Evidence map›Paper›PMID 25279835›Full record

ArticlePloS one2014

The structure, stability and pheromone binding of the male mouse protein sex pheromone darcin.

Marie M Phelan, Lynn McLean, Stuart D Armstrong, Jane L Hurst, Robert J Beynon, Lu-Yun Lian

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
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

11 citing papers in PubMed, 30 citations in OpenAlex.

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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

6 authors at 1 institution in 1 country.

Marie M PhelanNMR Centre for Structural Biology, Institute of Integrative Biology, University of Liverpool, Liverpool, United Kingdom.
Lynn McLeanProtein Function Group, Institute of Integrative Biology, University of Liverpool, Liverpool, United Kingdom.
Stuart D ArmstrongProtein Function Group, Institute of Integrative Biology, University of Liverpool, Liverpool, United Kingdom.
Jane L HurstMammalian Behaviour & Evolution Group, Institute of Integrative Biology, University of Liverpool, Leahurst Campus, Neston, United Kingdom.
Robert J BeynonProtein Function Group, Institute of Integrative Biology, University of Liverpool, Liverpool, United Kingdom.
Lu-Yun LianNMR Centre for Structural Biology, Institute of Integrative Biology, University of Liverpool, Liverpool, United Kingdom.
University of Liverpool · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J002631/1
6 · The paper itself

Abstract

Mouse urine contains highly polymorphic major urinary proteins that have multiple functions in scent communication through their abilities to bind, transport and release hydrophobic volatile pheromones. The mouse genome encodes for about 20 of these proteins and are classified, based on amino acid sequence similarity and tissue expression patterns, as either central or peripheral major urinary proteins. Darcin is a male specific peripheral major urinary protein and is distinctive in its role in inherent female attraction. A comparison of the structure and biophysical properties of darcin with MUP11, which belongs to the central class, highlights similarity in the overall structure between the two proteins. The thermodynamic stability, however, differs between the two proteins, with darcin being much more stable. Furthermore, the affinity of a small pheromone mimetic is higher for darcin, although darcin is more discriminatory, being unable to bind bulkier ligands. These attributes are due to the hydrophobic ligand binding cavity of darcin being smaller, caused by the presence of larger amino acid side chains. Thus, the physical and chemical characteristics of the binding cavity, together with its extreme stability, are consistent with darcin being able to exert its function after release into the environment.

Indexed as

Models, MolecularAmino Acid SequenceAnimalsBinding SitesCalorimetryHydrophobic and Hydrophilic InteractionsIntercellular Signaling Peptides and ProteinsLigandsMaleMiceMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularProtein BindingProtein ConformationProtein DenaturationProteinsIntercellular Signaling Peptides and ProteinsLigandsMup20 protein, mouseProteinsRecombinant ProteinsSex Attractants

Identifiers

PMID25279835
PMCPMC4184797
OpenAlexW2137424356

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.