Evidence map›Paper›PMID 19253304›Full record

ArticleProteomics2009

Energetic determinants of protein binding specificity: insights into protein interaction networks.

Pablo Carbonell, Ruth Nussinov, Antonio del Sol

Abstract read
In one paragraph

Article in Proteomics, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing 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

21 citing papers in PubMed.

  1. Article
  2. Molecular basis for protein-protein interactions.Beilstein journal of organic chemistry · 2021
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  15. Review
  16. Topology of protein interaction network shapes protein abundances and strengths of their functional and nonspecific interactions.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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

3 authors.

Pablo CarbonellBioinformatics Research Unit, Research and Development Division, Fujirebio, Inc., Komiya-cho, Hachioji-shi, Tokyo, Japan.
Ruth Nussinov
Antonio del Sol

Funding

Protein Structure, Stability, and Amyloid FormationZIABC010440 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$11.8M
Biomolecular Recognition and Binding MechanismsZIABC010441 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2009 to 2025
$9.4M
Protein Structure, Stability, and Amyloid FormationZ01BC010440 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI NUSSINOV, RUTH · 2002 to 2008
$1.4M
Intramural NIH HHS Z01 BC010440NCI NIH HHS N01 CO012400NCI NIH HHS N01-CO-12400
6 · The paper itself

Abstract

One of the challenges of the postgenomic era is to provide a more realistic representation of cellular processes by combining a systems biology description of functional networks with information on their interacting components. Here we carried out a systematic large-scale computational study on a structural protein-protein interaction network dataset in order to dissect thermodynamic characteristics of binding determining the interplay between protein affinity and specificity. As expected, interactions involving specific binding sites display higher affinities than those of promiscuous binding sites. Next, in order to investigate a possible role of modular distribution of hot spots in binding specificity, we divided binding sites into modules previously shown to be energetically independent. In general, hot spots that interact with different partners are located in different modules. We further observed that common hot spots tend to interact with partners exhibiting common binding motifs, whereas different hot spots tend to interact with partners with different motifs. Thus, energetic properties of binding sites provide insights into the way proteins modulate interactions with different partners. Knowledge of those factors playing a role in protein specificity is important for understanding how proteins acquire additional partners during evolution. It should also be useful in drug design.

Indexed as

Protein BindingProtein Interaction Domains and MotifsProtein Interaction MappingCalcium-Calmodulin-Dependent Protein KinasesComputer SimulationCytochromes bFungal ProteinsGTP PhosphohydrolasesProteinsSubstrate SpecificityThermodynamicsUbiquitinYeastsCalcium-Calmodulin-Dependent Protein KinasesCytochromes bFungal ProteinsGTP PhosphohydrolasesProteinsUbiquitin

Identifiers

PMID19253304
PMCPMC7299235

What OpenQuestion holds

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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.