Evidence map›Paper›PMID 21931164›Full record

ArticleThe Journal of biological chemistry2011

The cystic fibrosis transmembrane conductance regulator (CFTR): three-dimensional structure and localization of a channel gate.

Mark F Rosenberg, Liam P O'Ryan, Guy Hughes, Zhefeng Zhao, Luba A Aleksandrov, John R Riordan, Robert C Ford

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing 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

32 citing papers in PubMed.

  1. Article
  2. Review
  3. NM23 proteins: innocent bystanders or local energy boosters for CFTR?Laboratory investigation; a journal of technical methods and pathology · 2018
    Review
  4. The biophysics, biochemistry and physiology of CFTR.Cellular and molecular life sciences : CMLS · 2017
    Review
  5. Architecture and functional properties of the CFTR channel pore.Cellular and molecular life sciences : CMLS · 2017
    Review
  6. Article
  7. Molecular modelling and molecular dynamics of CFTR.Cellular and molecular life sciences : CMLS · 2017
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

7 authors.

Mark F RosenbergFaculty of Life Sciences, University of Manchester, Manchester Interdisciplinary Biocentre, Manchester M1 7DN, United Kingdom.
Liam P O'RyanFaculty of Life Sciences, University of Manchester, Manchester Interdisciplinary Biocentre, Manchester M1 7DN, United Kingdom.
Guy HughesFaculty of Life Sciences, University of Manchester, Manchester Interdisciplinary Biocentre, Manchester M1 7DN, United Kingdom.
Zhefeng ZhaoDepartment of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599.
Luba A AleksandrovDepartment of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599.
John R RiordanDepartment of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, North Carolina 27599.
Robert C FordFaculty of Life Sciences, University of Manchester, Manchester Interdisciplinary Biocentre, Manchester M1 7DN, United Kingdom. Electronic address: robert.ford@manchester.ac.uk.

Funding

MOLECULAR MECHANISMS OF CFTR FUNCTIONR01DK051619 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI RIORDAN, JOHN R · 1997 to 2013
$3.0M
NIDDK NIH HHS DK051619NIDDK NIH HHS R01 DK051619
6 · The paper itself

Abstract

Cystic fibrosis affects about 1 in 2500 live births and involves loss of transmembrane chloride flux due to a lack of a membrane protein channel termed the cystic fibrosis transmembrane conductance regulator (CFTR). We have studied CFTR structure by electron crystallography. The data were compared with existing structures of other ATP-binding cassette transporters. The protein was crystallized in the outward facing state and resembled the well characterized Sav1866 transporter. We identified regions in the CFTR map, not accounted for by Sav1866, which were potential locations for the regulatory region as well as the channel gate. In this analysis, we were aided by the fact that the unit cell was composed of two molecules not related by crystallographic symmetry. We also identified regions in the fitted Sav1866 model that were missing from the map, hence regions that were either disordered in CFTR or differently organized compared with Sav1866. Apart from the N and C termini, this indicated that in CFTR, the cytoplasmic end of transmembrane helix 5/11 and its associated loop could be partly disordered (or alternatively located).

Indexed as

Adenosine TriphosphateBiological TransportCell MembraneChromatography, AffinityCrystallizationCrystallography, X-RayCystic Fibrosis Transmembrane Conductance RegulatorHumansIonsMicroscopy, ElectronModels, MolecularMolecular ConformationPhosphorylationProtein ConformationProteinsProtein Structure, SecondaryAdenosine TriphosphateCFTR protein, humanCystic Fibrosis Transmembrane Conductance RegulatorIonsProteins

Identifiers

PMID21931164
PMCPMC3234965

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.