Evidence map›Paper›PMID 28300777›Full record

ArticleToxins2017

Functional Contributions of Positive Charges in the Pore-Lining Helix 3 of the Bordetella pertussis CyaA-Hemolysin to Hemolytic Activity and Ion-Channel Opening.

Chattip Kurehong, Chalermpol Kanchanawarin, Busaba Powthongchin, Panchika Prangkio, Gerd Katzenmeier, Chanan Angsuthanasombat

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Toxins, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.1field-weighted citation impact, top 26% 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

3 citing papers in PubMed, 7 citations in OpenAlex.

  1. Review
  2. Article
  3. Bioengineering ofToxins · 2018
    Review
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 4 institutions in 1 country.

Chattip KurehongBacterial Protein Toxin Research Cluster, Institute of Molecular Biosciences, Mahidol University, Salaya Campus, Nakornpathom 73170, Thailand. chattipk@gmail.com.
Chalermpol KanchanawarinLaboratory of Theoretical and Computational Biophysics, Department of Physics, Faculty of Science, Kasetsart University, Bangkok 10900, Thailand. katzenmeier.ger@mahidol.ac.th.
Busaba PowthongchinDepartment of Biopharmacy, Faculty of Pharmacy, Silpakorn University, Nakornpathom 73000, Thailand. fscicpk@ku.ac.th.
Panchika PrangkioDivision of Biochemistry and Biochemical Technology, Department of Chemistry, Faculty of Science, Chiang Mai University, Chiang Mai 50200, Thailand. p.busaba.su@gmail.com.
Gerd KatzenmeierBacterial Protein Toxin Research Cluster, Institute of Molecular Biosciences, Mahidol University, Salaya Campus, Nakornpathom 73170, Thailand. panchikap@gmail.com.
Chanan AngsuthanasombatBacterial Protein Toxin Research Cluster, Institute of Molecular Biosciences, Mahidol University, Salaya Campus, Nakornpathom 73170, Thailand. chanan.ang@mahidol.ac.th.
Mahidol University · THChiang Mai University · THKasetsart University · THSilpakorn University · TH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Bordetella pertussis CyaA-hemolysin (CyaA-Hly) domain was previously demonstrated to be an important determinant for hemolysis against target erythrocytes and ion-channel formation in planar lipid bilayers (PLBs). Here, net-charge variations in the pore-lining helix of thirteen related RTX cytolysins including CyaA-Hly were revealed by amino acid sequence alignments, reflecting their different degrees of hemolytic activity. To analyze possible functional effects of net-charge alterations on hemolytic activity and channel formation of CyaA-Hly, specific mutations were made at Gln

Indexed as

HemolysisIon Channel GatingAdenylate Cyclase ToxinAmino Acid SequenceAnimalsErythrocytesEscherichia coliHemolysin ProteinsSequence AlignmentSheepAdenylate Cyclase ToxinHemolysin ProteinsBordetella pertussischannel-open lifetimeCyaA-hemolysinMD simulationspore-lining helixRTX cytolysintrimeric pore

Identifiers

PMID28300777
PMCPMC5371864
OpenAlexW2596980296

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.