Evidence map›Paper›PMID 19865530›Full record

ReviewInternational journal of molecular sciences2009

Experimental and computational characterization of biological liquid crystals: a review of single-molecule bioassays.

Kilho Eom, Jaemoon Yang, Jinsung Park, Gwonchan Yoon, Young Soo Sohn, Shinsuk Park, Dae Sung Yoon, Sungsoo Na, Taeyun Kwon

Open access · goldAbstract readReview
PubMed Full text at PMC Publisher
In one paragraph

Review in International journal of molecular sciences, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

1 citing paper in PubMed, 17 citations in OpenAlex.

  1. 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

9 authors at 3 institutions in 1 country.

Kilho EomDepartment of Mechanical Engineering, Korea University, Seoul 136-701, Korea.
Jaemoon YangDepartment of Radiology, College of Medicine, Yonsei University, Seoul 120-752, Korea.
Jinsung ParkDepartment of Mechanical Engineering, Korea University, Seoul 136-701, Korea.
Gwonchan YoonDepartment of Mechanical Engineering, Korea University, Seoul 136-701, Korea.
Young Soo SohnDepartment of Biomedical Engineering, Catholic University of Daegu, Kyeongbuk 712-702, Korea.
Shinsuk ParkDepartment of Mechanical Engineering, Korea University, Seoul 136-701, Korea.
Dae Sung YoonDepartment of Biomedical Engineering, Yonsei University, Kangwon-do 220-740, Korea.
Sungsoo NaDepartment of Mechanical Engineering, Korea University, Seoul 136-701, Korea.
Taeyun KwonResearch Institute of Engineering and Technology, Korea University, Seoul 136-701, Korea.
Korea University · KRYonsei University · KRCatholic University of Daegu · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Quantitative understanding of the mechanical behavior of biological liquid crystals such as proteins is essential for gaining insight into their biological functions, since some proteins perform notable mechanical functions. Recently, single-molecule experiments have allowed not only the quantitative characterization of the mechanical behavior of proteins such as protein unfolding mechanics, but also the exploration of the free energy landscape for protein folding. In this work, we have reviewed the current state-of-art in single-molecule bioassays that enable quantitative studies on protein unfolding mechanics and/or various molecular interactions. Specifically, single-molecule pulling experiments based on atomic force microscopy (AFM) have been overviewed. In addition, the computational simulations on single-molecule pulling experiments have been reviewed. We have also reviewed the AFM cantilever-based bioassay that provides insight into various molecular interactions. Our review highlights the AFM-based single-molecule bioassay for quantitative characterization of biological liquid crystals such as proteins.

Indexed as

Models, ChemicalMolecular Dynamics SimulationBiomechanical PhenomenaHydrogen BondingLiquid CrystalsMicroscopy, Atomic ForceProteinsProtein UnfoldingThermodynamicsProteinsatomic force microscope (AFM)coarse-grained modelcoarse-grained molecular dynamics simulationin vitro molecular recognitionssingle-molecule experiments

Identifiers

PMID19865530
PMCPMC2769145
OpenAlexW2168314407

What OpenQuestion 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 OpenQuestion graph.