Evidence map›Paper›PMID 23819615›Full record

ArticleJournal of the American Chemical Society2013

GFP variants with alternative β-strands and their application as light-driven protease sensors: a tale of two tails.

Keunbong Do, Steven G Boxer

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed, 27 citations in OpenAlex.

  1. Structure Prediction of Alternate Frame Folding Systems with AlphaFold3.Journal of chemical information and modeling · 2025
    Article
  2. Seesaw protein: Design of a protein that adopts interconvertible alternative functional conformations and its dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Article
  4. Engineering highly stable variants of Corynactis californica green fluorescent proteins.Protein science : a publication of the Protein Society · 2024
    Article
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  12. Review
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  15. Mechanically switching single-molecule fluorescence of GFP by unfolding and refolding.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  16. Mechanism and bottlenecks in strand photodissociation of split green fluorescent proteins (GFPs).Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Review
  18. 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

2 authors at 1 institution in 1 country.

Keunbong DoDepartment of Chemistry, Stanford University, Stanford, California 94305-5012, United States. kbd0810@gmail.com
Steven G Boxer
Stanford University · US

Funding

NMR &CIDNP STUDIES OF MB MUTANTS &OLIGONUCLEOTIDE LOOPR01GM027738 · NIGMS · STANFORD UNIVERSITY · PI BOXER, STEVEN G. · 1985 to 2016
$4.3M
ELECTROSTATICS AND DYNAMICS IN MYOGLOBIN MUTANTSR37GM027738 · NIGMS · STANFORD UNIVERSITY · PI BOXER, STEVEN G. · 1994 to 2003
$1.2M
NIGMS NIH HHS GM27738NIGMS NIH HHS R01 GM027738NIGMS NIH HHS R37 GM027738
6 · The paper itself

Abstract

Green fluorescent protein (GFP) variants that carry one extra strand 10 (s10) were created and characterized, and their possible applications were explored. These proteins can fold with either one or the other s10, and the ratio of the two folded forms, unambiguously distinguished by their resulting colors, can be systematically modulated by mutating the residues on s10 or by changing the lengths of the two inserted linker sequences that connect each s10 to the rest of the protein. We have discovered robust empirical rules that accurately predict the product ratios of any given construct in both bacterial and mammalian expressions. Exploiting earlier studies on photodissociation of cut s10 from GFP (Do and Boxer, 2011), ratiometric protease sensors were designed from the construct by engineering a specific protease cleavage site into one of the inserted loops, where the bound s10 is replaced by the other strand upon protease cleavage and irradiation with light to switch its color. Since the conversion involves a large spectral shift, these genetically encoded sensors display a very high dynamic range. Further engineering of this class of proteins guided by mechanistic understanding of the light-driven process will enable interesting and useful application of the protein.

Indexed as

LightGreen Fluorescent ProteinsPeptide HydrolasesGreen Fluorescent ProteinsPeptide Hydrolases

Identifiers

PMID23819615
PMCPMC3756597
OpenAlexW2116524422

What OpenQuestion holds

Textmetadata
LicenceTDM
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.