ArticleBiophysical journal2000
Blockers of VacA provide insights into the structure of the pore.
Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 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
10 citing papers in PubMed, 26 citations in OpenAlex.
- There Are No Insurmountable Barriers: Passage of theMembranes · 2023Review
- Anion Channels of Mitochondria.Handbook of experimental pharmacology · 2017Review
- Cation-coupled bicarbonate transporters.Comprehensive Physiology · 2014Review
- SLC4A transporters.Current topics in membranes · 2012Article
- Helicobacter pylori vacuolating toxin A and apoptosis.Cell communication and signaling : CCS · 2011Article
- Helicobacter pylori VacA toxin/subunit p34: targeting of an anion channel to the inner mitochondrial membrane.PLoS pathogens · 2010Article
- Distribution of Helicobacter pylori in north China.World journal of gastroenterology · 2005Article
- How the loop and middle regions influence the properties of Helicobacter pylori VacA channels.Biophysical journal · 2001Article
- The Helicobacter pylori VacA toxin is a urea permease that promotes urea diffusion across epithelia.The Journal of clinical investigation · 2001Article
- Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The cytotoxic effects of the Helicobacter pylori toxin VacA, an important etiogenic factor in human gastric diseases, are due to its ability to form anion-selective pores in target cell membranes. We have studied the inhibition of channel activity by 5-nitro-2-(3-phenylpropylamino) benzoic acid (NPPB) and 4, 4'-diisothiocyanatostilbene-2,2'-disulfonic acid (DIDS), representatives of two popular classes of chloride channel blockers, to gain information on the mechanism of blocking and on the unknown structure of the VacA pore. The data indicate that both compounds produce a fast block by binding to separate but mutually exclusive sites within the channel lumen. DIDS binds close to the pore opening on the side of protein insertion, whereas NPPB blocks at a position in the opposite half of the channel. Although DIDS reaches the blocking site by traveling along the lumen, inhibition by NPPB appears to involve mainly partition of the compound into the membrane, voltage-independent diffusion from it to the inhibitory position, and voltage-dependent exit. The data are consistent with a pore that can be more easily entered from the side of protein insertion than from the opposite end.
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.