Zobrazeno 1 - 10
of 26
pro vyhledávání: '"Gabriele, Malengo"'
Autor:
Nicola Bellotto, Jaime Agudo-Canalejo, Remy Colin, Ramin Golestanian, Gabriele Malengo, Victor Sourjik
Publikováno v:
eLife, Vol 11 (2022)
Inside prokaryotic cells, passive translational diffusion typically limits the rates with which cytoplasmic proteins can reach their locations. Diffusion is thus fundamental to most cellular processes, but the understanding of protein mobility in the
Externí odkaz:
https://doaj.org/article/d54911285d5f4fa18e3b35d59f2002cf
Publikováno v:
Molecular Systems Biology, Vol 16, Iss 5, Pp 1-13 (2020)
Abstract Endocytosis is a fundamental cellular trafficking pathway, which requires an organized assembly of the multiprotein endocytic coat to pull the plasma membrane into the cell. Although the protein composition of the endocytic coat is known, it
Externí odkaz:
https://doaj.org/article/11c37104791142a49de1f8992406f086
Autor:
Heiko Babel, Pablo Naranjo-Meneses, Stephanie Trauth, Sonja Schulmeister, Gabriele Malengo, Victor Sourjik, Ilka B. Bischofs
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-13 (2020)
Gram-positive bacteria can release signaling peptides that are ‘probed’ by intracellular receptors after being pumped into the cytoplasm. Here, Babel et al. show that these pump-probe networks can infer the fraction of signal-producing cells in a
Externí odkaz:
https://doaj.org/article/0bde6e03dca6415f82696ad7f1b17df7
Autor:
Shan Jiang, Lydia C. Steup, Charlotte Kippnich, Symela Lazaridi, Gabriele Malengo, Thomas Lemmin, Jing Yuan
A large number of small membrane proteins have been discovered in bacteria, but their mechanism of action has remained mostly elusive. Here, we investigate the mechanism of a physiologically important small protein, MgrB, which represses the activity
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::814ffe15fd37af49faf03080b026c4a6
https://doi.org/10.1101/2022.12.22.521624
https://doi.org/10.1101/2022.12.22.521624
Publikováno v:
eLife, Vol 5 (2016)
The spindle position checkpoint (SPOC) is a spindle pole body (SPB, equivalent of mammalian centrosome) associated surveillance mechanism that halts mitotic exit upon spindle mis-orientation. Here, we monitored the interaction between SPB proteins an
Externí odkaz:
https://doaj.org/article/f1a059a336494e2890f1cd400d1c5dbb
Publikováno v:
Developmental cell. 56(17)
Summary Mechanical forces are integral to many cellular processes, including clathrin-mediated endocytosis, a principal membrane trafficking route into the cell. During endocytosis, forces provided by endocytic proteins and the polymerizing actin cyt
Mechanical forces are integral to many cellular processes, including clathrin-mediated endocytosis, a principal membrane trafficking route into the cell. During endocytosis, forces provided by endocytic proteins and the polymerizing actin cytoskeleto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f2323b7f7e27bc3103ca2fc11b12c837
https://doi.org/10.1101/2020.11.11.378273
https://doi.org/10.1101/2020.11.11.378273
Endocytosis is a fundamental cellular trafficking pathway, which requires an organized assembly of the multiprotein endocytic coat to pull the plasma membrane into the cell. Although the protein composition of the endocytic coat is known, its functio
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::001b7778585fd43cdb1be4acbe278fc2
https://doi.org/10.1101/480996
https://doi.org/10.1101/480996
Autor:
Jing Yuan, Mark Goulian, Victor Sourjik, Gabriele Malengo, Jeffrey N. Carey, Ted Goh, Bryce E. Nickels, Srujana S. Yadavalli, Sangeevan Vellappan
Publikováno v:
Journal of Bacteriology
The PhoQ/PhoP two-component system plays a vital role in the regulation of Mg2+ homeostasis, resistance to acid and hyperosmotic stress, cationic antimicrobial peptides, and virulence in Escherichia coli, Salmonella, and related bacteria. Previous st
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0d06556c8220f38c5bd8b3dc8ec718e0