Evidence map›Paper›PMID 17078969›Full record

ArticleJournal of molecular biology2007

Characteristics affecting expression and solubilization of yeast membrane proteins.

Michael A White, Kathleen M Clark, Elizabeth J Grayhack, Mark E Dumont

Open access · greenAbstract read
In one paragraph

Article in Journal of molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed, 1 pooled it
1.8field-weighted citation impact, top 17% 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

20 citing papers in PubMed, 1 synthesis or guideline pooled it, 44 citations in OpenAlex.

  1. Pooled it
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  4. Review
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  11. N-terminal domain of the V-ATPase a2-subunit displays integral membrane protein properties.Protein science : a publication of the Protein Society · 2010
    Article
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  15. Review
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  17. Article
  18. Quality control of overexpressed membrane proteins.Proceedings of the National Academy of Sciences of the United States of America · 2008
    Article
  19. Expression screening of integral membrane proteins from Helicobacter pylori 26695.Protein science : a publication of the Protein Society · 2007
    Article
  20. 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

4 authors at 1 institution in 1 country.

Michael A WhiteDepartment of Biochemistry and Biophysics, University of Rochester Medical Center, Rochester, NY 14642, USA.
Kathleen M Clark
Elizabeth J Grayhack
Mark E Dumont
University of Rochester Medical Center · US

Funding

TOOLS FOR HIGH THROUGHPUT STRUCTURAL BIOLOGYU54GM074899 · NIGMS · HAUPTMAN-WOODWARD MEDICAL RESEARCH INST · PI DETITTA, GEORGE T · 2005 to 2010
$16.5M
Biochemical Genomics Linking Genes and ActivitiesR01HG002311 · NHGRI · UNIVERSITY OF ROCHESTER · PI PHIZICKY, ERIC M. · 2001 to 2004
$1.7M
NHGRI NIH HHS HG 02311NHGRI NIH HHS R01 HG002311NIGMS NIH HHS U54 GM 074899NIGMS NIH HHS U54 GM074899
6 · The paper itself

Abstract

Biochemical and structural analysis of membrane proteins often critically depends on the ability to overexpress and solubilize them. To identify properties of eukaryotic membrane proteins that may be predictive of successful overexpression, we analyzed expression levels of the genomic complement of over 1000 predicted membrane proteins in a recently completed Saccharomyces cerevisiae protein expression library. We detected statistically significant positive and negative correlations between high membrane protein expression and protein properties such as size, overall hydrophobicity, number of transmembrane helices, and amino acid composition of transmembrane segments. Although expression levels of membrane and soluble proteins exhibited similar negative correlations with overall hydrophobicity, high-level membrane protein expression was positively correlated with the hydrophobicity of predicted transmembrane segments. To further characterize yeast membrane proteins as potential targets for structure determination, we tested the solubility of 122 of the highest expressed yeast membrane proteins in six commonly used detergents. Almost all the proteins tested could be solubilized using a small number of detergents. Solubility in some detergents depended on protein size, number of transmembrane segments, and hydrophobicity of predicted transmembrane segments. These results suggest that bioinformatic approaches may be capable of identifying membrane proteins that are most amenable to overexpression and detergent solubilization for structural and biochemical analyses. Bioinformatic approaches could also be used in the redesign of proteins that are not intrinsically well-adapted to such studies.

Indexed as

Adenosine TriphosphatasesCell MembraneDetergentsGene ExpressionHydrophobic and Hydrophilic InteractionsMembrane ProteinsMicellesMolecular WeightSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSolubilityTitrimetryAdenosine TriphosphatasesDetergentsMembrane ProteinsMicellesSaccharomyces cerevisiae Proteins

Identifiers

PMID17078969
PMCPMC1839945
OpenAlexW1977121829

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.