ArticleBiophysical journal2003
Pores formed by the nicotinic receptor m2delta Peptide: a molecular dynamics simulation study.
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 15 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
15 citing papers in PubMed, 36 citations in OpenAlex.
- A brief history of visualizing membrane systems in molecular dynamics simulations.Frontiers in bioinformatics · 2023Article
- Structural and molecular modeling features of P2X receptors.International journal of molecular sciences · 2014Review
- Structural characterization of two pore-forming peptides: consequences of introducing a C-terminal tryptophan.Proteins · 2010Article
- The conformational transition pathway of ATP binding cassette transporter MsbA revealed by atomistic simulations.The Journal of biological chemistry · 2010Article
- Molecular-dynamics simulations of ELIC-a prokaryotic homologue of the nicotinic acetylcholine receptor.Biophysical journal · 2009Article
- Partitioning of anesthetics into a lipid bilayer and their interaction with membrane-bound peptide bundles.Biophysical journal · 2006Article
- Conformation and environment of channel-forming peptides: a simulation study.Biophysical journal · 2006Article
- A molecular dynamics study of the formation, stability, and oligomerization state of two designed coiled coils: possibilities and limitations.Biophysical journal · 2005Article
- A gating mechanism proposed from a simulation of a human alpha7 nicotinic acetylcholine receptor.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- Molecular dynamics simulation of the M2 helices within the nicotinic acetylcholine receptor transmembrane domain: structure and collective motions.Biophysical journal · 2005Article
- The transmembrane domain of the acetylcholine receptor: insights from simulations on synthetic peptide models.Biophysical journal · 2005Article
- Homology modeling and molecular dynamics simulations of transmembrane domain structure of human neuronal nicotinic acetylcholine receptor.Biophysical journal · 2005Article
- Homology modelling and molecular dynamics simulations: comparative studies of human aquaporin-1.European biophysics journal : EBJ · 2004Article
- Helical kink and channel behaviour: a comparative study with the peptaibols alamethicin, trichotoxin and antiamoebin.European biophysics journal : EBJ · 2004Review
- Molecular dynamics investigation of an oriented cyclic peptide nanotube in DMPC bilayers.Biophysical journal · 2003Article
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 2 institutions in 2 countries.
Funding
Abstract
The M2delta peptide self-assembles to form a pentameric bundle of transmembrane alpha-helices that is a model of the pore-lining region of the nicotinic acetylcholine receptor. Long (>15 ns) molecular dynamics simulations of a model of the M2delta(5) bundle in a POPC bilayer have been used to explore the conformational dynamics of the channel assembly. On the timescale of the simulation, the bundle remains relatively stable, with the polar pore-lining side chains remaining exposed to the lumen of the channel. Fluctuations at the helix termini, and in the helix curvature, result in closing/opening transitions at both mouths of the channel, on a timescale of approximately 10 ns. On average, water within the pore lumen diffuses approximately 4x more slowly than water outside the channel. Examination of pore water trajectories reveals both single-file and path-crossing regimes to occur at different times within the simulation.
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.