An analysis of phosphorylation sites in protein kinases from Leishmania

Protein kinases are promising drug targets for Leishmaniasis. We have evaluated the phosphorylation potential of protein kinases in different species and strains of Leishmania. Phosphorylation potential of serine, threonine and tyrosine residues of kinases in Leishmania parasite were studied. The re...

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Detalles Bibliográficos
Autores principales: Sinha, Sukrat, Sundaram, Shanthy
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Biomedical Informatics 2016
Materias:
Hypothesis
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5290666/
https://www.ncbi.nlm.nih.gov/pubmed/28197062
http://dx.doi.org/10.6026/97320630012249
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author Sinha, Sukrat
Sundaram, Shanthy
author_facet Sinha, Sukrat
Sundaram, Shanthy
author_sort Sinha, Sukrat
collection PubMed
description Protein kinases are promising drug targets for Leishmaniasis. We have evaluated the phosphorylation potential of protein kinases in different species and strains of Leishmania. Phosphorylation potential of serine, threonine and tyrosine residues of kinases in Leishmania parasite were studied. The results indicate that some species specific residues of serine, threonine and tyrosine have a phosphorylation potential of 1 suggesting that these residues are important target sites in protein kinases based anti-leishmanial therapies.
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spelling pubmed-52906662017-02-14 An analysis of phosphorylation sites in protein kinases from Leishmania Sinha, Sukrat Sundaram, Shanthy Bioinformation Hypothesis Protein kinases are promising drug targets for Leishmaniasis. We have evaluated the phosphorylation potential of protein kinases in different species and strains of Leishmania. Phosphorylation potential of serine, threonine and tyrosine residues of kinases in Leishmania parasite were studied. The results indicate that some species specific residues of serine, threonine and tyrosine have a phosphorylation potential of 1 suggesting that these residues are important target sites in protein kinases based anti-leishmanial therapies. Biomedical Informatics 2016-07-26 /pmc/articles/PMC5290666/ /pubmed/28197062 http://dx.doi.org/10.6026/97320630012249 Text en © 2016 Biomedical Informatics This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.
spellingShingle Hypothesis
Sinha, Sukrat
Sundaram, Shanthy
An analysis of phosphorylation sites in protein kinases from Leishmania
title An analysis of phosphorylation sites in protein kinases from Leishmania
title_full An analysis of phosphorylation sites in protein kinases from Leishmania
title_fullStr An analysis of phosphorylation sites in protein kinases from Leishmania
title_full_unstemmed An analysis of phosphorylation sites in protein kinases from Leishmania
title_short An analysis of phosphorylation sites in protein kinases from Leishmania
title_sort analysis of phosphorylation sites in protein kinases from leishmania
topic Hypothesis
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5290666/
https://www.ncbi.nlm.nih.gov/pubmed/28197062
http://dx.doi.org/10.6026/97320630012249
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