Evidence map›Paper›PMID 25218435›Full record

ArticleFEBS letters2014

Structure-function of cyanobacterial outer-membrane protein, Slr1270: homolog of Escherichia coli drug export/colicin import protein, TolC.

Rachna Agarwal, Stanislav Zakharov, S Saif Hasan, Christopher M Ryan, Julian P Whitelegge, William A Cramer

Open access · bronzeAbstract read
In one paragraph

Article in FEBS letters, 2014. 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
0.7field-weighted citation impact, top 30% 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

8 citing papers in PubMed, 19 citations in OpenAlex.

  1. Triple-Gene Overexpression of the AcrA-AcrB-TolC Transporter System inInternational journal of molecular sciences · 2024
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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

6 authors at 3 institutions in 3 countries.

Rachna AgarwalDepartment of Biological Sciences, Purdue University, West Lafayette, IN, United States; Molecular Biology Division, Bhabha Atomic Research Centre, Mumbai, India.
Stanislav ZakharovDepartment of Biological Sciences, Purdue University, West Lafayette, IN, United States; Institute of Basic Problems of Biology, Russian Academy of Sciences, Puschino, Moscow Region, Russian Federation.
S Saif HasanDepartment of Biological Sciences, Purdue University, West Lafayette, IN, United States.
Christopher M RyanPasarow Mass Spectrometry Laboratory, NPI-Semel Institute for Neuroscience and Human Behavior, UCLA, Los Angeles, CA, United States.
Julian P WhiteleggePasarow Mass Spectrometry Laboratory, NPI-Semel Institute for Neuroscience and Human Behavior, UCLA, Los Angeles, CA, United States.
William A CramerDepartment of Biological Sciences, Purdue University, West Lafayette, IN, United States. Electronic address: waclab@purdue.edu.
Purdue University West Lafayette · USBhabha Atomic Research Centre · INInstitute of Basic Biological Problems · RU

Funding

Transgenic Mouse Core Facility Shared Resource (TMCF-SR)P30CA023168 · NCI · PURDUE UNIVERSITY WEST LAFAYETTE · PI John Tesmer · 1985 to 2026
$43.4M
Transgenic & Knock-out MouseP30DK063491 · NIDDK · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI PETER J TONTONOZ · 2003 to 2026
$40.4M
Trans-Membrane Signaling in the Cytochrome b6f Lipoprotein ComplexR01GM038323 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI CRAMER, WILLIAM A. · 1987 to 2017
$5.1M
Structure-Function of Hetero-oligomeric Integral Membrane ProteinsR56GM038323 · NIGMS · PURDUE UNIVERSITY · PI CRAMER, WILLIAM A. · 2007 to 2007
$336k
NCI NIH HHS P30 CA023168NIDDK NIH HHS P30 DK063491NIGMS NIH HHS GM-038323NIGMS NIH HHS R01 GM038323NIGMS NIH HHS R56 GM038323
6 · The paper itself

Abstract

Compared to thylakoid and inner membrane proteins in cyanobacteria, no structure-function information is available presently for integral outer-membrane proteins (OMPs). The Slr1270 protein from the cyanobacterium Synechocystis 6803, over-expressed in Escherichia coli, was refolded, and characterized for molecular size, secondary structure, and ion-channel function. Refolded Slr1270 displays a single band in native-electrophoresis, has an α-helical content of 50-60%, as in E. coli TolC with which it has significant secondary-structure similarity, and an ion-channel function with a single-channel conductance of 80-200pS, and a monovalent ion (K(+):Cl(-)) selectivity of 4.7:1. The pH-dependence of channel conductance implies a role for carboxylate residues in channel gating, analogous to that in TolC.

Indexed as

Sequence Homology, Amino AcidAmino Acid SequenceBacterial Outer Membrane ProteinsEscherichia coli ProteinsLipid BilayersMembrane Transport ProteinsModels, MolecularMolecular Sequence DataProtein MultimerizationProtein RefoldingProtein Structure, QuaternaryProtein Structure, SecondarySequence AlignmentSynechocystisBacterial Outer Membrane ProteinsEscherichia coli ProteinsLipid BilayersMembrane Transport ProteinstolC protein, E coliCyanobacteriaIon channelOuter-membrane proteinsSecondary-structureSlr1270TolC

Identifiers

PMID25218435
PMCPMC4288923
OpenAlexW2030093968

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.