Evidence map›Paper›PMID 16322766›Full record

ArticlePLoS computational biology2005

Refining protein subcellular localization.

Michelle S Scott, Sara J Calafell, David Y Thomas, Michael T Hallett

Abstract read
In one paragraph

Article in PLoS computational biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
–field-weighted citation impact
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

60 citing papers in PubMed.

  1. Article
  2. PTEN Subcellular Localization Dictates Function.bioRxiv : the preprint server for biology · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Review
  7. Druggable proteins ofFrontiers in pharmacology · 2025
    Article
  8. International journal of genomics · 2025
    Article
  9. Article
  10. Designing a multi-epitope vaccine againstFrontiers in genetics · 2024
    Article
  11. Article
  12. Comprehensive Analysis and Functional Verification of theInternational journal of molecular sciences · 2023
    Article
  13. Article
  14. Article
  15. Review
  16. Functional Analysis of Hypothetical Proteins ofBioinformatics and biology insights · 2022
    Article
  17. Genome-Wide Identification and Analysis of the Polycomb Group Family inInternational journal of molecular sciences · 2021
    Article
  18. Article
  19. Protein Subcellular Localization Prediction.Methods in molecular biology (Clifton, N.J.) · 2021
    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.

Michelle S ScottMcGill Center for Bioinformatics, McGill University, Montreal, Quebec, Canada.
Sara J Calafell
David Y Thomas
Michael T Hallett

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The study of protein subcellular localization is important to elucidate protein function. Even in well-studied organisms such as yeast, experimental methods have not been able to provide a full coverage of localization. The development of bioinformatic predictors of localization can bridge this gap. We have created a Bayesian network predictor called PSLT2 that considers diverse protein characteristics, including the combinatorial presence of InterPro motifs and protein interaction data. We compared the localization predictions of PSLT2 to high-throughput experimental localization datasets. Disagreements between these methods generally involve proteins that transit through or reside in the secretory pathway. We used our multi-compartmental predictions to refine the localization annotations of yeast proteins primarily by distinguishing between soluble lumenal proteins and soluble proteins peripherally associated with organelles. To our knowledge, this is the first tool to provide this functionality. We used these sub-compartmental predictions to characterize cellular processes on an organellar scale. The integration of diverse protein characteristics and protein interaction data in an appropriate setting can lead to high-quality detailed localization annotations for whole proteomes. This type of resource is instrumental in developing models of whole organelles that provide insight into the extent of interaction and communication between organelles and help define organellar functionality.

Indexed as

Amino Acid MotifsComputational BiologyDatabases, ProteinProtein BindingProteinsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID16322766
PMCPMC1289393

What OpenQuestion holds

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LicenceCC BY
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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.