Evidence map›Paper›PMID 23239312›Full record

ArticleProteins2013

Predicting permanent and transient protein-protein interfaces.

David La, Misun Kong, William Hoffman, Youn Im Choi, Daisuke Kihara

Abstract read
In one paragraph

Article in Proteins, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

23 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
  2. Beyond contacts: The important role of the support region in protein complex assembly.Protein science : a publication of the Protein Society · 2026
    Article
  3. Article
  4. Article
  5. Article
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  7. Article
  8. Article
  9. LZerD Protein-Protein Docking Webserver Enhanced WithFrontiers in molecular biosciences · 2021
    Review
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  13. Review
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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 1 institution in 1 country.

David LaDepartment of Biological Sciences, College of Science, Purdue University, West Lafayette, Indiana 47907, USA.
Misun Kong
William Hoffman
Youn Im Choi
Daisuke Kihara
Purdue University West Lafayette · US

Funding

Surface Shape Based Screening of Large Protein DatabasesR01GM075004 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI KIHARA, DAISUKE · 2005 to 2009
$1.5M
Identification of protein-metabolite interactome.R01GM097528 · NIGMS · PURDUE UNIVERSITY · PI KIHARA, DAISUKE · 2011 to 2014
$1.1M
Role of Mitochondrial CYP2E1 in Chemical Exposure-Driven NeurodegenerationF32ES027306 · NIEHS · DUKE UNIVERSITY · PI HARTMAN, JESSICA HELENE · 2016 to 2018
$171k
NIEHS NIH HHS 27306C0004NIGMS NIH HHS R01 GM075004NIGMS NIH HHS R01GM075004NIGMS NIH HHS R01 GM097528NIGMS NIH HHS R01GM097528
6 · The paper itself

Abstract

Protein-protein interactions (PPIs) are involved in diverse functions in a cell. To optimize functional roles of interactions, proteins interact with a spectrum of binding affinities. Interactions are conventionally classified into permanent and transient, where the former denotes tight binding between proteins that result in strong complexes, whereas the latter compose of relatively weak interactions that can dissociate after binding to regulate functional activity at specific time point. Knowing the type of interactions has significant implications for understanding the nature and function of PPIs. In this study, we constructed amino acid substitution models that capture mutation patterns at permanent and transient type of protein interfaces, which were found to be different with statistical significance. Using the substitution models, we developed a novel computational method that predicts permanent and transient protein binding interfaces (PBIs) in protein surfaces. Without knowledge of the interacting partner, the method uses a single query protein structure and a multiple sequence alignment of the sequence family. Using a large dataset of permanent and transient proteins, we show that our method, BindML+, performs very well in protein interface classification. A very high area under the curve (AUC) value of 0.957 was observed when predicted protein binding sites were classified. Remarkably, near prefect accuracy was achieved with an AUC of 0.991 when actual binding sites were classified. The developed method will be also useful for protein design of permanent and transient PBIs.

Indexed as

Models, BiologicalProtein Interaction MapsAlgorithmsAmino Acid SequenceAmino Acid SubstitutionBinding SitesDatabases, ProteinModels, MolecularMolecular Sequence DataProtein BindingProteinsProtein Structure, SecondaryProteins

Identifiers

PMID23239312
PMCPMC4084939
OpenAlexW2166496883

What OpenQuestion holds

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LicenceTDM
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.