Evidence map›Paper›PMID 18339603›Full record

ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2008

Nanobiomechanics of proteins and biomembrane.

Atsushi Ikai

Open access · greenAbstract readComparative Study
In one paragraph

Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2008. 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
1.6field-weighted citation impact, top 18% 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, 20 citations in OpenAlex.

  1. Nanomechanics of HaloTag tethers.Journal of the American Chemical Society · 2013
    Article
  2. Article
  3. Article
  4. The applications of atomic force microscopy to vision science.Investigative ophthalmology & visual science · 2010
    Review
  5. Introduction. Japan: its tradition and hot topics in biological sciences.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2008
    Article
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

1 author at 1 institution in 2 countries.

Atsushi IkaiGraduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, Yokohama 226-8501, Japan. aikai@bio.titech.ac.jp
Google (United States) · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A review of the work done in the Laboratory of Biodynamics of Tokyo Institute of Technology in the last decade has been summarized in this article in relation to the results reported from other laboratories. The emphasis here is the application of nanomechanics based on the force mode of atomic force microscopy (AFM) to proteins and protein-based biological structures. Globular proteins were stretched in various ways to detect the localized rigidity inside of the molecule. When studied by this method, bovine carbonic anhydrase II (BCA II), calmodulin and OspA protein all showed the presence of localized rigid structures inside the molecules. Protein compression experiments were done on BCA II to obtain an estimate of the Young modulus and its change in the process of denaturation. Then, the AFM probe method was turned on to cell membranes and cytoplasmic components. Force curves accompanying the extraction process of membrane proteins from intact cells were analysed in relation to their interaction with the cytoskeletal components. By pushing the AFM probe further into the cytoplasm, mRNAs were recovered from a live cell with minimal damage, and multiplied using PCR technology for their identification. Altogether, the work introduced here forms the basis of nanomechanics of protein and protein-based biostructures and application of the nanomechanical technology to cell biology.

Indexed as

3T3 CellsAnimalsAntigens, SurfaceBacterial Outer Membrane ProteinsBacterial VaccinesBiomechanical PhenomenaCalmodulinCarbonic Anhydrase IICattleLipoproteinsMembranesMiceMicroscopy, Atomic ForcePolymerase Chain ReactionRNA, MessengerAntigens, SurfaceBacterial Outer Membrane ProteinsBacterial VaccinesCalmodulinCarbonic Anhydrase IILipoproteinsOspA proteinRNA, Messenger

Identifiers

PMID18339603
PMCPMC2610188
OpenAlexW1995502172

What OpenQuestion holds

Textmetadata
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.