Bio

Professional Education


  • Bachelor of Science, Bilkent University (2006)
  • Doctor of Philosophy, Univ of Massachusetts Medical School (2012)

Stanford Advisors


Research & Scholarship

Current Research and Scholarly Interests


I study non-coding sequence elements that regulate protein translation during mammalian development.

Publications

Journal Articles


  • Argonaute proteins CURRENT BIOLOGY Cenik, E. S., Zamore, P. D. 2011; 21 (12): R446-R449

    View details for Web of Science ID 000292221900003

    View details for PubMedID 21683893

  • Phosphate and R2D2 Restrict the Substrate Specificity of Dicer-2, an ATP-Driven Ribonuclease MOLECULAR CELL Cenik, E. S., Fukunaga, R., Lu, G., Dutcher, R., Wang, Y., Hall, T. M., Zamore, P. D. 2011; 42 (2): 172-184

    Abstract

    Drosophila Dicer-2 generates small interfering RNAs (siRNAs) from long double-stranded RNA (dsRNA), whereas Dicer-1 produces microRNAs (miRNAs) from pre-miRNA. What makes the two Dicers specific for their biological substrates? We find that purified Dicer-2 can efficiently cleave pre-miRNA, but that inorganic phosphate and the Dicer-2 partner protein R2D2 inhibit pre-miRNA cleavage. Dicer-2 contains C-terminal RNase III domains that mediate RNA cleavage and an N-terminal helicase motif, whose function is unclear. We show that Dicer-2 is a dsRNA-stimulated ATPase that hydrolyzes ATP to ADP; ATP hydrolysis is required for Dicer-2 to process long dsRNA, but not pre-miRNA. Wild-type Dicer-2, but not a mutant defective in ATP hydrolysis, can generate siRNAs faster than it can dissociate from a long dsRNA substrate. We propose that the Dicer-2 helicase domain uses ATP to generate many siRNAs from a single molecule of dsRNA before dissociating from its substrate.

    View details for DOI 10.1016/j.molcel.2011.03.002

    View details for Web of Science ID 000289873700006

    View details for PubMedID 21419681

  • Variation in the attachment of Streptococcus pneumoniae to human pharyngeal epithelial cells after treatment with S-carboxymethylcysteine. Journal of infection and chemotherapy Suer, E., Sayrac, S., Sarinay, E., Ozturk, H. E., Turkoz, M., Ichinose, A., Nagatake, T., Ahmed, K. 2008; 14 (4): 333-336

    Abstract

    S-carboxymethylcysteine (S-CMC) is a mucolytic agent that can prevent respiratory infection by decreasing the attachment of respiratory pathogens to human pharyngeal epithelial cells (HPECs). Streptococcus pneumoniae is a major cause of respiratory infections. A previous study revealed that treatment of S. pneumoniae with S-CMC caused a decrease in the attachment of this bacterium to HPECs. In the present study we found that the effect of S-CMC varied according to hosts and strains. S-CMC treatment altered the surface structure of S. pneumoniae, resulting in a decrease of attachment, without affecting the virulence of the bacteria.

    View details for DOI 10.1007/s10156-008-0626-z

    View details for PubMedID 18709541

  • Turkish isolates of Helicobacter pylori belong to the Middle Eastern genotypes CLINICAL MICROBIOLOGY AND INFECTION Baglan, P. H., Sarinay, E., Ahmed, K., Ozkan, M., Bozday, G., Bozday, A. M., Ozden, A. 2006; 12 (1): 97-98

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