Evidence map›Paper›PMID 26618518›Full record

ArticlePLoS biology2015

Tandem Domains with Tuned Interactions Are a Powerful Biological Design Principle.

Ruth Nussinov, Chung-Jung Tsai

Abstract read
In one paragraph

Article in PLoS biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Structure-Function Relationship of the β-Hairpin ofInternational journal of molecular sciences · 2025
    Article
  2. 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

2 authors.

Ruth NussinovCancer and Inflammation Program, Leidos Biomedical Research, Inc., Frederick, Maryland, United States of America.
Chung-Jung TsaiCancer and Inflammation Program, Leidos Biomedical Research, Inc., Frederick, Maryland, United States of America.

Funding

CCR NIH HHS HHSN261200800001CIntramural NIH HHSNCI NIH HHS HHSN261200800001E
6 · The paper itself

Abstract

Allosteric effects of mutations, ligand binding, or post-translational modifications on protein function occur through changes to the protein's shape, or conformation. In a cell, there are many copies of the same protein, all experiencing these perturbations in a dynamic fashion and fluctuating through different conformations and activity states. According to the "conformational selection and population shift" theory, ligand binding selects a particular conformation. This perturbs the ensemble and induces a population shift. In a new PLOS Biology paper, Melacini and colleagues describe a novel model of protein regulation, the "Double-Conformational Selection Model", which demonstrates how two tandem ligand-binding domains interact to regulate protein function. Here we explain how tandem domains with tuned interactions-but not single domains-can provide a blueprint for sensitive activation sensors within a narrow window of ligand concentration, thereby promoting signaling control.

Indexed as

Evolution, MolecularModels, MolecularAnimalsCyclic AMP-Dependent Protein Kinase Catalytic SubunitsCyclic AMP-Dependent Protein Kinase RIalpha SubunitEnzyme ActivationEnzymesHumansLigandsMutationProtein ConformationProtein Interaction Domains and MotifsProtein SubunitsTandem Repeat SequencesCyclic AMP-Dependent Protein Kinase Catalytic SubunitsCyclic AMP-Dependent Protein Kinase RIalpha SubunitEnzymesLigandsProtein Subunits

Identifiers

PMID26618518
PMCPMC4664463

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.