Evidence map›Paper›PMID 24628212›Full record

ArticleThe Journal of chemical physics2014

Folding and self-assembly of a small heterotetramer.

Fatih Yaşar, Adam K Sieradzan, Ulrich H E Hansmann

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in The Journal of chemical physics, 2014. 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. Computational Models for the Study of Protein Aggregation.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  2. Review
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.

Fatih YaşarDepartment of Physics Engineering, Hacettepe University, Beytepe-Ankara 06800, Turkey.
Adam K SieradzanFaculty of Chemistry, University of Gdańsk, Wita Stwosza 63, 80-952 Gdańsk, Poland.
Ulrich H E HansmannDepartment of Chemistry and Biochemistry, University of Oklahoma, Norman, Oklahoma 73019-5251, USA.

Funding

Folding, Mis-Folding and Aggregation of Small ProteinsR01GM062838 · NIGMS · UNIVERSITY OF OKLAHOMA · PI HANSMANN, ULRICH H.E. · 2003 to 2012
$1.4M
NIGMS NIH HHS GM62838NIGMS NIH HHS R01 GM062838
6 · The paper itself

Abstract

Designed miniproteins offer a possibility to study folding and association of protein complexes, both experimentally and in silico. Using replica exchange molecular dynamics and the coarse-grain UNRES force field, we have simulated the folding and self-assembly of the heterotetramer BBAThet1, comparing it with that of the homotetramer BBAT1 which has the same size and ββα-fold. For both proteins, association of the tetramer precedes and facilitates folding of the individual chains.

Indexed as

Molecular Dynamics SimulationProtein FoldingProtein MultimerizationProteinsProtein Structure, SecondaryTemperatureProteins

Identifiers

PMID24628212
PMCPMC3977861

What OpenQuestion holds

Textmetadata
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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.