ArticleChembiochem : a European journal of chemical biology2013
FRET-capture: a sensitive method for the detection of dynamic protein interactions.
Article in Chembiochem : a European journal of chemical biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Rational Design of Phe-BODIPY Amino Acids as Fluorogenic Building Blocks for Peptide-Based Detection of Urinary Tract Candida Infections.Angewandte Chemie (International ed. in English) · 2022Article
- Rationales Design von Phe-BODIPY-Aminosäuren als fluorogene Bausteine für den peptidbasierten Nachweis vonAngewandte Chemie (Weinheim an der Bergstrasse, Germany) · 2022Article
- Fluorescent amino acids as versatile building blocks for chemical biology.Nature reviews. Chemistry · 2020Review
- Principles and Overview of Sampling Methods for Modeling Macromolecular Structure and Dynamics.PLoS computational biology · 2016Review
- Solvatoemissive dual fluorescence of N-(pyridylmethyl)-3-nitro-1,8-naphthalimides.Journal of fluorescence · 2014Article
Corrections and comments
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Authors and funding
2 authors.
Funding
Abstract
Caught in the act: The FRET-Capture approach exploits a bound solvatochromic fluorophore, 4-N,N-dimethylamino-1,8-naphthalimide, as a FRET donor in both inter- and intramolecular energy transfer. A unique feature of this method is the additional level of signal selectivity as the FRET signal is only turned on when the donor is specifically bound to the protein of interest, eliminating high background and false positive signals.
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Registered trials
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