ArticleEuropean biophysics journal : EBJ2007
A molecular dynamics study of Cyclophilin A free and in complex with the Ala-Pro dipeptide.
Article in European biophysics journal : EBJ, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 11 citations in OpenAlex.
- Human Cyclophilins-An Emerging Class of Drug Targets.Medicinal research reviews · 2026Review
- Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases.PLoS biology · 2010Article
- A cyclophilin A inducible expressed in gonad of zhikong scallop Chlamys farreri.Molecular biology reports · 2009Article
- Mechanism of action of cyclophilin a explored by metadynamics simulations.PLoS computational biology · 2009Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
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Abstract
Six different molecular dynamics simulations of Cyclophilin A, three with the protein free in water and three with the Ala-Pro dipeptide bound to the protein, have been performed, and analysed with respect to structure and hydration of the active site. The water structure in the binding pocket of the free Cyclophilin A was found to mimic the experimentally obtained binding cis conformation of the dipeptide. Cyclophilin A is a peptidyl-prolyl cis-trans isomerase (PPIase), but the mechanism of the cis/trans isomerization is not exactly clear. This study was performed to understand better the binding between dipeptide and Cyclophilin A, but also two previously proposed isomerization mechanisms are discussed.
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