Evidence map›Paper›PMID 26013293›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2015

Novel Xylene-Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation.

Kyung Ho Cho, Yang Du, Nicola J Scull, Parameswaran Hariharan, Kamil Gotfryd, Claus J Loland, Lan Guan, Bernadette Byrne, Brian K Kobilka, Pil Seok Chae

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

11 citing papers in PubMed, 18 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

10 authors at 6 institutions in 4 countries.

Kyung Ho ChoDepartment of Bionanotechnology, Hanyang University, Ansan, 426-791 (Republic of Korea).
Yang DuMolecular and Cellular Physiology, Stanford University, Stanford, CA 94305 (USA).
Nicola J ScullDepartment of Life Sciences, Imperial College London, London, SW7 2AZ (UK).
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).
Kamil GotfrydDepartment of Neuroscience and Pharmacology, University of Copenhagen, 2200 Copenhagen (Denmark).
Claus J LolandDepartment of Neuroscience and Pharmacology, University of Copenhagen, 2200 Copenhagen (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).
Bernadette ByrneDepartment of Life Sciences, Imperial College London, London, SW7 2AZ (UK).
Brian K KobilkaMolecular and Cellular Physiology, Stanford University, Stanford, CA 94305 (USA).
Pil Seok ChaeDepartment of Bionanotechnology, Hanyang University, Ansan, 426-791 (Republic of Korea). pchae@hanyang.ac.kr.
Hanyang University · KRImperial College London · GBStanford University · USUniversity of Copenhagen · DKTexas Tech University · USTexas Tech University Health Sciences Center · US

Funding

THE MECHANISM OF BETA2 ADRENOCEPTOR ACTIVATIONR01NS028471 · NINDS · STANFORD UNIVERSITY · PI KOBILKA, BRIAN K · 1990 to 2021
$6.7M
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 GM095538NIGMS NIH HHS R01GM095538NINDS NIH HHS R01 NS028471
6 · The paper itself

Abstract

Membrane proteins are key functional players in biological systems. These biomacromolecules contain both hydrophilic and hydrophobic regions and thus amphipathic molecules are necessary to extract membrane proteins from their native lipid environments and stabilise them in aqueous solutions. Conventional detergents are commonly used for membrane protein manipulation, but membrane proteins surrounded by these agents often undergo denaturation and aggregation. In this study, a novel class of maltoside-bearing amphiphiles, with a xylene linker in the central region, designated xylene-linked maltoside amphiphiles (XMAs) was developed. When these novel agents were evaluated with a number of membrane proteins, it was found that XMA-4 and XMA-5 have particularly favourable efficacy with respect to membrane protein stabilisation, indicating that these agents hold significant potential for membrane protein structural study.

Indexed as

DetergentsHydrophobic and Hydrophilic InteractionsMacromolecular SubstancesMaltoseMembrane ProteinsSolubilitySurface-Active AgentsXylenesDetergentsMacromolecular SubstancesMaltoseMembrane ProteinsSurface-Active AgentsXylenesamphiphile designdetergentsmembrane proteinsprotein stabilisationprotein structure

Identifiers

PMID26013293
PMCPMC4493440
OpenAlexW2161093993

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.