Evidence map›Paper›PMID 23745135›Full record

ArticleEvolutionary applications2013

Structural dynamics flexibility informs function and evolution at a proteome scale.

Zeynep Nevin Gerek, Sudhir Kumar, Sefika Banu Ozkan

Open access · goldAbstract read
In one paragraph

Article in Evolutionary applications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
3.7field-weighted citation impact, top 6% 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

65 citing papers in PubMed, 108 citations in OpenAlex.

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  15. Engineering gain-of-function mutants of a WW domain by dynamics and structural analysis.Protein science : a publication of the Protein Society · 2023
    Article
  16. Allosteric regulatory control in dihydrofolate reductase is revealed by dynamic asymmetry.Protein science : a publication of the Protein Society · 2023
    Article
  17. Article
  18. Functional Protein Dynamics Directly from Sequences.The journal of physical chemistry. B · 2023
    Article
  19. Article
  20. Article

5 more citing papers are in PubMed but not listed here.

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 at 2 institutions in 1 country.

Zeynep Nevin GerekCenter for Evolutionary Medicine and Informatics, Biodesign Institute, Arizona State University Tempe, AZ, USA ; Department of Physics, Center for Biological Physics, Bateman Physical Sciences F-Wing, Arizona State University Tempe, AZ, USA.
Sudhir Kumar
Sefika Banu Ozkan
Physical Sciences (United States) · USArizona State University · US

Funding

Center for the Rational Design of Membrane Protein CrystallographyU54GM094599 · NIGMS · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI FROMME, PETRA · 2010 to 2014
$6.8M
COMPARATIVE MOLECULAR SEQUENCE ANALYSISR01HG002096 · NHGRI · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI KUMAR, SUDHIR · 2000 to 2013
$3.0M
Evolutionary Bioinformatics of Human MutationsR01LM010834 · NLM · ARIZONA STATE UNIVERSITY-TEMPE CAMPUS · PI KUMAR, SUDHIR · 2010 to 2012
$1.1M
NHGRI NIH HHS R01 HG002096NIGMS NIH HHS U54 GM094599NLM NIH HHS R01 LM010834
6 · The paper itself

Abstract

Protein structures are dynamic entities with a myriad of atomic fluctuations, side-chain rotations, and collective domain movements. Although the importance of these dynamics to proper functioning of proteins is emerging in the studies of many protein families, there is a lack of broad evidence for the critical role of protein dynamics in shaping the biological functions of a substantial fraction of residues for a large number of proteins in the human proteome. Here, we propose a novel dynamic flexibility index (dfi) to quantify the dynamic properties of individual residues in any protein and use it to assess the importance of protein dynamics in 100 human proteins. Our analyses involving functionally critical positions, disease-associated and putatively neutral population variations, and the rate of interspecific substitutions per residue produce concordant patterns at a proteome scale. They establish that the preservation of dynamic properties of residues in a protein structure is critical for maintaining the protein/biological function. Therefore, structural dynamics needs to become a major component of the analysis of protein function and evolution. Such analyses will be facilitated by the dfi, which will also enable the integrative use of structural dynamics with evolutionary conservation in genomic medicine as well as functional genomics investigations.

Indexed as

elastic network modelsfunctional genomicssingle nucleotide variantsstructural dynamics

Identifiers

PMID23745135
PMCPMC3673471
OpenAlexW2013253738

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.