Evidence map›Paper›PMID 15326033›Full record

ArticleBiophysical journal2004

Permeation properties of an engineered bacterial OmpF porin containing the EEEE-locus of Ca2+ channels.

Henk Miedema, Anita Meter-Arkema, Jenny Wierenga, John Tang, Bob Eisenberg, Wolfgang Nonner, Hans Hektor, Dirk Gillespie, Wim Meijberg

Abstract readComparative Study
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
–field-weighted citation impact
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

29 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Outer membrane protein design.Current opinion in structural biology · 2017
    Review
  6. Article
  7. Review
  8. Review
  9. Ionizable side chains at catalytic active sites of enzymes.European biophysics journal : EBJ · 2012
    Article
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Multiple Scales in the Simulation of Ion Channels and Proteins.The journal of physical chemistry. C, Nanomaterials and interfaces · 2010
    Article
  17. Article
  18. Article
  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

9 authors.

Henk MiedemaBiomade Technology Foundation, Groningen, The Netherlands. miediema@biomade.nl
Anita Meter-Arkema
Jenny Wierenga
John Tang
Bob Eisenberg
Wolfgang Nonner
Hans Hektor
Dirk Gillespie
Wim Meijberg

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The selectivity filter of the bacterial porin OmpF carries a small net charge close to -1 e and is therefore only slightly cation-selective. Calcium channels, on the other hand, contain four negatively charged glutamates, the EEEE-locus, and are among the most selective cation channels known. We aimed to turn the essentially nonselective OmpF into a Ca2+-selective channel. To that end, two additional glutamates (R42E and R132E) were introduced in the OmpF constriction zone that already contains D113 and E117. Mutant OmpF containing this DEEE-locus has a high Ca2+ over Cl- selectivity and a Na+ current with a strongly increased sensitivity to 1 mM Ca2+. The charge/space competition model, initially applied to the L-type Ca2+ channel, identifies the fixed charge and filter volume as key determinants of ion selectivity, with the precise atomic arrangement having only second-order effects. By implication, the reproduction of fixed charge and filter volume should transform two channels into channels of similar selectivity, even if the two belong to entirely different ion channel families, as is the case for OmpF and the L-type Ca2+ channel. The results presented here fit quite well in the framework of charge/space competition theory.

Indexed as

Ion Channel GatingCalciumCalcium Channels, L-TypeCell Membrane PermeabilityMembrane PotentialsMutagenesis, Site-DirectedPermeabilityPorinsPorosityProtein EngineeringRecombinant ProteinsSodiumStructure-Activity RelationshipCalciumCalcium Channels, L-TypeOmpF proteinPorinsRecombinant ProteinsSodium

Identifiers

PMID15326033
PMCPMC1304784

What OpenQuestion holds

Textmetadata
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.