Evidence map›Paper›PMID 39466685›Full record

ArticleeLife2024

A synthetic method to assay polycystin channel biophysics.

Megan Larmore, Orhi Esarte Palomero, Neha Kamat, Paul G DeCaen

Abstract read
In one paragraph

Article in eLife, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing 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

3 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors.

Megan LarmoreDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, United States.
Orhi Esarte PalomeroDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, United States.ORCID https://orcid.org/0000-0003-2022-3140
Neha KamatDepartment of Biomedical Engineering, McCormick School of Engineering and Applied Science, Northwestern University, Evanston, United States.ORCID https://orcid.org/0000-0001-9362-6106
Paul G DeCaenDepartment of Pharmacology, Feinberg School of Medicine, Northwestern University, Chicago, United States.ORCID https://orcid.org/0000-0001-8776-983X

Funding

Molecular Biophysics Training Program at Northwestern UniversityT32GM008382 · NIGMS · NORTHWESTERN UNIVERSITY · PI RADHAKRISHNAN, ISHWAR · 1990 to 2020
$4.3M
Training Core for Chicago KUH FORWARDTL1DK132769 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Tamara Isakova · 2021 to 2026
$4.0M
Professional Development Core for Chicago KUH FORWARDU2CDK129917 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Nicolae Valentin David · 2021 to 2026
$2.9M
Molecular Biophysics Training Program at Northwestern UniversityT32GM140995 · NIGMS · NORTHWESTERN UNIVERSITY · PI Heather Wendy Pinkett, Reza Vafabakhsh · 2021 to 2026
$2.5M
Molecular dysregulation of primary cilia TRPP2 channels caused by Finger 1 variantsR01DK123463 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI DECAEN, PAUL GREGORY · 2019 to 2023
$2.0M
Cilia calcium dysregulation in polycystic kidney diseaseR01DK131118 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI Paul Gregory DeCaen · 2022 to 2026
$1.9M
Polycystin glycosylation regulation and dysregulation in ADPKDF32DK137477 · NIDDK · NORTHWESTERN UNIVERSITY AT CHICAGO · PI ESARTE PALOMERO, ORHI · 2024 to 2024
$77k
NIDDK NIH HHS F32 DK137477NIDDK NIH HHS F32DK137477-01A1NIDDK NIH HHS R01 DK123463NIDDK NIH HHS R01 DK123463-01NIDDK NIH HHS R01 DK131118NIDDK NIH HHS R01 DK131118-01NIDDK NIH HHS TL1 DK132769NIDDK NIH HHS U2C DK129917NIGMS NIH HHS T32 GM008382NIGMS NIH HHS T32 GM140995NIH HHS T32 GM008382NIH HHS TL1DK132769NIH HHS U2CDK129917
6 · The paper itself

Abstract

Ion channels are biological transistors that control ionic flux across cell membranes to regulate electrical transmission and signal transduction. They are found in all biological membranes and their conductive state kinetics are frequently disrupted in human diseases. Organelle ion channels are among the most resistant to functional and pharmacological interrogation. Traditional channel protein reconstitution methods rely upon exogenous expression and/or purification from endogenous cellular sources which are frequently contaminated by resident ionophores. Here, we describe a fully synthetic method to assay functional properties of polycystin channels that natively traffic to primary cilia and endoplasmic reticulum organelles. Using this method, we characterize their oligomeric assembly, membrane integration, orientation, and conductance while comparing these results to their endogenous channel properties. Outcomes define a novel synthetic approach that can be applied broadly to investigate channels resistant to biophysical analysis and pharmacological characterization.

Indexed as

TRPP Cation ChannelsAnimalsBiophysical PhenomenaBiophysicsCiliaEndoplasmic ReticulumHEK293 CellsHumansTRPP Cation ChannelsADPKDbiochemistrybiophysicschemical biologyion channelsnonePKDpolycystinssynthetic biology

Identifiers

PMID39466685
PMCPMC11517255

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Registered trials

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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.