Evidence map›Paper›PMID 34063660›Full record

ArticleMembranes2021

Physical Properties and Reactivity of Microdomains in Phosphatidylinositol-Containing Supported Lipid Bilayer.

Toshinori Motegi, Kingo Takiguchi, Yohko Tanaka-Takiguchi, Toshiki Itoh, Ryugo Tero

Open access · goldAbstract read
In one paragraph

Article in Membranes, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

6 citing papers in PubMed, 11 citations in OpenAlex.

  1. Article
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  5. [Simulation of gas chromatographic separation based on random diffusion].Se pu = Chinese journal of chromatography · 2022
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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 3 institutions in 1 country.

Toshinori MotegiElectronics-Inspired Interdisciplinary Research Institute, Toyohashi University of Technology, Toyohashi 441-8580, Japan.ORCID 0000-0002-2717-4823
Kingo TakiguchiDivision of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.ORCID 0000-0002-7640-0954
Yohko Tanaka-TakiguchiDivision of Biological Science, Graduate School of Science, Nagoya University, Nagoya 464-8602, Japan.
Toshiki ItohBiosignal Research Center, Kobe University, Kobe 657-8501, Japan.
Ryugo TeroElectronics-Inspired Interdisciplinary Research Institute, Toyohashi University of Technology, Toyohashi 441-8580, Japan.ORCID 0000-0002-3822-0530
Nagoya University · JPToyohashi University of Technology · JPKobe University · JP

Funding

Japan Science and Technology Agency JPMJCR14F3Japan Society for the Promotion of Science JP19K15407Japan Society for the Promotion of Science JP20H02690Japan Society for the Promotion of Science JP21015027
6 · The paper itself

Abstract

We characterized the size, distribution, and fluidity of microdomains in a lipid bilayer containing phosphatidylinositol (PI) and revealed their roles during the two-dimensional assembly of a membrane deformation protein (FBP17). The morphology of the supported lipid bilayer (SLB) consisting of PI and phosphatidylcholine (PC) on a mica substrate was observed with atomic force microscope (AFM). Single particle tracking (SPT) was performed for the PI+PC-SLB on the mica substrate by using the diagonal illumination setup. The AFM topography showed that PI-derived submicron domains existed in the PI+PC-SLB. The spatiotemporal dependence of the lateral lipid diffusion obtained by SPT showed that the microdomain had lower fluidity than the surrounding region and worked as the obstacles for the lipid diffusion. We observed the two-dimensional assembly of FBP17, which is one of F-BAR family proteins included in endocytosis processes and has the function generating lipid bilayer tubules in vitro. At the initial stage of the FBP17 assembly, the PI-derived microdomain worked as a scaffold for the FBP17 adsorption, and the fluid surrounding region supplied FBP17 to grow the FBP17 domain via the lateral molecular diffusion. This study demonstrated an example clearly revealing the roles of two lipid microregions during the protein reaction on a lipid bilayer.

Indexed as

atomic force microscopeF-BAR proteinlipid bilayer membranephosphatidylinositolsingle particle tracking

Identifiers

PMID34063660
PMCPMC8147626
OpenAlexW3157134627

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.