Πλοήγηση ανά Συγγραφέα "Nikolakaki, E."
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Association of protamine 1 with HP1 during spermiogenesis is mediated through their temporal interaction with LBR
Mylonis, I.; Voukkalis, N.; Sanidas, I.; Drosou, V.; Nikolakaki, E.; Sassone-Corsi, P.; Giannakouros, T. (2007) -
Cloning and characterization of an alternatively spliced form of SR protein kinase 1 that interacts specifically with scaffold attachment factor-B
Nikolakaki, E.; Kohen, R.; Hartmann, A. M.; Stamm, S.; Georgatsou, E.; Giannakouros, T. (2001)Serine/arginine protein kinases have been conserved throughout evolution and are thought to play important roles in the regulation of mRNA processing, nuclear import, germline development, polyamine transport, and ion ... -
The enzymatic activity of SR protein kinases 1 and 1a is negatively affected by interaction with scaffold attachment factors B1 and 2
Tsianou, D.; Nikolakaki, E.; Tzitzira, A.; Bonanou, S.; Giannakouros, T.; Georgatsou, E. (2009)SR protein kinases (SRPKs) phosphorylate Ser/Arg dipeptide-containing proteins that play crucial roles in a broad spectrum of basic cellular processes. Phosphorylation by SRPKs constitutes a major way of regulating such ... -
SAFB1 interacts with and suppresses the transcriptional activity of p53
Peidis, P.; Voukkalis, N.; Aggelidou, E.; Georgatsou, E.; Hadzopoulou-Cladaras, M.; Scott, R. E.; Nikolakaki, E.; Giannakouros, T. (2011)A significant amount of nuclear p53 is found associated with the nuclear matrix in cells that were exposed to genotoxic stress. In this study we identified Scaffold attachment factor B1 (SAFB1), a nuclear matrix-associated ... -
Serine-arginine protein kinase 1 (SRPK1) is resilient to nuclear translocation under different metabolic stimuli
Drakouli, S.; Mylonis, I.; Nikolakaki, E.; Giannakouros, T.; Georgatsou, E. (2014) -
Serine-arginine protein kinases: a small protein kinase family with a large cellular presence
Giannakouros, T.; Nikolakaki, E.; Mylonis, I.; Georgatsou, E. (2011)Serine-arginine protein kinases (SPRKs) constitute a relatively novel subfamily of serine-threonine kinases that specifically phosphorylate serine residues residing in serine-arginine/arginine-serine dipeptide motifs. ...