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The study of formation of retroviral capsids as a nucleic acids delivery system

The result's identifiers

  • Result code in IS VaVaI

    <a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22330%2F05%3A00015671" target="_blank" >RIV/60461373:22330/05:00015671 - isvavai.cz</a>

  • Result on the web

  • DOI - Digital Object Identifier

Alternative languages

  • Result language

    angličtina

  • Original language name

    The study of formation of retroviral capsids as a nucleic acids delivery system

  • Original language description

    Our research is focused on study of formation of Mason-Pfizer monkey virus (M-PMV) capsids in vitro. The understanding of retroviral capsid assembly mechanism and nucleic acids incorporation could significantly contribute to further use of these systemsfor therapeutic purposes. All retroviruses form a single structural precursor polyprotein Gag that initiates and directs the assembly of immature retroviral capsid. Our interest has been focused on minimized Gag domain, namely fused capsid and nucleocapsid proteins (CA-NC), which contain domains responsible for interactions during capsid assembly process. CA-NC protein was purified by several techniques to ensure the elimination of nucleic acids that could contaminate final product. We optimized the assembly reaction by monitoring of different conditions as various concentrations of salts, pH, temperature and presence of oligonucleotides or RNA. The assembly reaction of protein and RNA or oligonucleotide were performed during dialysis a

  • Czech name

    Studium tvorby kapsid retrovirů jako systému k přenosu nukleových kyselin

  • Czech description

    Our research is focused on study of formation of Mason-Pfizer monkey virus (M-PMV) capsids in vitro. The understanding of retroviral capsid assembly mechanism and nucleic acids incorporation could significantly contribute to further use of these systemsfor therapeutic purposes. All retroviruses form a single structural precursor polyprotein Gag that initiates and directs the assembly of immature retroviral capsid. Our interest has been focused on minimized Gag domain, namely fused capsid and nucleocapsid proteins (CA-NC), which contain domains responsible for interactions during capsid assembly process. CA-NC protein was purified by several techniques to ensure the elimination of nucleic acids that could contaminate final product. We optimized the assembly reaction by monitoring of different conditions as various concentrations of salts, pH, temperature and presence of oligonucleotides or RNA. The assembly reaction of protein and RNA or oligonucleotide were performed during dialysis a

Classification

  • Type

    O - Miscellaneous

  • CEP classification

    EE - Microbiology, virology

  • OECD FORD branch

Result continuities

  • Project

    <a href="/en/project/1M0520" target="_blank" >1M0520: Center for Applied Genomics</a><br>

  • Continuities

    P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Others

  • Publication year

    2005

  • Confidentiality

    S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů