Evidence map›Paper›PMID 25534273›Full record

ArticleJournal of the American Chemical Society2015

"Turn-on" protein fluorescence: in situ formation of cyanine dyes.

Ipek Yapici, Kin Sing Stephen Lee, Tetyana Berbasova, Meisam Nosrati, Xiaofei Jia, Chrysoula Vasileiou, Wenjing Wang, Elizabeth M Santos, James H Geiger, Babak Borhan

Open access · bronzeAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

31 citing papers in PubMed, 71 citations in OpenAlex.

  1. De Novo Design of Near-Infrared Fluorescence-Activating Proteins.Journal of the American Chemical Society · 2026
    Article
  2. Photoisomerization detected in a fully wavelength-tunable rhodopsin mimic system.Acta crystallographica. Section D, Structural biology · 2026
    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. Article
  5. Article
  6. Article
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  9. Article
  10. Review
  11. Article
  12. Genetically Encoded Activators of Small Molecules for Imaging and Drug Delivery.Angewandte Chemie (International ed. in English) · 2020
    Review
  13. Engineering of a Red Fluorogenic Protein/Merocyanine Complex for Live-Cell Imaging.Chembiochem : a European journal of chemical biology · 2020
    Article
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Mimicking Microbial Rhodopsin Isomerization in a Single Crystal.Journal of the American Chemical Society · 2019
    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

10 authors at 1 institution in 1 country.

Ipek YapiciDepartment of Chemistry, Michigan State University , East Lansing, Michigan 48824, United States.
Kin Sing Stephen Lee
Tetyana Berbasova
Meisam Nosrati
Xiaofei Jia
Chrysoula Vasileiou
Wenjing Wang
Elizabeth M Santos
James H Geiger
Babak Borhan
Michigan State University · US

Funding

Protein/Chromphore Interactions via Protein Design: Interrogation and ApplicationR01GM101353 · NIGMS · MICHIGAN STATE UNIVERSITY · PI BORHAN, BABAK, GEIGER, JAMES H · 2013 to 2022
$2.6M
Identifying the Receptors of Environmentally Sensitive Epoxy-Eicosanoids with AMSK99ES024806 · NIEHS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI LEE, KIN SING STEPHEN · 2015 to 2016
$132k
NIEHS NIH HHS K99 ES024806NIGMS NIH HHS GM101353NIGMS NIH HHS R01 GM101353
6 · The paper itself

Abstract

Protein reengineering of cellular retinoic acid binding protein II (CRABPII) has yielded a genetically addressable system, capable of binding a profluorophoric chromophore that results in fluorescent protein/chromophore complexes. These complexes exhibit far-red emission, with high quantum efficiencies and brightness and also exhibit excellent pH stability spanning the range of 2-11. In the course of this study, it became evident that single mutations of L121E and R59W were most effective in improving the fluorescent characteristics of CRABPII mutants as well as the kinetics of complex formation. The readily crystallizable nature of these proteins was invaluable to provide clues for the observed spectroscopic behavior that results from single mutation of key residues.

Indexed as

FluorescenceCarbocyaninesColoring AgentsHydrogen-Ion ConcentrationModels, MolecularMolecular StructureReceptors, Retinoic AcidCarbocyaninesColoring AgentsReceptors, Retinoic Acidretinoic acid binding protein II, cellular

Identifiers

PMID25534273
PMCPMC4311949
OpenAlexW2049961683

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.