Evidence map›Paper›PMID 20446733›Full record

ArticleJournal of the American Chemical Society2010

Mechanisms of quenching of Alexa fluorophores by natural amino acids.

Huimin Chen, Syed S Ahsan, Mitk'El B Santiago-Berrios, Hector D Abruña, Watt W Webb

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed
–field-weighted citation impact
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

75 citing papers in PubMed.

  1. Article
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  9. Thioether editing generally increases the photostability of rhodamine dyes on self-labeling tags.Proceedings of the National Academy of Sciences of the United States of America · 2025
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15 more citing papers are in PubMed but not listed here.

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

5 authors.

Huimin ChenSchool of Applied and Engineering Physics, 212 Clark Hall, Cornell University, Ithaca, New York 14853, USA.
Syed S Ahsan
Mitk'El B Santiago-Berrios
Hector D Abruña
Watt W Webb

Funding

Development of Medical Multiphoton Microscopic EndoscopyR01EB006736 · NIBIB · CORNELL UNIVERSITY · PI WEBB, WATT W · 2007 to 2011
$5.3M
NIBIB NIH HHS R01 EB006736
6 · The paper itself

Abstract

Quenching of fluorophores by the same proteins that they covalently label is a phenomenon that is neither well-known nor well-characterized. It is often assumed that fluorophores are unperturbed by their target proteins. However, it has been observed that attached fluorophores can be quenched by contact with amino acids within the same protein, and this property has been exploited to report on changing conformational states or intramolecular dynamics of proteins. We show in this communication that fluorescence of Alexa dyes is, in fact, quenched by interactions with Trp, Tyr, Met, and His residues through a combination of static and dynamic quenching mechanisms. In light of this finding, the potential effect of intramolecular quenching should be considered in the interpretation of data that involves quantitative measurements of fluorescence intensity in proteins.

Indexed as

FluorescenceAmino AcidsFluorescent DyesHistidineHydrazinesMethionineProtein ConformationProteinsTryptophanTyrosineAlexa 488 hydrazideAmino AcidsFluorescent DyesHistidineHydrazinesMethionineProteinsTryptophanTyrosine

Identifiers

PMID20446733
PMCPMC2892418

What OpenQuestion holds

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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.