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Breast cancer-associated protein--a novel binding partner of Mason-Pfizer monkey virus protease
M. Rumlová, I. Křížová, R. Hadravová, M. Doležal, K. Strohalmová, A. Keprová, I. Pichová, T. Ruml,
Jazyk angličtina Země Anglie, Velká Británie
Typ dokumentu časopisecké články, práce podpořená grantem
NLK
Free Medical Journals
od 1967 do Před 1 rokem
Freely Accessible Science Journals
od 1967 do Před 12 měsíci
PubMed
24659101
DOI
10.1099/vir.0.064345-0
Knihovny.cz E-zdroje
- MeSH
- adaptorové proteiny signální transdukční chemie genetika metabolismus MeSH
- druhová specificita MeSH
- endopeptidasy chemie genetika metabolismus MeSH
- HEK293 buňky MeSH
- interakční proteinové domény a motivy MeSH
- jaderné proteiny chemie genetika metabolismus MeSH
- lidé MeSH
- Masonův-Pfizerův opičí virus enzymologie genetika MeSH
- molekulární sekvence - údaje MeSH
- rekombinantní proteiny chemie genetika metabolismus MeSH
- sekvence aminokyselin MeSH
- sekvenční homologie aminokyselin MeSH
- vazba proteinů MeSH
- zvířata MeSH
- Check Tag
- lidé MeSH
- ženské pohlaví MeSH
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
We identified breast cancer-associated protein (BCA3) as a novel binding partner of Mason-Pfizer monkey virus (MPMV) protease (PR). The interaction was confirmed by co-immunoprecipitation and immunocolocalization of MPMV PR and BCA3. Full-length but not C-terminally truncated BCA3 was incorporated into MPMV virions. We ruled out the potential role of the G-patch domain, a glycine-rich domain located at the C terminus of MPMV PR, in BCA3 interaction and virion incorporation. Expression of BCA3 did not affect MPMV particle release and proteolytic processing; however, it slightly increased MPMV infectivity.
Citace poskytuje Crossref.org
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