Evidence map›Paper›PMID 25813698›Full record

ArticleThe Analyst2015

Maltose neopentyl glycol-3 (MNG-3) analogues for membrane protein study.

Kyung Ho Cho, Mohd Husri, Anowarul Amin, Kamil Gotfryd, Ho Jin Lee, Juyeon Go, Jin Woong Kim, Claus J Loland, Lan Guan, Bernadette Byrne and 1 more

Open access · greenAbstract read
In one paragraph

Article in The Analyst, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

27 citing papers in PubMed, 46 citations in OpenAlex.

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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

11 authors at 7 institutions in 4 countries.

Kyung Ho ChoDepartment of Bionanotechnology, Hanyang University, Ansan, 426-791, Korea. pchae@hanyang.ac.kr.
Mohd Husri
Anowarul Amin
Kamil Gotfryd
Ho Jin Lee
Juyeon Go
Jin Woong Kim
Claus J Loland
Lan Guan
Bernadette Byrne
Pil Seok Chae
Hanyang University · KRUniversity of Copenhagen · DKAnsan University · KRImperial College London · GBLubbock Christian University · USMembrane Technology & Research (United States) · USTransnational Press London

Funding

Novel capture reagents for membrane protein structure determinationR01GM095538 · NIGMS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI GUAN, LAN · 2010 to 2013
$1.2M
Biotechnology and Biological Sciences Research Council BB/K017292/1NIGMS NIH HHS R01 GM095538
6 · The paper itself

Abstract

Detergents are typically used to both extract membrane proteins (MPs) from the lipid bilayers and maintain them in solution. However, MPs encapsulated in detergent micelles are often prone to denaturation and aggregation. Thus, the development of novel agents with enhanced stabilization characteristics is necessary to advance MP research. Maltose neopentyl glycol-3 (MNG-3) has contributed to >10 crystal structures including G-protein coupled receptors. Here, we prepared MNG-3 analogues and characterised their properties using selected MPs. Most MNGs were superior to a conventional detergent, n-dodecyl-β-D-maltopyranoside (DDM), in terms of membrane protein stabilization efficacy. Interestingly, optimal stabilization was achieved with different MNG-3 analogues depending on the target MP. The origin for such detergent specificity could be explained by a novel concept: compatibility between detergent hydrophobicity and MP tendency to denature and aggregate. This set of MNGs represents viable alternatives to currently available detergents for handling MPs, and can be also used as tools to estimate MP sensitivity to denaturation and aggregation.

Indexed as

BacteriaBacterial ProteinsDetergentsGlycolsMaltoseMembrane ProteinsMembrane Transport ProteinsMicellesProtein AggregatesProtein StabilityBacterial ProteinsDetergentsdodecyl maltopyranosideGlycolsMaltoseMembrane ProteinsMembrane Transport ProteinsMicellesProtein Aggregates

Identifiers

PMID25813698
PMCPMC4497825
OpenAlexW1968596279

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.