Evidence map›Paper›PMID 15619636›Full record

ArticleNature structural & molecular biology2005

Side chain and backbone contributions of Phe508 to CFTR folding.

Patrick H Thibodeau, Chad A Brautigam, Mischa Machius, Philip J Thomas

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing 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

92 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Nanomechanics combined with HDX reveals allosteric drug binding sites of CFTR NBD1.Computational and structural biotechnology journal · 2022
    Article
  6. Article
  7. Recent Strategic Advances in CFTR Drug Discovery: An Overview.International journal of molecular sciences · 2020
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Structural mechanisms of CFTR function and dysfunction.The Journal of general physiology · 2018
    Review
  18. Article
  19. A common mechanism for CFTR potentiators.The Journal of general physiology · 2017
    Article
  20. Article

32 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Patrick H ThibodeauDepartment of Physiology, The University of Texas Southwestern Medical Center at Dallas, 75390 USA.
Chad A Brautigam
Mischa Machius
Philip J Thomas

Funding

MECHANISMS OF DRUG ACTION AND DISPOSITIONT32GM007062 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MANGELSDORF, DAVID J · 1985 to 2020
$7.4M
DEVELOPMENT OF MEMBRANE PROTEIN STRUCTURER37DK049835 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI THOMAS, PHILIP J · 2008 to 2017
$3.6M
Development of Membrane Protein StructureR01DK049835 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI THOMAS, PHILIP J · 1996 to 2007
$2.1M
NIDDK NIH HHS DK49835NIDDK NIH HHS R01 DK049835NIDDK NIH HHS R37 DK049835NIGMS NIH HHS GM07062NIGMS NIH HHS T32 GM007062
6 · The paper itself

Abstract

Mutations in the cystic fibrosis transmembrane conductance regulator (CFTR), an integral membrane protein, cause cystic fibrosis (CF). The most common CF-causing mutant, deletion of Phe508, fails to properly fold. To elucidate the role Phe508 plays in the folding of CFTR, missense mutations at this position were generated. Only one missense mutation had a pronounced effect on the stability and folding of the isolated domain in vitro. In contrast, many substitutions, including those of charged and bulky residues, disrupted folding of full-length CFTR in cells. Structures of two mutant nucleotide-binding domains (NBDs) reveal only local alterations of the surface near position 508. These results suggest that the peptide backbone plays a role in the proper folding of the domain, whereas the side chain plays a role in defining a surface of NBD1 that potentially interacts with other domains during the maturation of intact CFTR.

Indexed as

Protein FoldingAnimalsBinding SitesCell LineCrystallography, X-RayCystic Fibrosis Transmembrane Conductance RegulatorHumansHydrophobic and Hydrophilic InteractionsMiceModels, MolecularMutationPhenylalanineProtein DenaturationProtein Structure, TertiaryTemperatureThermodynamicsCFTR protein, humanCystic Fibrosis Transmembrane Conductance RegulatorPhenylalanine

Identifiers

PMID15619636
PMCPMC3516198

What OpenQuestion holds

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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.