Evidence map›Paper›PMID 19166624›Full record

ArticleBMC bioinformatics2009

VASCo: computation and visualization of annotated protein surface contacts.

Georg Steinkellner, Robert Rader, Gerhard G Thallinger, Christoph Kratky, Karl Gruber

Abstract read
In one paragraph

Article in BMC bioinformatics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing 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

44 citing papers in PubMed.

  1. Article
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  4. Re-engineering a transferase scaffold for indole C3 methylation in diketopiperazines.Protein science : a publication of the Protein Society · 2025
    Article
  5. AMPEC4:Molecules (Basel, Switzerland) · 2025
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  7. Article
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  12. eLife · 2023
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Structure and Catalytic Mechanism of a Bacterial Friedel-Crafts Acylase.Chembiochem : a European journal of chemical biology · 2019
    Article
  18. Article
  19. 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

5 authors.

Georg SteinkellnerInstitute of Molecular Biosciences, University of Graz, Humboldtstrasse 50/3, Graz, Austria. georg.steinkellner@uni-graz.at
Robert Rader
Gerhard G Thallinger
Christoph Kratky
Karl Gruber

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundStructural data from crystallographic analyses contain a vast amount of information on protein-protein contacts. Knowledge on protein-protein interactions is essential for understanding many processes in living cells. The methods to investigate these interactions range from genetics to biophysics, crystallography, bioinformatics and computer modeling. Also crystal contact information can be useful to understand biologically relevant protein oligomerisation as they rely in principle on the same physico-chemical interaction forces. Visualization of crystal and biological contact data including different surface properties can help to analyse protein-protein interactions.

resultsVASCo is a program package for the calculation of protein surface properties and the visualization of annotated surfaces. Special emphasis is laid on protein-protein interactions, which are calculated based on surface point distances. The same approach is used to compare surfaces of two aligned molecules. Molecular properties such as electrostatic potential or hydrophobicity are mapped onto these surface points. Molecular surfaces and the corresponding properties are calculated using well established programs integrated into the package, as well as using custom developed programs. The modular package can easily be extended to include new properties for annotation. The output of the program is most conveniently displayed in PyMOL using a custom-made plug-in.

conclusionVASCo supplements other available protein contact visualisation tools and provides additional information on biological interactions as well as on crystal contacts. The tool provides a unique feature to compare surfaces of two aligned molecules based on point distances and thereby facilitates the visualization and analysis of surface differences.

Indexed as

SoftwareBinding SitesDatabases, ProteinHydrophobic and Hydrophilic InteractionsModels, MolecularProtein ConformationProteinsProteins

Identifiers

PMID19166624
PMCPMC2649047

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.