Evidence map›Paper›PMID 34947992›Full record

ReviewInternational journal of molecular sciences2021

Revisiting CFTR Interactions: Old Partners and New Players.

Carlos M Farinha, Martina Gentzsch

Open access · goldAbstract readReview
In one paragraph

Review in International journal of molecular sciences, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
2.3field-weighted citation impact, top 10% 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

14 citing papers in PubMed, 1 synthesis or guideline pooled it, 20 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Restoring chloride efflux in cystic fibrosis with TMEM16a antisense oligonucleotides.Molecular therapy : the journal of the American Society of Gene Therapy · 2025
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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

2 authors at 2 institutions in 2 countries.

Carlos M FarinhaBioISI-Biosystems and Integrative Sciences Institute, Faculty of Sciences, University of Lisboa, 1749-016 Lisboa, Portugal.ORCID 0000-0002-5467-1710
Martina GentzschMarsico Lung Institute and Cystic Fibrosis Research Center, School of Medicine, University of North Carolina, Chapel Hill, NC 27599, USA.ORCID 0000-0002-9435-0321
University of Lisbon · PTUniversity of North Carolina at Chapel Hill · US

Funding

Vector CoreP30DK065988 · NIDDK · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Scott H Randell · 2004 to 2026
$26.5M
Cystic Fibrosis Foundation BOUCHE19R0Cystic Fibrosis Foundation FARINH19I0Cystic Fibrosis Foundation GENTZS18P0Cystic Fibrosis Foundation GENTZS19I0Fundação para a Ciência e Tecnologia PTDC/BIA-CEL/28408/2017NIDDK NIH HHS P30 DK065988NIH HHS P30DK065988
6 · The paper itself

Abstract

Remarkable progress in CFTR research has led to the therapeutic development of modulators that rescue the basic defect in cystic fibrosis. There is continuous interest in studying CFTR molecular disease mechanisms as not all cystic fibrosis patients have a therapeutic option available. Addressing the basis of the problem by comprehensively understanding the critical molecular associations of CFTR interactions remains key. With the availability of CFTR modulators, there is interest in comprehending which interactions are critical to rescue CFTR and which are altered by modulators or CFTR mutations. Here, the current knowledge on interactions that govern CFTR folding, processing, and stability is summarized. Furthermore, we describe protein complexes and signal pathways that modulate the CFTR function. Primary epithelial cells display a spatial control of the CFTR interactions and have become a common system for preclinical and personalized medicine studies. Strikingly, the novel roles of CFTR in development and differentiation have been recently uncovered and it has been revealed that specific CFTR gene interactions also play an important role in transcriptional regulation. For a comprehensive understanding of the molecular environment of CFTR, it is important to consider CFTR mutation-dependent interactions as well as factors affecting the CFTR interactome on the cell type, tissue-specific, and transcriptional levels.

Indexed as

Cystic FibrosisCystic Fibrosis Transmembrane Conductance RegulatorHumansMutationPrecision MedicineProtein BindingProtein FoldingProtein StabilitySignal TransductionCFTR protein, humanCystic Fibrosis Transmembrane Conductance RegulatorCFTR interactionsCFTR modulatorschaperonesdegradationfoldingprocessingproteostasisrare mutationtheratypingtranscriptional regulation

Identifiers

PMID34947992
PMCPMC8703571
OpenAlexW4200432183

What Socratic holds

Textmetadata
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 Socratic graph.