Helena Ryšlavá

Prof. Dr. Helena Ryšlavá

orcid

Research Focus & Metrics

Academic Career Length

29Years (1998-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

View All Publications
1 April 2011 in Plant Science
Verified
Journal Article
Closed access
VDVeronika Doubnerová
Veronika Doubnerová
HRHelena Ryšlavá
Helena Ryšlavá

1 October 2013 in Journal of Proteomics
Verified
Journal Article
Closed access
HRHelena Ryšlavá
Helena Ryšlavá
VDVeronika Doubnerová
Veronika Doubnerová
DKDaniel Kavan
Daniel Kavan
Ondrej VanekOndrej Vanek
Ondrej Vanek

1 March 2014 in Journal of Plant Physiology
Verified
Journal Article
Closed access
Veronika HyskovaVeronika Hyskova
Veronika Hyskova
LMLucia Miedzińska
Lucia Miedzińska
JDJana Dobrá
Jana Dobrá
RVRadomira Vankova
Radomira Vankova
HRHelena Ryšlavá
Helena Ryšlavá

1 September 2003 in Photosynthetica
Verified
Journal Article
Closed access
PDF file
HRHelena Ryšlavá
Helena Ryšlavá
KMKarel Müller
Karel Müller
ŠSŠ. Semorádová
Š. Semorádová
HSH. Synková
H. Synková
NCNoemi Cerovska
Noemi Cerovska
The influence of viral infection caused by two different potyviruses, Potato virus Y (PVY) and Potato virus A (PVA) on plant metabolism and photosynthetic apparatus of Nicotiana tabacum L. cv. Samsun and cv. Petit Havana SR1 was studied. The main stress was focused on the activities of phosphoenolpyruvate carboxylase (PEPC), NADP-malic enzyme (NADP-ME), and pyruvate phosphate dikinase (PPDK). The analysis of the presence of viral proteins, enzyme activities, and different photosynthetic parameters showed the time dependent progress of viral infection and NADP-ME and PEPC activities. PVY caused significant response, while PVA affected both tobacco cultivars only slightly. Viral infection, namely PVY, affected more negatively photosynthetic apparatus of cv. Petit Havana SR1 than cv. Samsun.

8 February 2022 in Microbiological Research
Verified
Journal Article
Closed access
KBKateřina Bělonožníková
Kateřina Bělonožníková
Veronika HyskovaVeronika Hyskova
Veronika Hyskova
JCJosef Chmelík
Josef Chmelík
DKDaniel Kavan
Daniel Kavan
NCNoemi Cerovska
Noemi Cerovska
HRHelena Ryšlavá
Helena Ryšlavá

25 October 2006 in International Journal of Cancer
Verified
Journal Article
Open access
PDF file
MSMarie Stiborova
Marie Stiborova
JPJitka Poljaková
Jitka Poljaková
HRHelena Ryšlavá
Helena Ryšlavá
MDMartin Dracinsky
Martin Dracinsky
TETomáš Eckschlager
Tomáš Eckschlager
EFEva Frei
Eva Frei
Ellipticine is a potent antineoplastic agent, whose mode of action is considered to be based mainly on DNA intercalation, inhibition of topoisomerase II and cytochrome P450‐mediated formation of covalent DNA adducts. This is the first report on the molecular mechanism of ellipticine oxidation by peroxidases (human myeloperoxidase, human and ovine cyclooxygenases, bovine lactoperoxidase, horseradish peroxidase) to species forming ellipticine‐DNA adducts. Using NMR spectroscopy, the structures of 2 ellipticine metabolites were identified; the major product is the ellipticine dimer, in which the 2 ellipticine skeletons are connected via N6 of the pyrrole ring of one ellipticine molecule and C9 in the second one. The minor metabolite is ellipticine N2‐oxide. Using 32P‐postlabeling and [3H]‐labeled ellipticine, we showed that ellipticine binds covalently to DNA after its activation by peroxidases. The DNA adduct pattern induced by ellipticine consisted of a cluster of up to 4 adducts. The 2 adducts are indistinguishable from the 2 major adducts generated between deoxyguanosine in DNA and either 13‐hydroxy‐ or 12‐hydroxyellipticine or in rats treated with ellipticine, or if ellipticine was activated with human hepatic and renal microsomes. The results presented here are the first characterization of the peroxidase‐mediated oxidative metabolites of ellipticine and we have proposed species, 2 carbenium ions, ellipticine‐13‐ylium and ellipticine‐12‐ylium, as reactive species generating 2 major DNA adducts seen in vivo in rats treated with ellipticine. The study forms the basis to further predict the susceptibility of human cancers to ellipticine.