Zobrazeno 1 - 3
of 3
pro vyhledávání: '"Giada Lo Gullo"'
Autor:
Giada Lo Gullo, Maria Luisa De Santis, Alessandro Paiardini, Serena Rosignoli, Alice Romagnoli, Anna La Teana, Paola Londei, Dario Benelli
Publikováno v:
Frontiers in Microbiology, Vol 12 (2021)
The translation factor IF6 is a protein of about 25 kDa shared by the Archaea and the Eukarya but absent in Bacteria. It acts as a ribosome anti-association factor that binds to the large subunit preventing the joining to the small subunit. It must b
Externí odkaz:
https://doaj.org/article/cbaf10abcc3c4408aea6f67802f53828
Autor:
Giada Lo Gullo, Rosanna Mattossovich, Giuseppe Perugino, Anna La Teana, Paola Londei, Dario Benelli
Publikováno v:
Archaea, Vol 2019 (2019)
A system is described which permits the efficient synthesis of proteins in vitro at high temperature. It is based on the use of an unfractionated cell lysate (S30) from Sulfolobus solfataricus previously well characterized in our laboratory for trans
Externí odkaz:
https://doaj.org/article/4d9f443b0d74411aa993b5d0dd09c7a0
Autor:
Rosanna Mattossovich, Giuseppe Perugino, Paola Londei, Giada Lo Gullo, Anna La Teana, Dario Benelli
Publikováno v:
Archaea, Vol 2019 (2019)
Archaea (2019): 1–10. doi:10.1155/2019/9848253
info:cnr-pdr/source/autori:Lo Gullo, Giada; Mattossovich, Rosanna; Perugino, Giuseppe; La Teana, Anna; Londei, Paola; Benelli, Dario/titolo:Optimization of an In Vitro Transcription%2FTranslation System Based on Sulfolobus solfataricus Cell Lysate/doi:10.1155%2F2019%2F9848253/rivista:Archaea/anno:2019/pagina_da:1/pagina_a:10/intervallo_pagine:1–10/volume
Archaea
Archaea (2019): 1–10. doi:10.1155/2019/9848253
info:cnr-pdr/source/autori:Lo Gullo, Giada; Mattossovich, Rosanna; Perugino, Giuseppe; La Teana, Anna; Londei, Paola; Benelli, Dario/titolo:Optimization of an In Vitro Transcription%2FTranslation System Based on Sulfolobus solfataricus Cell Lysate/doi:10.1155%2F2019%2F9848253/rivista:Archaea/anno:2019/pagina_da:1/pagina_a:10/intervallo_pagine:1–10/volume
Archaea
A system is described which permits the efficient synthesis of proteins in vitro at high temperature. It is based on the use of an unfractionated cell lysate (S30) from Sulfolobus solfataricus previously well characterized in our laboratory for trans