Evidence map›Paper›PMID 28809779›Full record

ReviewMolecules (Basel, Switzerland)2017

Application of Solution NMR to Structural Studies on α-Helical Integral Membrane Proteins.

Dae-Won Sim, Zhenwei Lu, Hyung-Sik Won, Seu-Na Lee, Min-Duk Seo, Bong-Jin Lee, Ji-Hun Kim

Open access · goldAbstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2017. 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
1.1field-weighted citation impact, top 23% 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, 12 citations in OpenAlex.

  1. Article
  2. Magic angle spinning NMR of G protein-coupled receptors.Progress in nuclear magnetic resonance spectroscopy · 2022
    Review
  3. Article
  4. Article
  5. Review
  6. 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

7 authors at 5 institutions in 2 countries.

Dae-Won SimDepartment of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungbuk 27478, Korea. konapapa@nate.com.
Zhenwei LuDepartment of Biochemistry, Vanderbilt University, Nashville, TN 37204, USA. zhenwei.lu@vanderbilt.edu.
Hyung-Sik WonDepartment of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungbuk 27478, Korea. wonhs@kku.ac.kr.
Seu-Na LeeDepartment of Biotechnology, College of Biomedical and Health Science, Konkuk University, Chungbuk 27478, Korea. leesn1029@naver.com.
Min-Duk SeoDepartment of Molecular Science and Technology & College of Pharmacy, Ajou University, Suwon 16499, Korea. mdseo@ajou.ac.kr.
Bong-Jin LeeThe Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Gwanak-gu, Seoul 151-742, Korea. lbj@nmr.snu.ac.kr.
Ji-Hun KimCollege of Pharmacy, Chungbuk National University, Cheongju 28160, Chungbuk, Korea. nmrjhkim@chungbuk.ac.kr.
Konkuk University · KRAjou University · KRChungbuk National University · KRSeoul National University · KRVanderbilt University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A large portion of proteins in living organisms are membrane proteins which play critical roles in the biology of the cell, from maintenance of the biological membrane integrity to communication of cells with their surroundings. To understand their mechanism of action, structural information is essential. Nevertheless, structure determination of transmembrane proteins is still a challenging area, even though recently the number of deposited structures of membrane proteins in the PDB has rapidly increased thanks to the efforts using X-ray crystallography, electron microscopy, and solid and solution nuclear magnetic resonance (NMR) technology. Among these technologies, solution NMR is a powerful tool for studying protein-protein, protein-ligand interactions and protein dynamics at a wide range of time scales as well as structure determination of membrane proteins. This review provides general and useful guideline for membrane protein sample preparation and the choice of membrane-mimetic media, which are the key step for successful structural analysis. Furthermore, this review provides an opportunity to look at recent applications of solution NMR to structural studies on α-helical membrane proteins through some success stories.

Indexed as

AnimalsCell MembraneCrystallography, X-RayHumansLigandsMembrane ProteinsMicroscopy, ElectronMolecular ConformationNuclear Magnetic Resonance, BiomolecularProtein BindingProtein ConformationLigandsMembrane Proteinsisotope labelingmembrane-mimeticssolution NMRstructureα-helical integral membrane protein

Identifiers

PMID28809779
PMCPMC6152068
OpenAlexW2747873177

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.