Evidence map›Paper›PMID 26291722›Full record

ArticlePloS one2015

Structural Model of the Bilitranslocase Transmembrane Domain Supported by NMR and FRET Data.

Amrita Roy Choudhury, Emilia Sikorska, Johannes van den Boom, Peter Bayer, Łukasz Popenda, Kosma Szutkowski, Stefan Jurga, Massimiliano Bonomi, Andrej Sali, Igor Zhukov and 2 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.9field-weighted citation impact, top 23% 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

6 citing papers in PubMed, 10 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

12 authors at 8 institutions in 6 countries.

Amrita Roy ChoudhuryNational Institute of Chemistry, Hajdrihova 19, Ljubljana, Slovenia.
Emilia SikorskaFaculty of Chemistry, University of Gdańsk, Gdańsk, Poland.
Johannes van den BoomInstitute for Structural and Medicinal Biochemistry, Center for Medical Biotechnology, University of Duisburg-Essen, Essen, Germany.
Peter BayerInstitute for Structural and Medicinal Biochemistry, Center for Medical Biotechnology, University of Duisburg-Essen, Essen, Germany.
Łukasz PopendaNanoBioMedical Center, Adam Mickiewicz University, Poznań, Poland.
Kosma SzutkowskiNanoBioMedical Center, Adam Mickiewicz University, Poznań, Poland; Faculty of Physics, Adam Mickiewicz University, Poznań, Poland.
Stefan JurgaNanoBioMedical Center, Adam Mickiewicz University, Poznań, Poland; Faculty of Physics, Adam Mickiewicz University, Poznań, Poland.
Massimiliano BonomiDepartment of Chemistry, University of Cambridge, Cambridge, United Kingdom; Department of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, University of California, San Francisco, California, United States of America.
Andrej SaliDepartment of Bioengineering and Therapeutic Sciences, Department of Pharmaceutical Chemistry, and California Institute for Quantitative Biosciences, University of California, San Francisco, California, United States of America.
Igor ZhukovNanoBioMedical Center, Adam Mickiewicz University, Poznań, Poland; Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Warsaw, Poland.
Sabina PassamontiDepartment of Life Sciences, University of Trieste, Trieste, Italy.
Marjana NovičNational Institute of Chemistry, Hajdrihova 19, Ljubljana, Slovenia.
Adam Mickiewicz University in Poznań · PLNational Institute of Chemistry · SIUniversity of Duisburg-Essen · DEInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PLQB3 · USUniversity of California, San Francisco · USUniversity of Gdańsk · PLUniversity of Trieste · IT

Funding

IMP: Software for Hybrid Determination of Macromolecular Assembly StructuresR01GM083960 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SALI, ANDREJ · 2008 to 2024
$5.2M
NIGMS NIH HHS R01 GM083960
6 · The paper itself

Abstract

We present a 3D model of the four transmembrane (TM) helical regions of bilitranslocase (BTL), a structurally uncharacterized protein that transports organic anions across the cell membrane. The model was computed by considering helix-helix interactions as primary constraints, using Monte Carlo simulations. The interactions between the TM2 and TM3 segments have been confirmed by Förster resonance energy transfer (FRET) spectroscopy and nuclear magnetic resonance (NMR) spectroscopy, increasing our confidence in the model. Several insights into the BTL transport mechanism were obtained by analyzing the model. For example, the observed cis-trans Leu-Pro peptide bond isomerization in the TM3 fragment may indicate a key conformational change during anion transport by BTL. Our structural model of BTL may facilitate further studies, including drug discovery.

Indexed as

Cell MembraneCeruloplasminFluorescence Resonance Energy TransferHumansMembrane ProteinsMicellesModels, StructuralMonte Carlo MethodNuclear Magnetic Resonance, BiomolecularProtein Structure, SecondaryProtein Structure, TertiarybilitranslocaseCeruloplasminMembrane ProteinsMicelles

Identifiers

PMID26291722
PMCPMC4546402
OpenAlexW2280269174

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.