Evidence map›Paper›PMID 38478271›Full record

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

Fluorescent Labeling of Outer Membrane Proteins Using the SpyCatcher-SpyTag System.

Rachael Duodu, Dirk Linke, Jack C Leo

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 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
4.5field-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

1 citing paper in PubMed, 3 citations in OpenAlex.

  1. Article
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

3 authors at 2 institutions in 2 countries.

Rachael DuoduAntimicrobial Resistance, Omics and Microbiota Group, Department of Biosciences, Nottingham Trent University, Nottingham, UK.
Dirk LinkeSection for Evolution and Genetics, Department of Biosciences, University of Oslo, Oslo, Norway.
Jack C LeoAntimicrobial Resistance, Omics and Microbiota Group, Department of Biosciences, Nottingham Trent University, Nottingham, UK. jack.leo@ntu.ac.uk.
Nottingham Trent University · GBUniversity of Oslo · NO

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The SpyCatcher-SpyTag system has become a popular and versatile tool for protein ligation. It is based on a small globular protein (SpyCatcher) that binds to a 13-residue peptide (SpyTag), which subsequently leads to the formation of a covalent isopeptide bond. Thus, the reaction is essentially irreversible. Here, we describe how the SpyCatcher-SpyTag system can be used to label surface-exposed bacterial outer membrane proteins, e.g., for topology mapping or fluorescent time-course experiments. We cover using fluorescence measurements and microscopy to measure labeling efficiency using SpyCatcher fused with superfolder GFP in this chapter.

Indexed as

Membrane ProteinsPeptidesColoring AgentsColoring AgentsMembrane ProteinsPeptidesFluorescent labelingOuter membrane proteinProtein ligationSpyCatcherSpyTagTopology mapping

Identifiers

PMID38478271
OpenAlexW4392775361

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.