Evidence map›Paper›PMID 26143069›Full record

ArticleJournal of biomolecular NMR2015

Backbone structure of Yersinia pestis Ail determined in micelles by NMR-restrained simulated annealing with implicit membrane solvation.

Francesca M Marassi, Yi Ding, Charles D Schwieters, Ye Tian, Yong Yao

Open access · greenAbstract read
In one paragraph

Article in Journal of biomolecular NMR, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
3.0field-weighted citation impact, top 8% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

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  14. Applications of NMR to membrane proteins.Archives of biochemistry and biophysics · 2017
    Review
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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

5 authors at 2 institutions in 1 country.

Francesca M MarassiSanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA, 92037, USA. fmarassi@sbmri.org.
Yi DingSanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA, 92037, USA.
Charles D SchwietersDivision of Computational Bioscience, Center for Information Technology, National Institutes of Health, Building 12A, Bethesda, MD, 20892-5624, USA.
Ye TianSanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA, 92037, USA.
Yong YaoSanford-Burnham Medical Research Institute, 10901 North Torrey Pines Road, La Jolla, CA, 92037, USA.
Sanford Burnham Prebys Medical Discovery Institute · USNational Institutes of Health · US

Funding

Tumor Microenvironment and Cancer ImmunologyP30CA030199 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI ELENA B PASQUALE · 1985 to 2026
$107.2M
RESOURCE FOR SOLID STATE NMR OF PROTEINSP41EB002031 · NIBIB · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI OPELLA, STANLEY J · 2003 to 2018
$16.3M
Biomedical ImagingZIACT000090 · CIT · CENTER FOR INFORMATION TECHNOLOGY · PI TRUS, BENES L · 2009 to 2018
$7.8M
Host recognition by pathogenic yersiniaeR01GM100265 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MARASSI, FRANCESCA M · 2012 to 2015
$1.7M
Membrane protein structure in lipido: computational developments.R01GM110658 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI MARASSI, FRANCESCA M · 2014 to 2015
$702k
Intramural NIH HHSNCI NIH HHS P30 CA030199NCI NIH HHS P30CA030199NIBIB NIH HHS P41 EB002031NIBIB NIH HHS P41EB002031NIGMS NIH HHS R01 GM100265NIGMS NIH HHS R01GM100265NIGMS NIH HHS R01 GM110658NIGMS NIH HHS R01GM110658
6 · The paper itself

Abstract

The outer membrane protein Ail (attachment invasion locus) is a virulence factor of Yersinia pestis that mediates cell invasion, cell attachment and complement resistance. Here we describe its three-dimensional backbone structure determined in decyl-phosphocholine (DePC) micelles by NMR spectroscopy. The NMR structure was calculated using the membrane function of the implicit solvation potential, eefxPot, which we have developed to facilitate NMR structure calculations in a physically realistic environment. We show that the eefxPot force field guides the protein towards its native fold. The resulting structures provide information about the membrane-embedded global position of Ail, and have higher accuracy, higher precision and improved conformational properties, compared to the structures calculated with the standard repulsive potential.

Indexed as

Computer SimulationMicellesNuclear Magnetic Resonance, BiomolecularBacterial Outer Membrane ProteinsCell MembraneModels, MolecularPhosphorylcholineReproducibility of ResultsSolventsVirulence FactorsYersinia pestisAil protein, Yersinia pestisBacterial Outer Membrane ProteinsMicellesPhosphorylcholineSolventsVirulence FactorsAilImplicit solvationMembrane proteinNMRStructureYersinia pestis

Identifiers

PMID26143069
PMCPMC4577439
OpenAlexW2207931586

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.