Richard Izrael

Richard Izrael
Hungarian Academy of Sciences | HAS · Institute of Enzymology

Master of Science

About

8
Publications
855
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17
Citations
Introduction
Richard Izrael currently works at the Institute of Enzymology, Hungarian Academy of Sciences. Richard does research in Parasitology, Molecular Biology and Cell Biology.
Additional affiliations
June 2016 - present
Research Centre of Natural Sciences
Position
  • PhD Student
Education
February 2020 - January 2024
University of Szeged
Field of study
  • Theoretical Medicine
January 2018 - January 2020
Budapest University of Technology and Economics
Field of study
  • Biochemical Engineering
September 2014 - January 2018
Budapest University of Technology and Economics
Field of study
  • Biochemical Engineering

Network

Cited By

Projects

Projects (3)
Project
Our current project aims to target the endogenous DNA glycosylases e.g. uracil DNA-glycosylase and 8-oxoguanine-glycosylase for gene disruption with CRISPR-Cas9 system. We plan to observe the essentiality of these genes, as well as their impact on the parasite fitness and the emergence rate of resistance.
Project
The fast occurance of drug resistant malaria parasites indicates an increased genomic variability. Disruption of genetic integrity can be caused either by mutagenic events in the DNA which is corrected by different repair mechanisms or by the misincorporation of dNTPs during the replication by the DNA polymerase. Perturbance of the dNTP pool under drug stress could lead to an increased mutation rate in the life cycle of the fast proliferating Plasmodium falciparum parasite.
Project
CTP:phosphocholine cytidylyltransferase catalyzes the rate-limiting step of phosphatidyl-choline biosynthesis, a phospholipid that is abundant in the membrane of malaria parasite. During the fast-proliferating intraerythrocytic life cycle the Plasmodium cells are in desperate need of membrangenesis, therefore it is an essential pathway for their development. In an effort to extend our knowledge about the nature of the special regulation that this enzyme is under, we investigate the subcellular localization of CCT in mammalian cell lines, to determine whether there are specific preferences for membrane binding or not.