Effect on DNA relaxation of the single Thr718Ala mutation in human topoisomerase I: a functional and molecular dynamics study

The functional and dynamical properties of the human topoisomerase I Thr718Ala mutant have been compared to that of the wild-type enzyme using functional assays and molecular dynamics (MD) simulations. At physiological ionic strength, the cleavage and religation rates, evaluated on oligonucleotides...

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Detalles Bibliográficos
Autores principales: Chillemi, Giovanni, Fiorani, Paola, Castelli, Silvia, Bruselles, Alessandro, Benedetti, Piero, Desideri, Alessandro
Formato: Texto
Lenguaje:English
Publicado: Oxford University Press 2005
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1145191/
https://www.ncbi.nlm.nih.gov/pubmed/15944452
http://dx.doi.org/10.1093/nar/gki642

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1145191/
https://www.ncbi.nlm.nih.gov/pubmed/15944452
http://dx.doi.org/10.1093/nar/gki642

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