Evidence map›Paper›PMID 20540583›Full record

ArticleThe journal of physical chemistry. B2010

Impact of distant charge reversals within a robust beta-barrel protein pore.

Mohammad M Mohammad, Liviu Movileanu

Open access · greenAbstract read
In one paragraph

Article in The journal of physical chemistry. B, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.5field-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

25 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Detergent Desorption of Membrane Proteins Exhibits Two Kinetic Phases.The journal of physical chemistry letters · 2018
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Global redesign of a native β-barrel scaffold.Biochimica et biophysica acta · 2016
    Article
  12. Article
  13. Article
  14. Review
  15. Watching single proteins using engineered nanopores.Protein and peptide letters · 2014
    Review
  16. Article
  17. Article
  18. Review
  19. Article
  20. Article
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

2 authors at 1 institution in 1 country.

Mohammad M MohammadDepartment of Physics, Syracuse University, 201 Physics Building, Syracuse, New York 13244-1130, USA.
Liviu Movileanu
Syracuse University · US

Funding

Engineered Nanopores for Single-Molecule Stochastic SensingR01GM088403 · NIGMS · SYRACUSE UNIVERSITY · PI MOVILEANU, LIVIU · 2009 to 2022
$3.8M
NIGMS NIH HHS R01 GM088403
6 · The paper itself

Abstract

Among all beta-barrel pores, staphylococcal alpha-hemolysin (alphaHL), a heptameric transmembrane protein of known high-resolution crystal structure, features a high stability in planar lipid bilayers under a wide range of harsh experimental conditions. Here, we employed single-channel electrical recordings and standard protein engineering to explore the impact of two distant charge reversals within the interior of the beta-barrel part of the pore. The charge reversals were replacements of lysines with aspartic acids. A charge reversal within the structurally stiff region of the beta barrel near the pore constriction reduced the open-state current of the pore, but produced a quiet pore, showing current fluctuation-free channel behavior. In contrast, a charge reversal on the trans entrance, within the structurally flexible glycine-rich turn of the beta barrel, increased the open-state current and produced gating activity of the pore in the form of large-amplitude and frequent current fluctuations. Remarkably, cumulative insertion of the two distant charge reversals resulted in a large-amplitude permanent blockade of the beta barrel, as judged by both single-channel and macroscopic current measurements. The results from this work suggest that these distant charge reversals are energetically coupled, producing different impacts on the ionic transport, the unitary conductance and the open-state probability of the pore.

Indexed as

Amino Acid SequenceBacterial ProteinsBacterial ToxinsElectric ConductivityHemolysin ProteinsIon Channel GatingModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutationPorosityProtein MultimerizationProtein StabilityProtein Structure, QuaternaryProtein Structure, SecondaryStaphylococcusBacterial ProteinsBacterial ToxinsHemolysin Proteinsstaphylococcal alpha-toxin

Identifiers

PMID20540583
PMCPMC2907733
OpenAlexW2035272291

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.