Evidence map›Paper›PMID 21801404›Full record

ArticleBMC bioinformatics2011

Comprehensive, atomic-level characterization of structurally characterized protein-protein interactions: the PICCOLO database.

George R Bickerton, Alicia P Higueruelo, Tom L Blundell

Abstract read
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Article in BMC bioinformatics, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

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0cells of the map it votes in
30citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

Who cites it

30 citing papers in PubMed.

  1. COCFrontiers in bioinformatics · 2025
    Article
  2. Article
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  4. Inhibition of FOXP3 by stapled alpha-helical peptides dampens regulatory T cell function.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Structural landscapes of PPI interfaces.Briefings in bioinformatics · 2022
    Review
  6. mPPI: a database extension to visualize structural interactome in a one-to-many manner.Database : the journal of biological databases and curation · 2021
    Article
  7. Structural motifs in protein cores and at protein-protein interfaces are different.Protein science : a publication of the Protein Society · 2021
    Article
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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

George R BickertonDepartment of Biochemistry, University of Cambridge, Cambridge, CB2 1GA, UK. grbickerton@dundee.ac.uk
Alicia P Higueruelo
Tom L Blundell

Funding

Biotechnology and Biological Sciences Research Council
6 · The paper itself

Abstract

backgroundStructural studies are increasingly providing huge amounts of information on multi-protein assemblies. Although a complete understanding of cellular processes will be dependent on an explicit characterization of the intermolecular interactions that underlie these assemblies and mediate molecular recognition, these are not well described by standard representations.

resultsHere we present PICCOLO, a comprehensive relational database capturing the details of structurally characterized protein-protein interactions. Interactions are described at the level of interacting pairs of atoms, residues and polypeptide chains, with the physico-chemical nature of the interactions being characterized. Distance and angle terms are used to distinguish 12 different interaction types, including van der Waals contacts, hydrogen bonds and hydrophobic contacts. The explicit aim of PICCOLO is to underpin large-scale analyses of the properties of protein-protein interfaces. This is exemplified by an analysis of residue propensity and interface contact preferences derived from a much larger data set than previously reported. However, PICCOLO also supports detailed inspection of particular systems of interest.

conclusionsThe current PICCOLO database comprises more than 260 million interacting atom pairs from 38,202 protein complexes. A web interface for the database is available at http://www-cryst.bioc.cam.ac.uk/piccolo.

Indexed as

Databases, ProteinHumansModels, MolecularProtein Interaction MappingProteinsSoftwareProteins

Identifiers

PMID21801404
PMCPMC3161047

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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.