Evidence map›Paper›PMID 37856026›Full record

ArticleMethods in molecular biology (Clifton, N.J.)2024

Affinity Purification of Intraflagellar Transport (IFT) Proteins in Mice Using Endogenous Streptavidin/FLAG Tags.

Tina Beyer, Tiago Martins, Jeshmi Jeyabalan Srikaran, Marian Seda, Emma Peskett, Franziska Klose, Katrin Junger, Philip L Beales, Marius Ueffing, Karsten Boldt and 1 more

Abstract read
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In one paragraph

Article in Methods in molecular biology (Clifton, N.J.), 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
3.9field-weighted citation impact, top 7% 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

2 citing papers in PubMed, 2 citations in OpenAlex.

  1. Review
  2. Review
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

11 authors at 3 institutions in 2 countries.

Tina BeyerInstitute for Ophthalmic Research, Center for Ophthalmology, University of Tübingen, Tübingen, Germany.
Tiago MartinsUCL Great Ormond Street Institute of Child Health, University College London, London, UK.
Jeshmi Jeyabalan SrikaranUCL Great Ormond Street Institute of Child Health, University College London, London, UK.
Marian SedaUCL Great Ormond Street Institute of Child Health, University College London, London, UK.
Emma PeskettUCL Great Ormond Street Institute of Child Health, University College London, London, UK.
Franziska KloseInstitute for Ophthalmic Research, Center for Ophthalmology, University of Tübingen, Tübingen, Germany.
Katrin JungerInstitute for Ophthalmic Research, Center for Ophthalmology, University of Tübingen, Tübingen, Germany.
Philip L BealesUCL Great Ormond Street Institute of Child Health, University College London, London, UK.
Marius UeffingInstitute for Ophthalmic Research, Center for Ophthalmology, University of Tübingen, Tübingen, Germany.
Karsten BoldtInstitute for Ophthalmic Research, Center for Ophthalmology, University of Tübingen, Tübingen, Germany.
Dagan JenkinsUCL Great Ormond Street Institute of Child Health, University College London, London, UK. d.jenkins@ucl.ac.uk.
University College London · GBSTZ eyetrial · DEUniversity of Tübingen · DE

Funding

Department of HealthWellcome Trust 210585/Z/18/Z
6 · The paper itself

Abstract

Biological complexity is achieved through elaborate interactions between relatively few individual components. Affinity purification (AP) has allowed these networks of protein-protein interactions that regulate key biological processes to be interrogated systematically. In order to perform these studies at the required scale, easily transfectable immortalized cell lines have typically been used. Gene-editing now affords the systematic creation of isogenic mouse models carrying endogenous tags for affinity proteomics. This may allow protein-protein interactions to be characterized in the appropriate tissue for a particular biological process or disease phenotype under physiological conditions, and for interaction landscapes to be compared across tissues. Here we demonstrate application to intraflagellar transport (IFT) proteins, which are WD40-domain-containing proteins that are essential for the formation and function of all types of cilia. We describe a method to generate mice with an endogenous C-terminal streptavidin/FLAG tag, using Ift80 as an example, and demonstrate the successful implementation of AP in this model. This method can easily be adapted for N- and C-terminal tagging of many other proteins in vivo.

Indexed as

Carrier ProteinsProteinsAnimalsBiological TransportCiliaMiceStreptavidinCarrier ProteinsProteinsStreptavidinAffinity purificationC57Bl6/N miceCas9Gene-editinggRNAMass spectrometryProtein complexStreptavidin/FLAG tag

Identifiers

PMID37856026
OpenAlexW4387764692

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.