Evidence map›Paper›PMID 28303608›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2017

Resorcinarene-Based Facial Glycosides: Implication of Detergent Flexibility on Membrane-Protein Stability.

Hazrat Hussain, Yang Du, Elena Tikhonova, Jonas S Mortensen, Orquidea Ribeiro, Claudia Santillan, Manabendra Das, Muhammad Ehsan, Claus J Loland, Lan Guan and 3 more

Open access · greenAbstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Glyco-Steroidal Amphiphiles (GSAs) for Membrane Protein Structural Study.Chembiochem : a European journal of chemical biology · 2022
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Chemical tools for membrane protein structural biology.Current opinion in structural biology · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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

13 authors at 5 institutions in 4 countries.

Hazrat HussainDepartment of Bionanotechnology, Hanyang University, Ansan, 155-88, Korea.ORCID http://orcid.org/0000-0002-5449-7660
Yang DuMolecular and Cellular Physiology, Stanford University, Stanford, CA, 94305, USA.ORCID http://orcid.org/0000-0001-5115-0736
Elena TikhonovaDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX, 79430, USA.ORCID http://orcid.org/0000-0002-7892-9173
Jonas S MortensenCenter of Neuroscience, University of Copenhagen, Copenhagen, 2200, Denmark.ORCID http://orcid.org/0000-0002-6743-276X
Orquidea RibeiroDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK.ORCID http://orcid.org/0000-0003-0746-6666
Claudia SantillanDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX, 79430, USA.ORCID http://orcid.org/0000-0003-4803-4077
Manabendra DasDepartment of Bionanotechnology, Hanyang University, Ansan, 155-88, Korea.ORCID http://orcid.org/0000-0003-3690-3183
Muhammad EhsanDepartment of Bionanotechnology, Hanyang University, Ansan, 155-88, Korea.ORCID http://orcid.org/0000-0002-4723-7924
Claus J LolandCenter of Neuroscience, University of Copenhagen, Copenhagen, 2200, Denmark.ORCID http://orcid.org/0000-0002-1773-1446
Lan GuanDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences Center, Lubbock, TX, 79430, USA.ORCID http://orcid.org/0000-0002-2274-361X
Brian K KobilkaMolecular and Cellular Physiology, Stanford University, Stanford, CA, 94305, USA.ORCID http://orcid.org/0000-0001-5958-3990
Bernadette ByrneDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK.ORCID http://orcid.org/0000-0001-9598-9832
Pil Seok ChaeDepartment of Bionanotechnology, Hanyang University, Ansan, 155-88, Korea.ORCID http://orcid.org/0000-0003-1799-3304
Hanyang University · KRTexas Tech University · USImperial College London · GBStanford University · USUniversity of Copenhagen · DK

Funding

THE MECHANISM OF BETA2 ADRENOCEPTOR ACTIVATIONR01NS028471 · NINDS · STANFORD UNIVERSITY · PI KOBILKA, BRIAN K · 1990 to 2021
$6.7M
NINDS NIH HHS R01 NS028471
6 · The paper itself

Abstract

As a membrane-mimetic system, detergent micelles are popularly used to extract membrane proteins from lipid environments and to maintain their solubility and stability in an aqueous medium. However, many membrane proteins encapsulated in conventional detergents tend to undergo structural degradation during extraction and purification, thus necessitating the development of new agents with enhanced properties. In the current study, two classes of new amphiphiles are introduced, resorcinarene-based glucoside and maltoside amphiphiles (designated RGAs and RMAs, respectively), for which the alkyl chains are facially segregated from the carbohydrate head groups. Of these facial amphiphiles, two RGAs (RGA-C11 and RGA-C13) conferred markedly enhanced stability to four tested membrane proteins compared to a gold-standard conventional detergent. The relatively high water solubility and micellar stability of the RGAs compared to the RMAs, along with their generally favourable behaviours for membrane protein stabilisation described here, are likely to be, at least in part, a result of the high conformational flexibility of these glucosides. This study suggests that flexibility could be an important factor in determining the suitability of new detergents for membrane protein studies.

Indexed as

Aspergillus nidulansBacterial ProteinsCalixarenesCoumarinsDetergentsFungal ProteinsGlycosidesHydrophobic and Hydrophilic InteractionsMembrane ProteinsMembrane Transport ProteinsPhenylalanineProtein DenaturationProtein StabilitySalmonella typhimuriumSymportersBacterial ProteinsCalixarenesCoumarinsDetergentsFungal ProteinsGlycosidesmelibiose permeaseMembrane ProteinsMembrane Transport ProteinsN-(4-(7-diethylamino-4-methylcoumarin-3-yl)phenyl)maleimidePhenylalanineresorcinareneSymportersUAPA protein, Aspergillus nidulansfacial amphiphilesmembrane proteinsmolecular designprotein stabilityresorcinarene glycosides

Identifiers

PMID28303608
PMCPMC5818266
OpenAlexW2595112061

What OpenQuestion holds

Textmetadata
LicenceTDM
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.