Evidence map›Paper›PMID 35574633›Full record

ArticleJournal of the American Chemical Society2022

The Magic of Linking Rings: Discovery of a Unique Photoinduced Fluorescent Protein Crosslink.

Manman Lu, Dmitri Toptygin, Yufei Xiang, Yi Shi, Charles D Schwieters, Emma C Lipinski, Jinwoo Ahn, In-Ja L Byeon, Angela M Gronenborn

Open access · greenAbstract read
In one paragraph

Article in Journal of the American Chemical Society, 2022. 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
0.9field-weighted citation impact, top 29% 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, 11 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

9 authors at 3 institutions in 1 country.

Manman LuDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, United States.ORCID 0000-0002-4156-4975
Dmitri ToptyginDepartment of Biology, Johns Hopkins University, Baltimore, Maryland 21218, United States.ORCID 0000-0001-5800-861X
Yufei XiangDepartment of Cell Biology, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, United States.
Yi ShiDepartment of Cell Biology, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, United States.
Charles D SchwietersComputational Biomolecular Magnetic Resonance Core, Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0520, United States.
Emma C LipinskiDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, United States.
Jinwoo AhnDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, United States.
In-Ja L ByeonDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, United States.
Angela M GronenbornDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261, United States.ORCID 0000-0001-9072-3525
University of Pittsburgh · USJohns Hopkins University · USNational Institutes of Health · US

Funding

Technology Development 2: MAS NMR and dynamic nuclear polarization for HIV-1 structural biologyP50AI150481 · NIAID · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI GRONENBORN, ANGELA M. · 2019 to 2021
$14.1M
Mapping the Dynamic Interactome of Ig-fold Membrane Proteins Using Nanobody-Based ToolsR35GM137905 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI Yi Shi · 2020 to 2026
$2.8M
NIAID NIH HHS P50 AI150481NIGMS NIH HHS R35 GM137905
6 · The paper itself

Abstract

Fluorosubstituted tryptophans serve as valuable probes for fluorescence and nuclear magnetic resonance (NMR) studies of proteins. Here, we describe an unusual photoreactivity introduced by replacing the single tryptophan in cyclophilin A with 7-fluoro-tryptophan. UV exposure at 282 nm defluorinates 7-fluoro-tryptophan and crosslinks it to a nearby phenylalanine, generating a bright fluorophore. The crosslink-containing fluorescent protein possesses a large quantum yield of ∼0.40 with a fluorescence lifetime of 2.38 ns. The chemical nature of the crosslink and the three-dimensional protein structure were determined by mass spectrometry and NMR spectroscopy. To the best of our knowledge, this is the first report of a Phe-Trp crosslink in a protein. Our finding may break new ground for developing novel fluorescence probes and for devising new strategies to exploit aromatic crosslinks in proteins.

Indexed as

PhenylalanineTryptophanSpectrometry, FluorescencePhenylalanineTryptophan

Identifiers

PMID35574633
PMCPMC9233106
OpenAlexW4280561889

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.