Evidence map›Paper›PMID 24158483›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Pheromone discrimination by a pH-tuned polymorphism of the Bombyx mori pheromone-binding protein.

Fred F Damberger, Erich Michel, Yuko Ishida, Walter S Leal, Kurt Wüthrich

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

22 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Transcriptome Profiling ofInternational journal of molecular sciences · 2025
    Article
  5. Article
  6. Olfactory Gene Families inInternational journal of molecular sciences · 2022
    Article
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  9. Review
  10. Review
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  15. Article
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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

5 authors at 2 institutions in 2 countries.

Fred F DambergerInstitute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zürich, CH-8093 Zurich, Switzerland.
Erich Michel
Yuko Ishida
Walter S Leal
Kurt Wüthrich
ETH Zurich · CHUniversity of California, Davis · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Bombyx mori pheromone-binding protein (BmorPBP) is known to adopt two different conformations. These are BmorPBP(A), where a regular helix formed by the C-terminal dodecapeptide segment, α7, occupies the ligand-binding cavity, and BmorPBP(B), where the binding site is free to accept ligands. NMR spectra of delipidated BmorPBP solutions at the physiological pH of the bulk sensillum lymph near pH 6.5 show only BmorPBP(A), and in mixtures, the two species are in slow exchange on the chemical shift frequency scale. This equilibrium has been monitored at variable pH and ligand concentrations, demonstrating that it is an intrinsic property of BmorPBP that is strongly affected by pH variation and ligand binding. This polymorphism tunes BmorPBP for optimal selective pheromone transport: Competition between α7 and lipophilic ligands for its binding cavity enables selective uptake of bombykol at the pore endings in the sensillum wall, whereas compounds with lower binding affinity can only be bound in the bulk sensillum lymph. After transport across the bulk sensillum lymph into the lower pH area near the dendritic membrane surface, bombykol is ejected near the receptor, whereas compounds with lower binding affinity are ejected before reaching the olfactory receptor, rendering them susceptible to degradation by enzymes present in the sensillum lymph.

Indexed as

Protein ConformationAnimalsBiological TransportBombyxCarrier ProteinsFatty AlcoholsHydrogen-Ion ConcentrationInsect ProteinsIntercellular Signaling Peptides and ProteinsMolecular StructureNuclear Magnetic Resonance, BiomolecularPheromonesPolymorphism, GeneticSmellbombykolCarrier ProteinsFatty AlcoholsInsect ProteinsIntercellular Signaling Peptides and Proteinspheromone-binding protein, BombyxPheromonesamide proton exchangeconformational equilibriuminsect odorant-binding proteinNMR structureselective transport of pheromones

Identifiers

PMID24158483
PMCPMC3832013
OpenAlexW1980006322

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.