Evidence map›Paper›PMID 21086444›Full record

ArticleProtein science : a publication of the Protein Society2011

Exploring the factors determining the dynamics of different protein folds.

S M Hollup, E Fuglebakk, W R Taylor, N Reuter

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

11 citing papers in PubMed, 26 citations in OpenAlex.

  1. Review
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  8. The interface of protein structure, protein biophysics, and molecular evolution.Protein science : a publication of the Protein Society · 2012
    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

4 authors at 2 institutions in 1 country.

S M HollupDepartment of Informatics, University of Bergen, N-5020 Bergen, Norway.
E Fuglebakk
W R Taylor
N Reuter
University of Bergen · NOUni Research (Norway) · NO

Funding

Medical Research Council U117581331
6 · The paper itself

Abstract

Normal mode analyses of homologous proteins at the family and superfamily level show that slow dynamics are similar and are preserved through evolution. This study investigates how the slow dynamics of proteins is affected by variation in the protein architecture and fold. For this purpose, we have used computer-generated protein models based on idealized protein structures with varying folds. These are shown to be protein-like in their behavior, and they are used to investigate the influence of architecture and fold on the slow dynamics. We compared the dynamics of models having different folds but similar architecture and found the architecture to be the dominant factor for the slow dynamics.

Indexed as

Protein FoldingComputer SimulationFlavodoxinGlutaredoxinsModels, MolecularProteinsProtein StabilityProtein Structure, SecondaryStatistics, NonparametricFlavodoxinGlutaredoxinsProteins

Identifiers

PMID21086444
PMCPMC3047076
OpenAlexW1504837664

What OpenQuestion holds

Textmetadata
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.