Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Nataša Lindič"'
Autor:
Patrick Y. A. Reinke, Edmarcia Elisa de Souza, Sebastian Günther, Sven Falke, Julia Lieske, Wiebke Ewert, Jure Loboda, Alexander Herrmann, Aida Rahmani Mashhour, Katarina Karničar, Aleksandra Usenik, Nataša Lindič, Andreja Sekirnik, Viviane Fongaro Botosso, Gláucia Maria Machado Santelli, Josana Kapronezai, Marcelo Valdemir de Araújo, Taiana Tainá Silva-Pereira, Antônio Francisco de Souza Filho, Mariana Silva Tavares, Lizdany Flórez-Álvarez, Danielle Bruna Leal de Oliveira, Edison Luiz Durigon, Paula Roberta Giaretta, Marcos Bryan Heinemann, Maurice Hauser, Brandon Seychell, Hendrik Böhler, Wioletta Rut, Marcin Drag, Tobias Beck, Russell Cox, Henry N. Chapman, Christian Betzel, Wolfgang Brehm, Winfried Hinrichs, Gregor Ebert, Sharissa L. Latham, Ana Marcia de Sá Guimarães, Dusan Turk, Carsten Wrenger, Alke Meents
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-13 (2023)
Abstract Several drug screening campaigns identified Calpeptin as a drug candidate against SARS-CoV-2. Initially reported to target the viral main protease (Mpro), its moderate activity in Mpro inhibition assays hints at a second target. Indeed, we s
Externí odkaz:
https://doaj.org/article/959ee7d783844cc0965882267049dc4f
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 17, p 6153 (2020)
SecA protein is a major component of the general bacterial secretory system. It is an ATPase that couples nucleotide hydrolysis to protein translocation. In some Gram-positive pathogens, a second paralogue, SecA2, exports a different set of substrate
Externí odkaz:
https://doaj.org/article/763eedf700b64c768cb6357f610cc1b9
Publikováno v:
International Journal of Molecular Sciences
Volume 21
Issue 17
International Journal of Molecular Sciences, Vol 21, Iss 6153, p 6153 (2020)
Volume 21
Issue 17
International Journal of Molecular Sciences, Vol 21, Iss 6153, p 6153 (2020)
SecA protein is a major component of the general bacterial secretory system. It is an ATPase that couples nucleotide hydrolysis to protein translocation. In some Gram-positive pathogens, a second paralogue, SecA2, exports a different set of substrate
Autor:
Jure Borišek, Gregor Pretnar, Miha Renko, Aleksandra Usenik, Nataša Lindič, Andrej Perdih, Dušan Turk, Marko Mihelič, Uwe Müller
Publikováno v:
Structure. 25:514-521
Bacterial cell wall proteins play crucial roles in cell survival, growth, and environmental interactions. In Gram-positive bacteria, cell wall proteins include several types that are non-covalently attached via cell wall binding domains. Of the two c
Autor:
Maruška Budič, Toni Petan, Binyamin A. Knisbacher, Nika Lovšin, Erez Y. Levanon, Nataša Lindič
Publikováno v:
Retrovirology
Background The role of AID/APOBEC proteins in the mammalian immune response against retroviruses and retrotransposons is well established. G to A hypermutations, the hallmark of their cytidine deaminase activity, are present in several mammalian retr