Evidence map›Paper›PMID 37916770›Full record

ArticleNano letters2023

Imaging Proteins Sensitive to Direct Fusions Using Transient Peptide-Peptide Interactions.

Zoe Gidden, Curran Oi, Emily J Johnston, Zuzanna Konieczna, Haresh Bhaskar, Lorena Mendive-Tapia, Fabio de Moliner, Susan J Rosser, Simon G J Mochrie, Marc Vendrell and 2 more

Open access · hybridAbstract read
In one paragraph

Article in Nano letters, 2023. 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
2.1field-weighted citation impact, top 11% 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

3 citing papers in PubMed, 6 citations in OpenAlex.

  1. Review
  2. Article
  3. Experimental Approaches to Visualize Effector Protein Translocation During Host-Pathogen Interactions.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    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

12 authors at 4 institutions in 2 countries.

Zoe GiddenSchool of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3DW, U.K.
Curran OiDepartment of Genome Sciences, University of Washington, Seattle, Washington 98195, United States.
Emily J JohnstonSchool of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3DW, U.K.
Zuzanna KoniecznaEaStCHEM School of Chemistry, The University of Edinburgh, Edinburgh, EH9 3FJ, U.K.
Haresh BhaskarSchool of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3DW, U.K.
Lorena Mendive-TapiaIRR Chemistry Hub, Institute for Regeneration and Repair, The University of Edinburgh, Edinburgh, EH16 4UU, U.K.
Fabio de MolinerIRR Chemistry Hub, Institute for Regeneration and Repair, The University of Edinburgh, Edinburgh, EH16 4UU, U.K.
Susan J RosserSchool of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3DW, U.K.ORCID 0000-0002-2560-6485
Simon G J MochrieDepartment of Physics, Yale University, New Haven, Connecticut 06520, United States.
Marc VendrellIRR Chemistry Hub, Institute for Regeneration and Repair, The University of Edinburgh, Edinburgh, EH16 4UU, U.K.
Mathew H HorrocksEaStCHEM School of Chemistry, The University of Edinburgh, Edinburgh, EH9 3FJ, U.K.ORCID 0000-0001-5495-5492
Lynne ReganSchool of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3DW, U.K.
MRC Centre for Regenerative Medicine · GBUniversity of Edinburgh · GBYale University · USUniversity of Washington · US

Funding

Designed proteins to study and modulate cellular processesR01GM118528 · NIGMS · YALE UNIVERSITY · PI MOCHRIE, SIMON · 2017 to 2020
$1.2M
NIGMS NIH HHS R01 GM118528Wellcome Trust
6 · The paper itself

Abstract

Fluorescence microscopy enables specific visualization of proteins in living cells and has played an important role in our understanding of the protein subcellular location and function. Some proteins, however, show altered localization or function when labeled using direct fusions to fluorescent proteins, making them difficult to study in live cells. Additionally, the resolution of fluorescence microscopy is limited to ∼200 nm, which is 2 orders of magnitude larger than the size of most proteins. To circumvent these challenges, we previously developed LIVE-PAINT, a live-cell super-resolution approach that takes advantage of short interacting peptides to transiently bind a fluorescent protein to the protein-of-interest. Here, we successfully use LIVE-PAINT to image yeast membrane proteins that do not tolerate the direct fusion of a fluorescent protein by using peptide tags as short as 5-residues. We also demonstrate that it is possible to resolve multiple proteins at the nanoscale concurrently using orthogonal peptide interaction pairs.

Indexed as

PeptidesProteinsDiagnostic ImagingFluorescent DyesSaccharomyces cerevisiaeFluorescent DyesPeptidesProteinslive-cell imagingLIVE-PAINTmembrane proteinprotein−protein interactionsuper-resolution microscopyyeast

Identifiers

PMID37916770
PMCPMC10683072
OpenAlexW4388232738

What OpenQuestion 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 OpenQuestion graph.