Zobrazeno 1 - 10
of 145
pro vyhledávání: '"Cell division site"'
Publikováno v:
New Phytologist, 2017 Jul 01. 215(1), 187-201.
Externí odkaz:
https://www.jstor.org/stable/90010642
Autor:
Quentin Gaday, Anne Marie Wehenkel, Adrià Sogues, Sylvain Trépout, Rosario Durán, Alexandre Chenal, Mathilde Ben Assaya, Martín Graña, Pedro M. Alzari, Mariano A. Martinez, Alexis Voegele, Patrick England, Ahmed Haouz, Michael S. VanNieuwenhze
Publikováno v:
Nature Communications, Vol 11, Iss 1, Pp 1-14 (2020)
Nature Communications
Nature Communications, 2020, 11 (1), pp.1641. ⟨10.1038/s41467-020-15490-8⟩
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.1641. ⟨10.1038/s41467-020-15490-8⟩
'Nature Communications ', vol: 11, pages: 1641-1-1641-14 (2020)
Nature Communications
Nature Communications, 2020, 11 (1), pp.1641. ⟨10.1038/s41467-020-15490-8⟩
Nature Communications, Nature Publishing Group, 2020, 11 (1), pp.1641. ⟨10.1038/s41467-020-15490-8⟩
'Nature Communications ', vol: 11, pages: 1641-1-1641-14 (2020)
The mechanisms of Z-ring assembly and regulation in bacteria are poorly understood, particularly in non-model organisms. Actinobacteria, a large bacterial phylum that includes the pathogen Mycobacterium tuberculosis, lack the canonical FtsZ-membrane
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9509fda3998c16d33abe8812d2f6173
http://link.springer.com/article/10.1038/s41467-020-15490-8
http://link.springer.com/article/10.1038/s41467-020-15490-8
Autor:
Frederico J. Gueiros-Filho, Felix Dempwolff, Daniel B. Kearns, Reid T. Oshiro, Yuanchen Yu, Stephen C. Jacobson
Publikováno v:
Journal of Bacteriology. 203
During growth, bacteria increase in size and divide. Division is initiated by the formation of the Z-ring, an intense ring-like cytoskeletal structure formed by treadmilling protofilaments of the tubulin homolog FtsZ. FtsZ localization is thought to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1402bd801edb3c31461b326c1aa9ba93
https://doi.org/10.1128/jb.00249-21
https://doi.org/10.1128/jb.00249-21
Autor:
Zachary C. Elmore, Rachel H. Roberts-Galbraith, Alaina H. Willet, Rahul Bhattacharjee, Liping Ren, Sierra N. Cullati, Janel R. Beckley, Alyssa E. Johnson, Kathleen L. Gould, Jun-Song Chen, Maya G. Igarashi
Publikováno v:
J Cell Sci
The F-BAR protein Imp2 is an important contributor to cytokinesis in the fission yeast Schizosaccharomyces pombe. Because cell cycle-regulated phosphorylation of the central intrinsically disordered region (IDR) of the Imp2 paralog Cdc15 controls Cdc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::41de648745a10d9d2e6b901d44d08d3e
https://europepmc.org/articles/PMC8435286/
https://europepmc.org/articles/PMC8435286/
Publikováno v:
Microscopy. 68:441-449
Peptidoglycan, which is the main component of the bacterial cell wall, is a heterogeneous polymer of glycan strands crosslinked with short peptides and is synthesized in cooperation with the cell division cycle. Although it plays a critical role in b
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::172d0f58ea1409432f1c44d2814287dc
https://doi.org/10.1093/jmicro/dfz033
https://doi.org/10.1093/jmicro/dfz033
Publikováno v:
eLife, Vol 10 (2021)
Cell division site positioning is precisely regulated but the underlying mechanisms are incompletely understood. In the social bacterium Myxococcus xanthus, the ~15 MDa tripartite PomX/Y/Z complex associates with and translocates across the nucleoid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5907578d9e9f3dd44ca18dbd97f901a
https://elifesciences.org/articles/66160
https://elifesciences.org/articles/66160
Autor:
Longfang Yao, Lan Mi, Jiong Ma, Liwen Chen, Li Zhang, Baoju Wang, Xingyu Gong, Jiahui Zhong, Yiyan Fei
Publikováno v:
SSRN Electronic Journal.
When Saccharomyces cerevisiae divides, a structure composed of different septin proteins arranged according to a certain rule is formed at the cell division site. The structure undergoes multiple remodeling stages during the cell cycle, thus guiding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::583a8a291ccfc3aab5946b62b3ee95f7
https://doi.org/10.2139/ssrn.3917170
https://doi.org/10.2139/ssrn.3917170
Autor:
Riyaz Maderbocus, Vassiliy N. Bavro, Gabriela Boelter, Ian R. Henderson, Douglas G. Ward, Manuel Banzhaf, Timothy J. Knowles, Eva Heinz, Mark Jeeves, Alvin C. K. Teo, Amanda E. Rossiter, David I. Roper, Timothy J. Wells, Adam Colyer, Dema Alodaini, Peter J. Wotherspoon, Yanina R. Sevastsyanovich, Adam F. Cunningham, Faye C. Morris, Shu-Sin Chng, Jack A. Bryant, Douglas F. Browning, Michael Overduin, Pooja Sridhar, Kara A. Staunton, Christopher Icke, Trevor Lithgow, Emily C. A. Goodall, Zhi-Soon Chong
Publikováno v:
eLife, Vol 9 (2020)
eLife
eLife
The Gram-negative outer-membrane envelops the bacterium and functions as a permeability barrier against antibiotics, detergents, and environmental stresses. Some virulence factors serve to maintain the integrity of the outer membrane, including DolP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c73781758231d185cf3af7872510f68f
http://wrap.warwick.ac.uk/147267/1/WRAP-structure-dual-BON-domain-protein-DolP-identifies-phospholipid-binding-new-mechanism-protein-localisation-Roper-2020.pdf
http://wrap.warwick.ac.uk/147267/1/WRAP-structure-dual-BON-domain-protein-DolP-identifies-phospholipid-binding-new-mechanism-protein-localisation-Roper-2020.pdf
Autor:
Adam Colyer, Vassiliy N. Bavro, Gabriela Boelter, Riyaz Maderbocus, Douglas G. Ward, Peter J. Wotherspoon, Timothy J. Wells, Kara A. Staunton, Alvin C. K. Teo, S-S. Chng, David I. Roper, Faye C. Morris, Michael Overduin, Adam F. Cunningham, Dema Alodaini, Yanina R. Sevastsyanovich, Eva Heinz, Z-S. Chong, Pooja Sridhar, Timothy J. Knowles, I.R. Henderson, Jack A. Bryant, Douglas F. Browning, Mark Jeeves, Christopher Icke, Manuel Banzhaf, Trevor Lithgow
Publikováno v:
bioRxiv
BioRxiv
BioRxiv
The Gram-negative outer membrane envelops the bacterium and functions as a permeability barrier against antibiotics, detergents and environmental stresses. Some virulence factors serve to maintain the integrity of the outer membrane, including DolP (
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e3c441f729408c3b9771dee9a1762e23
https://doi.org/10.1101/2020.08.10.244616
https://doi.org/10.1101/2020.08.10.244616
Publikováno v:
Curr Biol
Summary Septins form rod-shaped hetero-oligomeric complexes that assemble into filaments and other higher-order structures, such as rings or hourglasses, at the cell division site in fungal and animal cells [ 1 , 2 , 3 , 4 ] to carry out a wide range
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::04d0fd08d87b297749cea71d429504c9
https://europepmc.org/articles/PMC7314651/
https://europepmc.org/articles/PMC7314651/