Evidence map›Paper›PMID 26549015›Full record

ArticleScientific reports2015

Deciphering Supramolecular Structures with Protein-Protein Interaction Network Modeling.

Toshiyuki Tsuji, Takao Yoda, Tsuyoshi Shirai

Abstract read
In one paragraph

Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Integrative modelling of cellular assemblies.Current opinion in structural biology · 2017
    Review
  4. 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

3 authors.

Toshiyuki TsujiNagahama Institute of Bio-Science and Technology, and Japan Science and Technology Agency, Bioinformatics Research Division, Nagahama, Shiga 526-0829, Japan.
Takao YodaNagahama Institute of Bio-Science and Technology, and Japan Science and Technology Agency, Bioinformatics Research Division, Nagahama, Shiga 526-0829, Japan.
Tsuyoshi ShiraiNagahama Institute of Bio-Science and Technology, and Japan Science and Technology Agency, Bioinformatics Research Division, Nagahama, Shiga 526-0829, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Many biological molecules are assembled into supramolecules that are essential to perform complicated functions in the cell. However, experimental information about the structures of supramolecules is not sufficient at this point. We developed a method of predicting and modeling the structures of supramolecules in a biological network by combining structural data of the Protein Data Bank (PDB) and interaction data in IntAct databases. Templates for binary complexes in IntAct were extracted from PDB. Modeling was attempted by assembling binary complexes with superposed shared subunits. A total of 3,197 models were constructed, and 1,306 (41% of the total) contained at least one subunit absent from experimental structures. The models also suggested 970 (25% of the total) experimentally undetected subunit interfaces, and 41 human disease-related amino acid variants were mapped onto these model-suggested interfaces. The models demonstrated that protein-protein interaction network modeling is useful to fill the information gap between biological networks and structures.

Indexed as

Models, MolecularProtein ConformationProtein Interaction MapsAmino Acid SubstitutionComputational BiologyDatabases, ProteinHumansMultiprotein ComplexesProtein BindingProtein Interaction MappingProteinsMultiprotein ComplexesProteins

Identifiers

PMID26549015
PMCPMC4637837

What OpenQuestion holds

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Registered trials

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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.