Evidence map›Paper›PMID 28533371›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Blue fluorescent amino acid for biological spectroscopy and microscopy.

Mary Rose Hilaire, Ismail A Ahmed, Chun-Wei Lin, Hyunil Jo, William F DeGrado, Feng Gai

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
4.5field-weighted citation impact, top 4% 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

44 citing papers in PubMed, 138 citations in OpenAlex.

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  20. Miniaturized Chemical Tags for Optical Imaging.Angewandte Chemie (International ed. in English) · 2022
    Review
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

6 authors at 3 institutions in 1 country.

Mary Rose HilaireDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104.
Ismail A AhmedDepartment of Biochemistry and Molecular Biophysics, University of Pennsylvania, Philadelphia, PA 19104.
Chun-Wei LinDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104.
Hyunil JoDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94158.
William F DeGradoDepartment of Pharmaceutical Chemistry, University of California, San Francisco, CA 94158; william.degrado@ucsf.edu gai@sas.upenn.edu.
Feng GaiDepartment of Chemistry, University of Pennsylvania, Philadelphia, PA 19104; william.degrado@ucsf.edu gai@sas.upenn.edu.
University of Pennsylvania · USUniversity of California, San Francisco · USOptica · US

Funding

Multidisciplinary Training in Cardiovascular BiologyT32HL007954 · NHLBI · UNIVERSITY OF PENNSYLVANIA · PI DAVIES, PETER FRANCIS · 2000 to 2019
$9.9M
ULTRAFAST OPTICAL PROCESSES LABORATORYP41GM104605 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI GAI, FENG · 2012 to 2017
$5.6M
De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
NHLBI NIH HHS T32 HL007954NIGMS NIH HHS P41 GM104605NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R37 GM054616
6 · The paper itself

Abstract

Many fluorescent proteins are currently available for biological spectroscopy and imaging measurements, allowing a wide range of biochemical and biophysical processes and interactions to be studied at various length scales. However, in applications where a small fluorescence reporter is required or desirable, the choice of fluorophores is rather limited. As such, continued effort has been devoted to the development of amino acid-based fluorophores that do not require a specific environment and additional time to mature and have a large fluorescence quantum yield, long fluorescence lifetime, good photostability, and an emission spectrum in the visible region. Herein, we show that a tryptophan analog, 4-cyanotryptophan, which differs from tryptophan by only two atoms, is the smallest fluorescent amino acid that meets these requirements and has great potential to enable in vitro and in vivo spectroscopic and microscopic measurements of proteins.

Indexed as

Amino AcidsChromophore-Assisted Light InactivationFluorescenceFluorescent DyesMicroscopyProteinsSpectrometry, FluorescenceSpectrum AnalysisTryptophanAmino AcidsFluorescent DyesProteinsTryptophanfluorescence probefluorescence proteinimagingunnatural amino acid

Identifiers

PMID28533371
PMCPMC5468623
OpenAlexW2620137284

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.