Evidence map›Paper›PMID 28944753›Full record

ArticleeLife2017

Asymmetry of movements in CFTR's two ATP sites during pore opening serves their distinct functions.

Ben Sorum, Beáta Töröcsik, László Csanády

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

17 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. CFTR Modulators: From Mechanism to Targeted Therapeutics.Handbook of experimental pharmacology · 2024
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Physiological and pharmacological characterization of the N1303K mutant CFTR.Journal of cystic fibrosis : official journal of the European Cystic Fibrosis Society · 2018
    Article
  15. Article
  16. Article
  17. Structural mechanisms of CFTR function and dysfunction.The Journal of general physiology · 2018
    Review
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 1 institution in 1 country.

Ben SorumDepartment of Medical Biochemistry, Semmelweis University, Budapest, Hungary.ORCID http://orcid.org/0000-0001-6742-1094
Beáta TöröcsikDepartment of Medical Biochemistry, Semmelweis University, Budapest, Hungary.
László CsanádyDepartment of Medical Biochemistry, Semmelweis University, Budapest, Hungary.ORCID http://orcid.org/0000-0002-6547-5889
Semmelweis University · HU

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

CFTR, the chloride channel mutated in cystic fibrosis (CF) patients, is opened by ATP binding to two cytosolic nucleotide binding domains (NBDs), but pore-domain mutations may also impair gating. ATP-bound NBDs dimerize occluding two nucleotides at interfacial binding sites; one site hydrolyzes ATP, the other is inactive. The pore opens upon tightening, and closes upon disengagement, of the catalytic site following ATP hydrolysis. Extent, timing, and role of non-catalytic-site movements are unknown. Here we exploit equilibrium gating of a hydrolysis-deficient mutant and apply Φ value analysis to compare timing of opening-associated movements at multiple locations, from the cytoplasmic ATP sites to the extracellular surface. Marked asynchrony of motion in the two ATP sites reveals their distinct roles in channel gating. The results clarify the molecular mechanisms of functional cross-talk between canonical and degenerate ATP sites in asymmetric ABC proteins, and of the gating defects caused by two common CF mutations.

Indexed as

Protein MultimerizationAdenosine TriphosphateAnimalsCystic Fibrosis Transmembrane Conductance RegulatorHumansHydrolysisOocytesPatch-Clamp TechniquesProtein BindingProtein ConformationXenopus laevisAdenosine TriphosphateCFTR protein, humanCystic Fibrosis Transmembrane Conductance Regulatorasymmetric ABC proteinbiophysicscystic fibrosisdeltaF508E. coliR117HREFERstructural biologyxenopus

Identifiers

PMID28944753
PMCPMC5626490
OpenAlexW2758229051

What OpenQuestion holds

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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.