Evidence map›Paper›PMID 26657413›Full record

ArticleScientific reports2015

Anomalous Dynamics of a Lipid Recognition Protein on a Membrane Surface.

Eiji Yamamoto, Antreas C Kalli, Takuma Akimoto, Kenji Yasuoka, Mark S P Sansom

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

12 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. PIPBiophysical journal · 2021
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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

5 authors at 2 institutions in 2 countries.

Eiji YamamotoDepartment of Mechanical Engineering, Keio University, Yokohama, Kanagawa, 223-8522, Japan.
Antreas C KalliDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom.
Takuma AkimotoDepartment of Mechanical Engineering, Keio University, Yokohama, Kanagawa, 223-8522, Japan.
Kenji YasuokaDepartment of Mechanical Engineering, Keio University, Yokohama, Kanagawa, 223-8522, Japan.
Mark S P SansomDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, United Kingdom.
Keio University · JPUniversity of Oxford · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pleckstrin homology (PH) domains are lipid-binding modules present in peripheral membrane proteins which interact with phosphatidyl-inositol phosphates (PIPs) in cell membranes. We use multiscale molecular dynamics simulations to characterize the localization and anomalous dynamics of the DAPP1 PH domain on the surface of a PIP-containing lipid bilayer. Both translational and rotational diffusion of the PH domain on the lipid membrane surface exhibit transient subdiffusion, with an exponent α ≈ 0.5 for times of less than 10 ns. In addition to a PIP3 molecule at the canonical binding site of the PH domain, we observe additional PIP molecules in contact with the protein. Fluctuations in the number of PIPs associated with the PH domain exhibit 1/f noise. We suggest that the anomalous diffusion and long-term correlated interaction of the PH domain with the membrane may contribute to an enhanced probability of encounter with target complexes on cell membrane surfaces.

Indexed as

Models, MolecularAlgorithmsCell MembraneLipid BilayersLipid-Linked ProteinsMolecular ConformationMolecular Dynamics SimulationPhosphatidylinositol PhosphatesProtein Interaction Domains and MotifsLipid BilayersLipid-Linked ProteinsPhosphatidylinositol Phosphates

Identifiers

PMID26657413
PMCPMC4677404
OpenAlexW2176220900

What OpenQuestion holds

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Registered trials

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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.