Evidence map›Paper›PMID 27110345›Full record

ArticleChemical science2016

A Class of Rigid Linker-bearing Glucosides for Membrane Protein Structural Study.

Aiman Sadaf, Jonas S Mortensen, Stefano Capaldi, Elena Tikhonova, Parameswaran Hariharan, Orquidea de Castro Ribeiro, Claus J Loland, Lan Guan, Bernadette Byrne, Pil Seok Chae

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2016. 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
2.4field-weighted citation impact, top 11% 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, 44 citations in OpenAlex.

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  7. Glyco-Steroidal Amphiphiles (GSAs) for Membrane Protein Structural Study.Chembiochem : a European journal of chemical biology · 2022
    Article
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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 5 institutions in 6 countries.

Aiman SadafDepartment of Bionanotechnology, Hanyang University, Ansan, 426-791 (Korea).
Jonas S MortensenDepartment of Neuroscience and Pharmacology, University of Copenhagen, DK-2200 Copenhagen (Denmark).
Stefano CapaldiDepartment of Life Sciences, Imperial College London London, SW7 2AZ (UK) ; Department of Biotechnology, University of Verona, 37134 Verona (Italy).
Elena TikhonovaDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences.
Parameswaran HariharanDepartment of Cell Physiology and Molecular Biophysics, Center for Membrane Protein Research, School of Medicine, Texas Tech University Health Sciences.
Orquidea de Castro RibeiroDepartment of Neuroscience and Pharmacology, University of Copenhagen, DK-2200 Copenhagen (Denmark).
Claus J Loland
Lan Guan
Bernadette Byrne
Pil Seok Chae
Texas Tech University · USUniversity of Copenhagen · DKAnsan University · KRTransnational Press LondonUniversity of Verona · IT

Funding

Novel capture reagents for membrane protein structure determinationR01GM095538 · NIGMS · TEXAS TECH UNIVERSITY HEALTH SCIS CENTER · PI GUAN, LAN · 2010 to 2013
$1.2M
NIGMS NIH HHS R01 GM095538
6 · The paper itself

Abstract

Membrane proteins are amphipathic bio-macromolecules incompatible with the polar environments of aqueous media. Conventional detergents encapsulate the hydrophobic surfaces of membrane proteins allowing them to exist in aqueous solution. Membrane proteins stabilized by detergent micelles are used for structural and functional analysis. Despite the availability of a large number of detergents, only a few agents are sufficiently effective at maintaining the integrity of membrane proteins to allow successful crystallization. In the present study, we describe a novel class of synthetic amphiphiles with a branched tail group and a triglucoside head group. These head and tail groups were connected via an amide or ether linkage by using a tris(hydroxylmethyl)aminomethane (TRIS) or neopentyl glycol (NPG) linker to produce TRIS-derived triglucosides (TDTs) and NPG-derived triglucosides (NDTs), respectively. Members of this class conferred enhanced stability on target membrane proteins compared to conventional detergents. Because of straightforward synthesis of the novel agents and their favourable effects on a range of membrane proteins, these agents should be of wide applicability to membrane protein science.

Identifiers

PMID27110345
PMCPMC4836865
OpenAlexW2219472438

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.