Evidence map›Paper›PMID 10933509›Full record

ArticleProtein science : a publication of the Protein Society2000

Mesoscopic surfactant organization and membrane protein crystallization.

M C Wiener, A S Verkman, R M Stroud, A N van Hoek

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein science : a publication of the Protein Society, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

4 authors.

M C WienerDepartment of Molecular Physiology & Biological Physics, University of Virginia, Charlottesville 22908-0736, USA. mwiener@virginia.edu
A S Verkman
R M Stroud
A N van Hoek

Funding

STRUCTURE/FUNCTION OF PROTEINS AT MOLECULAR LEVELR01GM024485 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 1985 to 2024
$7.5M
Molecular Basis for Transmembrane Conduction & SignalingR37GM024485 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI STROUD, ROBERT M · 2007 to 2016
$4.7M
X RAY CRYSTALLOGRAPHY OF HUMAN AQUAPORIN WATER CHANNELSR01GM056251 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI WIENER, MICHAEL C. · 1997 to 2001
$399k
NIGMS NIH HHS GM24485NIGMS NIH HHS GM56251
6 · The paper itself

Abstract

The paucity of detailed X-ray crystallographic structures of integral membrane proteins arises from substantive technical obstacles in the overexpression of multimilligram quantities of protein, and in the crystallization of purified protein-detergent complexes (PDCs). With rare exception, crystal contacts within the lattice are mediated by protein-protein interaction, and the detergent surrounding the protein behaves as a disordered solvent. The addition and use of surfactants that display mesoscopic self-assembly behavior in membrane protein crystallization experiments presents a novel alternative strategy. Well-ordered crystals of the water channel human aquaporin-1 (hAQP1) that diffract to 4 A resolution have been obtained with this approach.

Indexed as

Aquaporin 1AquaporinsBlood Group AntigensCrystallizationCrystallography, X-RayDeoxycholic AcidHumansMembrane ProteinsSurface-Active AgentsAQP1 protein, humanAquaporin 1AquaporinsBlood Group AntigensDeoxycholic AcidMembrane ProteinsSurface-Active Agents

Identifiers

PMID10933509
PMCPMC2144676

What OpenQuestion holds

Textmetadata
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.