English   español  
Please use this identifier to cite or link to this item: http://hdl.handle.net/10261/211992
Share/Impact:
Statistics
logo share SHARE logo core CORE   Add this article to your Mendeley library MendeleyBASE

Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL
Exportar a otros formatos:

Title

Differential protein kinase C phosphorylation sites in the L17 ribosomal protein from Leishmania infantum

AuthorsGonzález-Aseguinolaza, Gloria; Taladriz, Soraya; Marquet, Alberto; Larraga, Vicente
KeywordsProtein kinase
Protein family
Phosphorylation site
Macrolide
Encode gene
Issue DateJan-2000
PublisherSpringer
CitationParasitol Res 86 (1) 36-40 (2000)
AbstractLeishmania infantum, the protozoan parasite responsible for leishmaniasis in Europe, is capable of undergoing developmental changes in vitro and provides an excellent model for the study of cell differentiation processes. We have cloned the gene encoding the L17 ribosomal protein. The LiL17 protein family belongs to the macrolide binding site, related to the peptidyl transferase center of the ribosome. Its comparison with other members of the protein family shows several structural differences that may reflect functional variations. The protein kinase C phosphorylation sites display an intermediate pattern involving differences in location and type of residue with respect to all the species considered. Gene-structural analysis suggests the existence of two different encoding genes. The expression of the genes seem to be different with the distinct growth phases of the parasite.
Description5 p.-4 fig.
Publisher version (URL)https://doi.org/10.1007/PL00008504
URIhttp://hdl.handle.net/10261/211992
DOI10.1007/PL00008504
ISSN0932-0113
E-ISSN1432-1955
Appears in Collections:(CIB) Artículos
Files in This Item:
File Description SizeFormat 
accesoRestringido.pdfRestringido15,38 kBAdobe PDFThumbnail
View/Open
Show full item record
Review this work
 

Related articles:


WARNING: Items in Digital.CSIC are protected by copyright, with all rights reserved, unless otherwise indicated.