Evidence map›Paper›PMID 12020354›Full record

ArticleThe Biochemical journal2002

Functional analysis of the C-terminal boundary of the second nucleotide binding domain of the cystic fibrosis transmembrane conductance regulator and structural implications.

Martina Gentzsch, Andrei Aleksandrov, Luba Aleksandrov, John R Riordan

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
3.1field-weighted citation impact, top 9% 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

15 citing papers in PubMed, 30 citations in OpenAlex.

  1. Systematic deletion of symmetricalNAR molecular medicine · 2024
    Article
  2. Open reading frame correction using splice-switching antisense oligonucleotides for the treatment of cystic fibrosis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  3. Article
  4. Article
  5. Review
  6. A sequence upstream of canonical PDZ-binding motif within CFTR COOH-terminus enhances NHERF1 interaction.American journal of physiology. Lung cellular and molecular physiology · 2016
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Endocytic trafficking of CFTR in health and disease.Journal of cystic fibrosis : official journal of the European Cystic Fibrosis Society · 2007
    Review
  12. Article
  13. Article
  14. Article
  15. 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 1 institution in 1 country.

Martina GentzschMayo Foundation and Mayo Clinic Scottsdale, S. C. Johnson Medical Research Center, 13400 E. Shea Blvd., Scottsdale, AZ 85259, USA.
Andrei Aleksandrov
Luba Aleksandrov
John R Riordan
Mayo Clinic in Arizona · US

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 DK51619
6 · The paper itself

Abstract

The cystic fibrosis transmembrane conductance regulator (CFTR) contains two nucleotide-binding domains (NBDs) or ATP-binding cassettes (ABCs) that characterize a large family of membrane transporters. Although the three-dimensional structures of these domains from several ABC proteins have been determined, this is not the case for CFTR, and hence the domains are defined simply on the basis of sequence alignment. The functional C-terminal boundary of NBD1 of CFTR was located by analysis of chloride channel function [Chan, Csanady, Seto-Young, Nairn and Gadsby (2000) J. Gen. Physiol. 116, 163-180]. However, the boundary between the C-terminal end of NBD2 and sequences further downstream in the whole protein, that are important for its cellular localization and endocytotic turnover, has not been defined. We have now done this by assaying the influence of progressive C-terminal truncations on photolabelling of NBD2 by 8-azido-ATP, which reflects hydrolysis, as well as binding, at that domain, and on NBD2-dependent channel gating itself. The boundary defined in this way is between residues 1420 and 1424, which corresponds to the final beta-strand in aligned NBDs whose structures have been determined. Utilization of this information should facilitate the generation of monodisperse NBD2 polypeptides for structural analysis, which until now has not been possible. The established boundary includes within NBD2 a hydrophobic patch of four residues (1413-1416) previously shown to be essential for CFTR maturation and stability [Gentzsch and Riordan (2001) J. Biol. Chem. 276, 1291-1298]. This hydrophobic cluster is conserved in most ABC proteins, and on alignment with ones of known structure constitutes the penultimate beta-strand of the domain which is likely to participate in essential structure-stabilizing beta-sheet formation.

Indexed as

Adenosine TriphosphateAffinity LabelsAmino Acid SequenceAnimalsAzidesBinding SitesCell LineChloride ChannelsCricetinaeCystic Fibrosis Transmembrane Conductance RegulatorKidneyMicrosomesModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedNucleotides8-azidoadenosine 5'-triphosphateAdenosine TriphosphateAffinity LabelsAzidesChloride ChannelsCystic Fibrosis Transmembrane Conductance RegulatorNucleotidesRecombinant Proteins

Identifiers

PMID12020354
PMCPMC1222794
OpenAlexW1979869569

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.