflection studies of proteins associated with fluid membranes.

Frank Heinrich, Mathias Lösche

Open access · greenAbstract readReview
In one paragraph

Review 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 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 94 citations in OpenAlex.

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  18. The hanging heart: How KRAS lures its prey to the membrane.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. 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
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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

2 authors at 1 institution in 1 country.

Frank HeinrichPhysics Department, Carnegie Mellon University, Pittsburgh, PA, U.S.A.; NIST Center for Neutron Research, Gaithersburg, MD, U.S.A.
Mathias LöschePhysics Department, Carnegie Mellon University, Pittsburgh, PA, U.S.A.; NIST Center for Neutron Research, Gaithersburg, MD, U.S.A.. Electronic address: quench@cmu.edu.
NIST Center for Neutron Research · US

Funding

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 1R01 GM101647NIGMS NIH HHS R01 GM101647
6 · The paper itself

Abstract

Neutron reflectometry (NR) is an emerging experimental technique for the structural characterization of proteins interacting with fluid bilayer membranes under conditions that mimic closely the cellular environment. Thus, cellular processes can be emulated in artificial systems and their molecular basis studied by adding cellular components one at a time in a well-controlled environment while the resulting structures, or structural changes in response to external cues, are monitored with neutron reflection. In recent years, sample environments, data collection strategies and data analysis were continuously refined. The combination of these improvements increases the information which can be obtained from NR to an extent that enables structural characterization of protein-membrane complexes at a length scale that exceeds the resolution of the measurement by far. Ultimately, the combination of NR with molecular dynamics (MD) simulations can be used to cross-validate the results of the two techniques and provide atomic-scale structural models. This review discusses these developments in detail and demonstrates how they provide new windows into relevant biomedical problems. This article is part of a Special Issue entitled: Interfacially Active Peptides and Proteins. Guest Editors: William C. Wimley and Kalina Hristova.

Indexed as

Molecular Dynamics SimulationHumansLipid BilayersMembrane ProteinsModels, MolecularNeutronsPeptidesProtein Structure, SecondaryLipid BilayersMembrane ProteinsPeptidesComposition-space modelingMD simulationMembrane proteinMembrane structureScattering techniques

Identifiers

PMID24674984
PMCPMC4082750
OpenAlexW2017134979

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.