Zobrazeno 1 - 10
of 19
pro vyhledávání: '"Harry H Low"'
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract The bacterial tight adherence pilus system (TadPS) assembles surface pili essential for adhesion and colonisation in many human pathogens. Pilus dynamics are powered by the ATPase CpaF (TadA), which drives extension and retraction cycles in
Externí odkaz:
https://doaj.org/article/40a21052391d48629e85566a09c911da
Publikováno v:
PLoS ONE, Vol 9, Iss 9, p e107211 (2014)
Escherichia coli (ETEC) strain H10407 contains a GTPase virulence factor, LeoA, which is encoded on a pathogenicity island and has been shown to enhance toxin release, potentially through vesicle secretion. By sequence comparisons and X-ray structure
Externí odkaz:
https://doaj.org/article/6500c90e6f1a451ab21d267993eab9bb
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-13 (2023)
Abstract The bacterial Tight adherence Secretion System (TadSS) assembles surface pili that drive cell adherence, biofilm formation and bacterial predation. The structure and mechanism of the TadSS is mostly unknown. This includes characterisation of
Externí odkaz:
https://doaj.org/article/9bc2645b939c4617ac8a18162866e2ee
Autor:
Anastasia A. Chernyatina, Harry H. Low
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-10 (2019)
Bacterial type II secretion systems (T2SSs) translocate virulence factors, toxins and enzymes across the cell outer membrane. Here, Chernyatina and Low use negative stain and cryo-electron microscopy to reveal the core architecture of an assembled T2
Externí odkaz:
https://doaj.org/article/1de41cbd5ffc46d4b3ef225bf6deedd9
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-12 (2018)
Dynamin-like proteins (DLPs) such as the mitofusins form homotypic and heterotypic oligomers that bridge and fuse opposing membranes. Here, Liu, Noel and Low present the crystal structure of a bacterial DLP heterotypic pair, providing insights into t
Externí odkaz:
https://doaj.org/article/f1643599edcc4dc59aca5dbb3c15a920
Autor:
Martin Buck, Souvik Naskar, Buzz Baum, Jeffrey K. Noel, Jiwei Liu, Matteo Tassinari, Diorge P. Souza, Tom A. Williams, Harry H. Low, Olga Bohuszewicz
Publikováno v:
3673.e18
Cell
Liu, J, Tassinari, M, Souza, D, Naskar, S, Noel, J K, Bohuszewicz, O, Buck, M, Williams, T, Baum, B & Low, H H 2021, ' Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily ', Cell, vol. 184, no. 14, pp. 3660-3673.e18 . https://doi.org/10.1016/j.cell.2021.05.041
Cell
Liu, J, Tassinari, M, Souza, D, Naskar, S, Noel, J K, Bohuszewicz, O, Buck, M, Williams, T, Baum, B & Low, H H 2021, ' Bacterial Vipp1 and PspA are members of the ancient ESCRT-III membrane-remodeling superfamily ', Cell, vol. 184, no. 14, pp. 3660-3673.e18 . https://doi.org/10.1016/j.cell.2021.05.041
Summary Membrane remodeling and repair are essential for all cells. Proteins that perform these functions include Vipp1/IM30 in photosynthetic plastids, PspA in bacteria, and ESCRT-III in eukaryotes. Here, using a combination of evolutionary and stru
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::83d3faeffb9ab8a6a6d378438d49062c
http://hdl.handle.net/10044/1/90126
http://hdl.handle.net/10044/1/90126
Autor:
Martin Buck, Buzz Baum, Diorge P. Souza, Harry H. Low, Souvik Naskar, Matteo Tassinari, Tom A. Williams, Jiwei Liu, Olga Bohuszewicz, Jeffrey K. Noel
Membrane remodelling and repair are essential for all cells. Proteins that perform these functions include Vipp1/IM30 in photosynthetic plastids, PspA in bacteria, CdvB in TACK archaea and ESCRT-III in eukaryotes. Here, we show that these protein fam
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::365e5df297a7c27393dd65f346971bdc
https://doi.org/10.1101/2020.08.13.249979
https://doi.org/10.1101/2020.08.13.249979
Autor:
Harry H. Low, Olga Bohuszewicz
Publikováno v:
Nature structural & molecular biology
Dynamin 1-like proteins (DNM1-L) are mechanochemical GTPases that induce membrane fission in mitochondria and peroxisomes. Their mechanism depends on conformational changes driven by nucleotide and lipid cycling. Here we show the crystal structure of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::97440fab1c34f56dabc2ae0ef8da3c05
http://europepmc.org/articles/PMC6104806
http://europepmc.org/articles/PMC6104806
Autor:
Jenny E. Hinshaw, Thomas D. Pollard, Vadim A. Frolov, Oliver Daumke, Adam Frost, Pietro De Camilli, Harry H. Low, Elizabeth H. Chen, Tom Kirchhausen, Martin Lenz, Christopher G. Burd, Sandra L. Schmid, Harvey T. McMahon, Philip Robinson, Aurélien Roux, Bruno Antonny, Michael M. Kozlov, Katja Faelber, Marijn G. J. Ford, Christien J. Merrifield
Publikováno v:
EMBO Journal
EMBO Journal, EMBO Press, 2016, 35 (21), pp.2270-2284. ⟨10.15252/embj.201694613⟩
EMBO Journal, 2016, 35 (21), pp.2270-2284. ⟨10.15252/embj.201694613⟩
EMBO Journal, Vol. 35, No 21 (2016) pp. 2270-2284
The EMBO Journal
Europe PubMed Central
EMBO J
EMBO Journal, EMBO Press, 2016, 35 (21), pp.2270-2284. ⟨10.15252/embj.201694613⟩
EMBO Journal, 2016, 35 (21), pp.2270-2284. ⟨10.15252/embj.201694613⟩
EMBO Journal, Vol. 35, No 21 (2016) pp. 2270-2284
The EMBO Journal
Europe PubMed Central
EMBO J
The large GTPase dynamin is the first protein shown to catalyze membrane fission. Dynamin and its related proteins are essential to many cell functions, from endocytosis to organelle division and fusion, and it plays a critical role in many physiolog
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ed5c546e5c13240d1a13229952065bb6
https://hal.archives-ouvertes.fr/hal-01597491
https://hal.archives-ouvertes.fr/hal-01597491
Autor:
Jan Löwe, Harry H. Low
Publikováno v:
Nature. 444:766-769
Dynamins form a superfamily of large mechano-chemical GTPases that includes the classical dynamins and dynamin-like proteins (DLPs)1. They are found throughout the Eukarya, functioning in core cellular processes such as endocytosis and organelle divi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::894742405e304d67b65eafc8a415cdb2
https://doi.org/10.1038/nature05312
https://doi.org/10.1038/nature05312