ArticleJournal of fluorescence2008
Fluorescence characterization of the hydrophobic pocket of cyclophilin B.
Article in Journal of fluorescence, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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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.
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Who cites it
2 citing papers in PubMed, 6 citations in OpenAlex.
- Origin of tryptophan fluorescence lifetimes part 1. Fluorescence lifetimes origin of tryptophan free in solution.Journal of fluorescence · 2014Article
- Fluorescence lifetimes of tryptophan: structural origin and relation with So --> 1Lb and So --> 1La transitions.Journal of fluorescence · 2009Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
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Abstract
Human cyclophilin B is a monomeric protein that contains two tryptophan residues, Trp104 and 128. Trp128-residue belongs to the binding site of cyclosporin A and is the homologous of Trp 121 in CyPA, while Trp104 residue belongs to the hydrophobic pocket. In the present work, we studied the dynamics of Trp residue(s) of cyclophilin B and of the CyPB(w128A) mutant and of TNS-mutant complex. Our results showed that Trp-104 and TNS show restricted motions within their environments and that energy transfer between the two fluorophores is occurring.
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