ArticleBiophysical journal2003
Multistep mechanism of chloride translocation in a strongly anion-selective porin channel.
Article in Biophysical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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.
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.
Who cites it
8 citing papers in PubMed, 27 citations in OpenAlex.
- High-resolution experimental and computational electrophysiology reveals weak β-lactam binding events in the porin PorB.Scientific reports · 2019Article
- Fosfomycin Permeation through the Outer Membrane Porin OmpF.Biophysical journal · 2019Article
- Modulation of the Neisseria gonorrhoeae drug efflux conduit MtrE.Scientific reports · 2017Article
- Modeling and simulation of ion channels.Chemical reviews · 2012Review
- Computational electrophysiology: the molecular dynamics of ion channel permeation and selectivity in atomistic detail.Biophysical journal · 2011Article
- A role for anions in ATP synthesis and its molecular mechanistic interpretation.Journal of bioenergetics and biomembranes · 2011Article
- Chemical modification of the bacterial porin OmpF: gain of selectivity by volume reduction.Biophysical journal · 2006Article
- Permeation properties of an engineered bacterial OmpF porin containing the EEEE-locus of Ca2+ channels.Biophysical journal · 2004Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The strongly anion-selective porin channel Omp32 from the bacterium Delftia acidovorans differs from other unspecific porins by its pronounced selectivity for anions and its particularly small channel cross-section. Multinanosecond molecular dynamics simulations of chloride ion movement in this pore protein suggest that translocated anions interact intimately with the charges of a "basic ladder", whose dynamics lead the anions in a stepwise manner through the constriction zone of the channel. The ladder-steps comprise the central clustered arginine groups and flanking basic residues at its exoplasmic and periplasmic sides. The computed free energy profile of ion movement in and around the constriction zone shows a corresponding succession of free energy minima and barriers. A number of polar atoms from other amino acids contribute to the coordination of Cl(-) at certain sites and to its temporary immobilization in the channel. A special binding site occurs at the transition of the constriction zone to the periplasmic funnel, binding the chloride ion over significant lengths of time. The results from our MD study offer a possible explanation for the nonlinear conductance properties and unusual salt-dependent characteristics of Omp32 observed earlier in experimental measurements.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.