Evidence map›Paper›PMID 33609699›Full record

ArticleMethods (San Diego, Calif.)2022

Topographically smooth and stable supported lipid bilayer for high-resolution AFM studies.

Siddhartha Banerjee, Yuri L Lyubchenko

Open access · greenAbstract read
In one paragraph

Article in Methods (San Diego, Calif.), 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.8field-weighted citation impact, top 30% 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

5 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Lipid Self-Assemblies under the Atomic Force Microscope.International journal of molecular sciences · 2021
    Review
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

2 authors at 2 institutions in 1 country.

Siddhartha BanerjeeDepartment of Pharmaceutical Sciences, University of Nebraska Medical Center, 986025 Nebraska Medical Center, Omaha, NE 68198-6025, United States.
Yuri L LyubchenkoDepartment of Pharmaceutical Sciences, University of Nebraska Medical Center, 986025 Nebraska Medical Center, Omaha, NE 68198-6025, United States. Electronic address: ylyubchenko@unmc.edu.
Nebraska Medical Center · USUniversity of Nebraska Medical Center · US

Funding

Protein Self-Assembly into NanoaggregatesR01GM096039 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI LYUBCHENKO, YURI L · 2011 to 2018
$2.9M
APOBEC3-Nucleic Acid Interactions and Molecular Mechanisms of HIV RestrictionR01GM118006 · NIGMS · UNIVERSITY OF NEBRASKA MEDICAL CENTER · PI LYUBCHENKO, YURI L · 2016 to 2019
$1.5M
NIGMS NIH HHS R01 GM096039NIGMS NIH HHS R01 GM118006
6 · The paper itself

Abstract

The cellular membrane has been identified to play a critical role in various biological processes including the assembly of biological systems. Membranes are complex, primarily two-dimensional assemblies with varied lipid compositions depending on the particular region of the cell. Supported lipid bilayers are considered as appropriate models for physio-chemical studies of membranes including numerous single molecule techniques. Atomic force microscopy (AFM) as a topographic technique is a fully appropriate single molecule technique capable of direct observation of molecular processes on membranes. However, reliable experimental AFM studies require the preparation of the bilayer with a sub-nanometer smooth morphology, which remains stable over long-time observation. Here we present the methodology, which allows one to prepare a smooth, stable, structurally homogeneous lipid bilayer without the presence of any trapped vesicles. We described the application of such lipid bilayers to probe time-dependent early stages of aggregation of monomeric amyloid proteins. Importantly, the proposed methodology can be extended to bilayers with various compositions, by incorporating different lipids for on-membrane aggregation study including cholesterol. Furthermore, this methodology development allowed us to monitor the aggregation of amyloid protein at its physiologically relevant low protein concentration. The flexibility of altering the membrane composition allows to identify the specific role of a particular lipid towards the aggregation kinetics, revealing the plausible mechanism of disease development.

Indexed as

CholesterolLipid BilayersCell MembraneMicroscopy, Atomic ForceCholesterolLipid BilayersAmyloidProtein aggregationSupported lipid bilayerTime-lapse AFM

Identifiers

PMID33609699
PMCPMC8371085
OpenAlexW3131894476

What OpenQuestion holds

Textmetadata
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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 OpenQuestion graph.