P
Petr Pečinka
Researcher at University of Ostrava
Publications - 50
Citations - 1284
Petr Pečinka is an academic researcher from University of Ostrava. The author has contributed to research in topics: DNA & Medicine. The author has an hindex of 14, co-authored 41 publications receiving 1037 citations. Previous affiliations of Petr Pečinka include Academy of Sciences of the Czech Republic & Czechoslovak Academy of Sciences.
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Journal ArticleDOI
DNA tetraplex formation in the control region of c-myc.
TL;DR: It is shown that the targeted control element adopts an intrastrand fold-back DNA tetraplex, which requires potassium ions for stability in vitro, and proposed a transcription initiation mechanism that explains how anti-gene therapy silence c-myc at the molecular level.
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The Presence and Localization of G-Quadruplex Forming Sequences in the Domain of Bacteria
Martin Bartas,Michaela Čutová,Václav Brázda,Patrik Kaura,Jiří Šťastný,Jan Kolomazník,Jan Coufal,Pratik Goswami,Jiří Červeň,Petr Pečinka +9 more
TL;DR: G-quadruplex-forming sequences were identified in all species, however the frequency differed significantly across evolutionary groups, and the highest frequency was detected in the subgroup Deinococcus-Thermus and the lowest frequency in Thermotogae.
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In-Depth Bioinformatic Analyses of Nidovirales Including Human SARS-CoV-2, SARS-CoV, MERS-CoV Viruses Suggest Important Roles of Non-canonical Nucleic Acid Structures in Their Lifecycles
Martin Bartas,Václav Brázda,Václav Brázda,Natália Bohálová,Natália Bohálová,Alessio Cantara,Alessio Cantara,Adriana Volná,Tereza Stachurová,Kateřina Malachová,Eva B. Jagelská,Otília Porubiaková,Otília Porubiaková,Jiří Červeň,Petr Pečinka +14 more
TL;DR: Evaluated genomes of all coronaviruses sequenced to date found much evidence of putative G-quadruplex sites and even much more of inverted repeats (IRs) loci, which indicate a possible mechanism for genomic RNA packaging.
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Role of tumor suppressor p53 domains in selective binding to supercoiled DNA
Marie Brázdová,Jan Paleček,Dmitry I. Cherny,Sabina Billová,Miroslav Fojta,Petr Pečinka,Bořivoj Vojtěšek,Thomas M. Jovin,Emil Paleček +8 more
TL;DR: It is demonstrated here that the p53 C-terminal domain (amino acids 347-382) and a p53 oligomeric state are important for SCS binding and a model according to which two DNA duplexes are compacted into p53-scDNA filaments is proposed and a role for filament formation in recombination is discussed.
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The Amino Acid Composition of Quadruplex Binding Proteins Reveals a Shared Motif and Predicts New Potential Quadruplex Interactors.
TL;DR: The amino acid composition of all seventy-seven described G-quadruplex binding proteins of Homo sapiens is analyzed and a new set of potential G- quadruplexbinding proteins are predicted sharing this interesting domain rich in glycine and arginine residues.