Evidence map›Paper›PMID 25877662›Full record

ArticleProtein engineering, design & selection : PEDS2015

Solution structure of a soluble fragment derived from a membrane protein by shotgun proteolysis.

Mark D Allen, Mary Christie, Peter Jones, Benjamin T Porebski, Brendan Roome, Stefan M V Freund, Ashley M Buckle, Mark Bycroft, Daniel Christ

Open access · bronzeAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Protein engineering, design & selection : PEDS, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

4 citing papers in PubMed, 7 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. 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

9 authors at 3 institutions in 2 countries.

Mark D AllenMRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.
Mary ChristieDepartment of Immunology, Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, Sydney, NSW 2010, Australia Faculty of Medicine, St Vincent's Clinical School, The University of New South Wales, Darlinghurst, Sydney, NSW 2010, Australia.
Peter JonesMRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.
Benjamin T PorebskiDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.
Brendan RoomeDepartment of Immunology, Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, Sydney, NSW 2010, Australia Faculty of Medicine, St Vincent's Clinical School, The University of New South Wales, Darlinghurst, Sydney, NSW 2010, Australia.
Stefan M V FreundMRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.
Ashley M BuckleDepartment of Biochemistry and Molecular Biology, Monash University, Clayton, Victoria 3800, Australia.
Mark BycroftMRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK.
Daniel ChristDepartment of Immunology, Garvan Institute of Medical Research, 384 Victoria Street, Darlinghurst, Sydney, NSW 2010, Australia Faculty of Medicine, St Vincent's Clinical School, The University of New South Wales, Darlinghurst, Sydney, NSW 2010, Australia d.christ@garvan.org.au.
MRC Laboratory of Molecular Biology · GBUNSW Sydney · AUMonash University · AU

Funding

Medical Research Council MC_U105184326
6 · The paper itself

Abstract

We have previously reported a phage display method for the identification of protein domains on a genome-wide scale (shotgun proteolysis). Here we present the solution structure of a fragment of the Escherichia coli membrane protein yrfF, as identified by shotgun proteolysis, and determined by NMR spectroscopy. Despite the absence of computational predictions, the fragment formed a well-defined beta-barrel structure, distantly falling within the OB-fold classification. Our results highlight the potential of high-throughput experimental approaches for the identification of protein domains for structural studies.

Indexed as

ProteolysisAmino Acid SequenceEscherichia coli ProteinsMagnetic Resonance SpectroscopyMembrane ProteinsModels, MolecularMolecular Sequence DataPeptide FragmentsProtein Structure, SecondarySequence AnalysisSolubilityEscherichia coli ProteinsMembrane ProteinsPeptide FragmentsyrfF protein, E colimembrane proteinsNMR spectroscopyphage displayprotein domainsproteolysis

Identifiers

PMID25877662
PMCPMC4661788
OpenAlexW1983864727

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.