Evidence map›Paper›PMID 28638082›Full record

ArticleScientific reports2017

Tandem malonate-based glucosides (TMGs) for membrane protein structural studies.

Hazrat Hussain, Jonas S Mortensen, Yang Du, Claudia Santillan, Orquidea Ribeiro, Juyeon Go, Parameswaran Hariharan, Claus J Loland, Lan Guan, Brian K Kobilka and 2 more

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PubMed Full text at PMC Publisher
In one paragraph

Article in Scientific reports, 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
–field-weighted citation impact
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.

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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

12 authors.

Hazrat HussainDepartment of Bionanotechnology, Hanyang University, Ansan, 155-88, South Korea.
Jonas S MortensenCenter of Neuroscience, University of Copenhagen, Copenhagen, DK-2200, Denmark.ORCID 0000-0002-6743-276X
Yang DuMolecular and Cellular Physiology, Stanford University, Stanford, CA, 94305, USA.
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.
Orquidea RibeiroDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK.
Juyeon GoDepartment of Bionanotechnology, Hanyang University, Ansan, 155-88, South Korea.
Parameswaran HariharanDepartment 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 0000-0002-6020-1547
Claus J LolandCenter of Neuroscience, University of Copenhagen, Copenhagen, DK-2200, Denmark.
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 0000-0002-2274-361X
Brian K KobilkaMolecular and Cellular Physiology, Stanford University, Stanford, CA, 94305, USA.
Bernadette ByrneDepartment of Life Sciences, Imperial College London, London, SW7 2AZ, UK.ORCID 0000-0001-9598-9832
Pil Seok ChaeDepartment of Bionanotechnology, Hanyang University, Ansan, 155-88, South Korea. pchae@hanyang.ac.kr.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

High-resolution membrane protein structures are essential for understanding the molecular basis of diverse biological events and important in drug development. Detergents are usually used to extract these bio-macromolecules from the membranes and maintain them in a soluble and stable state in aqueous solutions for downstream characterization. However, many eukaryotic membrane proteins solubilized in conventional detergents tend to undergo structural degradation, necessitating the development of new amphiphilic agents with enhanced properties. In this study, we designed and synthesized a novel class of glucoside amphiphiles, designated tandem malonate-based glucosides (TMGs). A few TMG agents proved effective at both stabilizing a range of membrane proteins and extracting proteins from the membrane environment. These favourable characteristics, along with synthetic convenience, indicate that these agents have potential in membrane protein research.

Indexed as

Escherichia coliGlucosidesMembrane ProteinsSalmonella typhimuriumSolubilitySurface-Active AgentsSymportersGlucosidesmelibiose permeaseMembrane ProteinsSurface-Active AgentsSymporters

Identifiers

PMID28638082
PMCPMC5479785

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Registered trials

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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.