Evidence map›Paper›PMID 23826884›Full record

ReviewThe FEBS journal2013

Structural changes of CFTR R region upon phosphorylation: a plastic platform for intramolecular and intermolecular interactions.

Zoltan Bozoky, Mickael Krzeminski, P Andrew Chong, Julie D Forman-Kay

Open access · hybridAbstract readReview
In one paragraph

Review in The FEBS journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
6.2field-weighted citation impact, top 3% 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

24 citing papers in PubMed, 56 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Molecular modelling and molecular dynamics of CFTR.Cellular and molecular life sciences : CMLS · 2017
    Review
  13. Finding Our Way in the Dark Proteome.Journal of the American Chemical Society · 2016
    Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Regulation of the cystic fibrosis transmembrane conductance regulator anion channel by tyrosine phosphorylation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015
    Article
  19. 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 at 2 institutions in 1 country.

Zoltan BozokyProgram in Molecular Structure and Function, Hospital for Sick Children, Toronto, Ontario, Canada.
Mickael Krzeminski
P Andrew Chong
Julie D Forman-Kay
Hospital for Sick Children · CAUniversity of Toronto · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chloride channel gating and trafficking of the cystic fibrosis transmembrane conductance regulator (CFTR) are regulated by phosphorylation. Intrinsically disordered segments of the protein are responsible for phospho-regulation, particularly the regulatory (R) region that is a target for several kinases and phosphatases. The R region remains disordered following phosphorylation, with different phosphorylation states sampling various conformations. Recent studies have demonstrated the crucial role that intramolecular and intermolecular interactions of the R region play in CFTR regulation. Different partners compete for the same binding segment, with the R region containing multiple overlapping binding elements. The non-phosphorylated R region interacts with the nucleotide binding domains and inhibits channel activity by blocking heterodimerization. Phosphorylation shifts the equilibrium such that the R region is excluded from the dimer interface, facilitating gating and processing by stimulating R region interactions with other domains and proteins. The dynamic conformational sampling and transient binding of the R region to multiple partners enables complex control of CFTR channel activity and trafficking.

Indexed as

Protein Processing, Post-TranslationalBinding SitesCystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorHumansModels, MolecularPhosphorylationProtein BindingProtein FoldingProtein Interaction Domains and MotifsProtein MultimerizationProtein TransportSignal TransductionCFTR protein, humanCystic Fibrosis Transmembrane Conductance RegulatorbindingdisorderedhubIDPpost-translational modificationregulation

Identifiers

PMID23826884
PMCPMC4160016
OpenAlexW1973541009

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.