Evidence map›Paper›PMID 37071053›Full record

ArticleCurrent protocols2023

Fluorescent Protein Production, Purification, and Coupling to Microspheres.

Marija Dramicanin, Kevin Lim, Simon Monard

Open access · hybridAbstract read
In one paragraph

Article in Current protocols, 2023. 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
0.7field-weighted citation impact, top 19% 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. 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 1 country.

Marija DramicaninWalter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.
Kevin LimWalter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.
Simon MonardWalter and Eliza Hall Institute of Medical Research, Parkville, Victoria, Australia.
Walter and Eliza Hall Institute of Medical Research · AUThe University of Melbourne · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fluorescent proteins (FPs) have become an essential tool for biological research. Since the isolation and description of green FP, hundreds of FPs have been discovered and created with various characteristics. The excitation of these proteins ranges from ultraviolet (UV) up to near infrared (NIR). Using conventional cytometry, with each detector assigned to a fluorochrome, great care must be taken when selecting the optimal bandpass filters to minimalize the spectral overlap as the emission spectra of FPs are broad. Full-spectrum flow cytometers eliminate the need to change optical filters for analyzing FPs, which simplifies instrument setup. In experiments where more than one FP is used, single-color controls are required. These can be cells expressing each of the proteins separately. In the case of the confetti system, for instance, when four FPs are used, all these proteins will need to be expressed separately so that compensation or spectral unmixing can be performed, and this can be inconvenient and expensive. An appealing alternative is to produce FPs in Escherichia coli, purify them, and covalently couple them to carboxylate polystyrene microspheres. Such microspheres are ready to use and can be stored at 4°C for months or even years without any deterioration in fluorescence. The same procedure can be used to couple antibodies or other proteins to these particles. Here, we describe how to express and purify FPs, how to couple them to microspheres, and how to evaluate the fluorescent properties of the particles. © 2023 The Authors. Current Protocols published by Wiley Periodicals LLC. Basic Protocol 1: Escherichia coli expression and purification of recombinant mPlum Basic Protocol 2: Coupling fluorescent proteins to polystyrene microspheres Support Protocol 1: Comparing the cell-bound and bead-bound fluorescence signatures Support Protocol 2: Comparing spectral signatures via the similarity index, complexity matrix, and spillover spread matrix of fluorescent protein-coupled beads.

Indexed as

Fluorescent DyesPolystyrenesFluorescenceLuminescent ProteinsMicrospheresFluorescent DyesLuminescent ProteinsPolystyrenesfluorescent proteinsfull-spectrum cytometrymicrospheresprotein expressionprotein purification

Identifiers

PMID37071053
PMCPMC13528252
OpenAlexW4366234881

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.