Evidence map›Paper›PMID 23098413›Full record

ArticleJournal of proteome research2012

High-throughput isolation and characterization of untagged membrane protein complexes: outer membrane complexes of Desulfovibrio vulgaris.

Peter J Walian, Simon Allen, Maxim Shatsky, Lucy Zeng, Evelin D Szakal, Haichuan Liu, Steven C Hall, Susan J Fisher, Bonita R Lam, Mary E Singer and 7 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of proteome research, 2012. 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
0.7field-weighted citation impact, top 31% 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, 32 citations in OpenAlex.

  1. Article
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  3. Reconstitution of a biofilm adhesin system from a sulfate-reducing bacterium inProceedings of the National Academy of Sciences of the United States of America · 2024
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  5. Microorganisms · 2023
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  6. Genomic insight into iron acquisition by sulfate-reducing bacteria in microaerophilic environments.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023
    Review
  7. Article
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  10. Review
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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

17 authors at 4 institutions in 1 country.

Peter J WalianLawrence Berkeley National Laboratory, Berkeley, California, United States. pjwalian@lbl.gov
Simon Allen
Maxim Shatsky
Lucy Zeng
Evelin D Szakal
Haichuan Liu
Steven C Hall
Susan J Fisher
Bonita R Lam
Mary E Singer
Jil T Geller
Steven E Brenner
John-Marc Chandonia
Terry C Hazen
H Ewa Witkowska
Mark D Biggin
Bing K Jap
Lawrence Berkeley National Laboratory · USUniversity of California, San Francisco · USUniversity of California, Berkeley · USUniversity of Tennessee System · US

Funding

Translational InformaticsP30CA082103 · NCI · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI Jennifer Leigh Clarke · 1999 to 2026
$209.7M
NCI NIH HHS P30 CA082103
6 · The paper itself

Abstract

Cell membranes represent the "front line" of cellular defense and the interface between a cell and its environment. To determine the range of proteins and protein complexes that are present in the cell membranes of a target organism, we have utilized a "tagless" process for the system-wide isolation and identification of native membrane protein complexes. As an initial subject for study, we have chosen the Gram-negative sulfate-reducing bacterium Desulfovibrio vulgaris. With this tagless methodology, we have identified about two-thirds of the outer membrane- associated proteins anticipated. Approximately three-fourths of these appear to form homomeric complexes. Statistical and machine-learning methods used to analyze data compiled over multiple experiments revealed networks of additional protein-protein interactions providing insight into heteromeric contacts made between proteins across this region of the cell. Taken together, these results establish a D. vulgaris outer membrane protein data set that will be essential for the detection and characterization of environment-driven changes in the outer membrane proteome and in the modeling of stress response pathways. The workflow utilized here should be effective for the global characterization of membrane protein complexes in a wide range of organisms.

Indexed as

Bacterial Outer Membrane ProteinsCell MembraneChromatography, Ion ExchangeDesulfovibrio vulgarisDetergentsElectrophoresis, Polyacrylamide GelEscherichia coliHigh-Throughput Screening AssaysMass SpectrometryMembrane ProteinsMolecular WeightMultiprotein ComplexesPeriplasmProtein Interaction MappingProtein Interaction MapsProteomeBacterial Outer Membrane ProteinsDetergentsMembrane ProteinsMultiprotein ComplexesProteome

Identifiers

PMID23098413
PMCPMC3516867
OpenAlexW2139876247

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.