Evidence map›Paper›PMID 38151801›Full record

ArticleProtein science : a publication of the Protein Society2024

Engineering highly stable variants of Corynactis californica green fluorescent proteins.

Li-Wei Hung, Thomas C Terwilliger, Geoffrey S Waldo, Hau B Nguyen

Open access · hybridAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 31% 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

4 citing papers in PubMed, 3 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Engineering highly stable variants of Corynactis californica green fluorescent proteins.Protein science : a publication of the Protein Society · 2024
    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

4 authors at 1 institution in 1 country.

Li-Wei HungBioscience Division, MS M888, Los Alamos National Laboratory, Los Alamos, New Mexico, USA.
Thomas C TerwilligerBioscience Division, MS M888, Los Alamos National Laboratory, Los Alamos, New Mexico, USA.
Geoffrey S WaldoBioscience Division, MS M888, Los Alamos National Laboratory, Los Alamos, New Mexico, USA.
Hau B NguyenBioscience Division, MS M888, Los Alamos National Laboratory, Los Alamos, New Mexico, USA.ORCID 0000-0003-0174-9622
Los Alamos National Laboratory · US

Funding

User Training and OutreachP30GM124169 · NIGMS · UNIVERSITY OF CALIF-LAWRENC BERKELEY LAB · PI James M Holton · 2017 to 2026
$28.6M
Proj 3: Enhancing crystallization by supplying natural binding partnersP01GM098177 · NIGMS · LOS ALAMOS NAT SECTY-LOS ALAMOS NAT LAB · PI BRADBURY, ANDREW · 2012 to 2015
$4.7M
NIGMS NIH HHS P01 GM098177NIGMS NIH HHS P30 GM124169NIH HHS
6 · The paper itself

Abstract

Fluorescent proteins (FPs) are versatile biomarkers that facilitate effective detection and tracking of macromolecules of interest in real time. Engineered FPs such as superfolder green fluorescent protein (sfGFP) and superfolder Cherry (sfCherry) have exceptional refolding capability capable of delivering fluorescent readout in harsh environments where most proteins lose their native functions. Our recent work on the development of a split FP from a species of strawberry anemone, Corynactis californica, delivered pairs of fragments with up to threefold faster complementation than split GFP. We present the biophysical, biochemical, and structural characteristics of five full-length variants derived from these split C. californica GFP (ccGFP). These ccGFP variants are more tolerant under chemical denaturation with up to 8 kcal/mol lower unfolding free energy than that of the sfGFP. It is likely that some of these ccGFP variants could be suitable as biomarkers under more adverse environments where sfGFP fails to survive. A structural analysis suggests explanations of the variations in stabilities among the ccGFP variants.

Indexed as

Green Fluorescent ProteinsBiomarkersBiomarkersGreen Fluorescent Proteinsdenaturationgreen fluorescent proteinprotein detectionprotein expressionprotein fragment complementationprotein stabilityprotein taggingsolubilitystable

Identifiers

PMID38151801
PMCPMC10804665
OpenAlexW4390342156

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.