Evidence map›Paper›PMID 17114231›Full record

ArticleBiophysical journal2007

Membrane simulations of OpcA: gating in the loops?

Peter J Bond, Jeremy P Derrick, Mark S P Sansom

Open access · bronzeAbstract readLetter
In one paragraph

Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.8field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 35 citations in OpenAlex.

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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

3 authors at 2 institutions in 1 country.

Peter J Bond
Jeremy P Derrick
Mark S P Sansom
University of Oxford · GBUniversity of Manchester · GB

Funding

Biotechnology and Biological Sciences Research Council B19456Biotechnology and Biological Sciences Research Council BBS/B/16011Biotechnology and Biological Sciences Research Council BEP17032
6 · The paper itself

Abstract

Mobility of extracellular loops may play an important role in the function of outer membrane proteins from Gram-negative bacteria. Molecular dynamics simulations of OpcA from Neisseria meningitidis, embedded in a lipid bilayer, have been used to explore the relationship between the crystal structure and dynamic function of this protein. The results suggest that the crystal environment may constrain the membrane protein structure in a nonphysiological state. The presence of lipids and physiological salt concentrations result in changes in the conformation of the extracellular loops of OpcA, leading to opening of a pore, and to modulation of the molecular surface implicated in recognition of proteoglycan. These changes may be related to the role of OpcA in pathogenesis via modulation of the conformation of a possible sialic acid binding site.

Indexed as

Ion Channel GatingModels, ChemicalModels, MolecularBacterial Outer Membrane ProteinsCell MembraneComputer SimulationLipid BilayersProtein ConformationBacterial Outer Membrane ProteinsLipid BilayersOpcA protein, Neisseria meningitidis

Identifiers

PMID17114231
PMCPMC1751375
OpenAlexW2094639723

What OpenQuestion holds

Textmetadata
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.