Evidence map›Paper›PMID 30019371›Full record

ArticleProtein science : a publication of the Protein Society2018

Disordered linkers in multidomain allosteric proteins: Entropic effect to favor the open state or enhanced local concentration to favor the closed state?

Maodong Li, Huaiqing Cao, Luhua Lai, Zhirong Liu

Abstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing 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

20 citing papers in PubMed.

  1. Article
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  3. Article
  4. Article
  5. Review
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  9. Article
  10. Protein Binding: A Fuzzy Concept.Life (Basel, Switzerland) · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Effective concentrations enforced by intrinsically disordered linkers are governed by polymer physics.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  20. 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

4 authors.

Maodong LiCenter for Quantitative Biology, Peking University, Beijing, 100871, China.
Huaiqing CaoCollege of Chemistry and Molecular Engineering, Peking University, Beijing, 100871, China.
Luhua LaiCenter for Quantitative Biology, Peking University, Beijing, 100871, China.
Zhirong LiuCenter for Quantitative Biology, Peking University, Beijing, 100871, China.

Funding

Ministry of Science and Technology of the People's Republic of China 2015CB910300National Natural Science Foundation of China 21633001
6 · The paper itself

Abstract

There are many multidomain allosteric proteins where an allosteric signal at the allosteric domain modifies the activity of the functional domain. Intrinsically disordered regions (linkers) are widely involved in this kind of regulation process, but the essential role they play therein is not well understood. Here, we investigated the effect of linkers in stabilizing the open or the closed states of multidomain proteins using combined thermodynamic deduction and coarse-grained molecular dynamics simulations. We revealed that the influence of linker can be fully characterized by an effective local concentration [B]

Indexed as

Molecular Dynamics SimulationThermodynamicsAllosteric RegulationProtein ConformationProteinsProteinscoarse-grained molecular dynamics simulationdisordered linkerslocal concentrationmultidomain protein

Identifiers

PMID30019371
PMCPMC6194284

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.