Isil Aksan Kurnaz

Affiliations: 
2008-2012 Genetics and Bioengineering Yeditepe University, Istanbul Turkey 
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"Isil Kurnaz"
Mean distance: 16.28 (cluster 11)
 
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Publications

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Kandemir B, Kurnaz IA. (2024) The Role of Pea3 Transcription Factor Subfamily in the Nervous System. Molecular Neurobiology
Sogut MS, Venugopal C, Kandemir B, et al. (2021) ETS-Domain Transcription Factor Elk-1 Regulates Stemness Genes in Brain Tumors and CD133+ BrainTumor-Initiating Cells. Journal of Personalized Medicine. 11
Babal YK, Kandemir B, Kurnaz IA. (2021) Gene Regulatory Network of ETS Domain Transcription Factors in Different Stages of Glioma. Journal of Personalized Medicine. 11
Kandemir B, Gulfidan G, Arga KY, et al. (2020) Transcriptomic profile of Pea3 family members reveal regulatory codes for axon outgrowth and neuronal connection specificity. Scientific Reports. 10: 18162
Kandemir B, Davis S, Yiğit EN, et al. (2020) Expression of Pea3 protein subfamily members in hippocampus and potential regulation following neuronal stimulation. Neuroscience Letters. 135348
Süer C, Liman N, Kandemir B, et al. (2015) P.1.e.017 A decrease in phosphorylation of CREB may explain delayed place learning and attenuated long-term potentiation in adult-onset hyperthyroidism European Neuropsychopharmacology. 25: S218-S219
Kandemir B, Caglayan B, Hausott B, et al. (2014) Pea3 transcription factor promotes neurite outgrowth. Frontiers in Molecular Neuroscience. 7: 59
Demir O, Kurnaz IA. (2013) Phospho-Ser383-Elk-1 is localized to the mitotic spindles during cell cycle and interacts with mitotic kinase Aurora-A. Cell Biochemistry and Function. 31: 591-8
Mut M, Lule S, Demir O, et al. (2012) Both mitogen-activated protein kinase (MAPK)/extracellular-signal-regulated kinases (ERK) 1/2 and phosphatidylinositide-3-OH kinase (PI3K)/Akt pathways regulate activation of E-twenty-six (ETS)-like transcription factor 1 (Elk-1) in U138 glioblastoma cells. The International Journal of Biochemistry & Cell Biology. 44: 302-10
Demir O, Ari O, Kurnaz IA. (2012) Elk-1 interacts with dynein upon serum stimulation but independent of serine 383 phosphorylation. Cellular and Molecular Neurobiology. 32: 185-9
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