Evidence map›Paper›PMID 23814603›Full record

ArticleMolecular bioSystems2010

Tripod Amphiphiles for Membrane Protein Manipulation.

Pil Seok Chae, Philip D Laible, Samuel H Gellman

Open access · greenAbstract read
In one paragraph

Article in Molecular bioSystems, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 25% 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

16 citing papers in PubMed, 49 citations in OpenAlex.

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  11. Tandem neopentyl glycol maltosides (TNMs) for membrane protein stabilisation.Chemical communications (Cambridge, England) · 2016
    Article
  12. Article
  13. Novel Xylene-Linked Maltoside Amphiphiles (XMAs) for Membrane Protein Stabilisation.Chemistry (Weinheim an der Bergstrasse, Germany) · 2015
    Article
  14. Article
  15. Article
  16. Novel tripod amphiphiles for membrane protein analysis.Chemistry (Weinheim an der Bergstrasse, Germany) · 2013
    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

3 authors at 2 institutions in 1 country.

Pil Seok ChaeDepartment of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI 53706 (USA). ; Tel: (+1) 608-262-3303.
Philip D Laible
Samuel H Gellman
University of Wisconsin–Madison · USArgonne National Laboratory · US

Funding

Synthesis/evaluation of novel surfactants for membrane protein structural biologyP01GM075913 · NIGMS · UNIVERSITY OF CHICAGO · PI LAIBLE, PHILIP D · 2005 to 2009
$4.2M
NIGMS NIH HHS P01 GM075913
6 · The paper itself

Abstract

Integral membrane proteins (IMPs) are crucial biological components, mediating the transfer of material and information between cells and their environment. Many IMPs have proven to be difficult to isolate and study. High-resolution structural information on this class of proteins is limited, largely because of difficulties in generating soluble forms of such proteins that retain native folding and activity, and difficulties in generating high-quality crystals from such preparations. Isolated IMPs typically do not dissolve in aqueous solution, a property that arises from the large patches of hydrophobic surface necessary for favorable interactions with the core of a lipid bilayer. Detergents are generally required for IMP solubilization: hydrophobic segments of detergent molecules cluster around and shield from water the hydrophobic protein surfaces. The critical role played by detergents in membrane protein manipulation, and the fact that many IMPs are recalcitrant to solubilization and/or crystallization with currently available detergents, suggest that it should be valuable to explore new types of amphiphiles for these purposes. This review constitutes a progress report on our long-term effort to develop a new class of organic molecules, collectively designated "tripod amphiphiles," that are intended as alternatives to conventional detergents for membrane protein manipulation. One long-range goal of this research is to identify new types of amphiphiles that facilitate IMP crystallization. This review should help introduce an important biochemical need to organic chemists, and perhaps inspire new approaches to the problem.

Identifiers

PMID23814603
PMCPMC3693755
OpenAlexW2148304771

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.