Evidence map›Paper›PMID 19308324›Full record

ReviewCellular and molecular life sciences : CMLS2009

Functional aspects of protein flexibility.

Kaare Teilum, Johan G Olsen, Birthe B Kragelund

Abstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 113 papers.

0numbers the graph read from it
0cells of the map it votes in
113citing 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

113 citing papers in PubMed.

  1. Article
  2. Article
  3. A Multi-Stimuli Transformational Network of Benzil-Based Pd(II) Assemblies.Angewandte Chemie (International ed. in English) · 2026
    Article
  4. Article
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  15. Article
  16. PEGASUS: Prediction of MD-derived protein flexibility from sequence.Protein science : a publication of the Protein Society · 2025
    Article
  17. Article
  18. 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025
    Review
  19. Review
  20. Data-driven evaluation of suitable immunogens for improved antibody selection.Protein science : a publication of the Protein Society · 2025
    Article

53 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.

Kaare TeilumStructural Biology and NMR Laboratory (SBiN-Lab), Department of Biology, University of Copenhagen, Ole Maaloes Vej 5, Copenhagen N, Denmark.
Johan G Olsen
Birthe B Kragelund

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Proteins are dynamic entities, and they possess an inherent flexibility that allows them to function through molecular interactions within the cell, among cells and even between organisms. Appreciation of the non-static nature of proteins is emerging, but to describe and incorporate this into an intuitive perception of protein function is challenging. Flexibility is of overwhelming importance for protein function, and the changes in protein structure during interactions with binding partners can be dramatic. The present review addresses protein flexibility, focusing on protein-ligand interactions. The thermodynamics involved are reviewed, and examples of structure-function studies involving experimentally determined flexibility descriptions are presented. While much remains to be understood about protein flexibility, it is clear that it is encoded within their amino acid sequence and should be viewed as an integral part of their structure.

Indexed as

Binding SitesLigandsModels, MolecularProtein BindingProtein ConformationProteinsStructure-Activity RelationshipThermodynamicsLigandsProteins

Identifiers

PMID19308324
PMCPMC11115794

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.