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- W2893703076 abstract "Abstract The dynamin superfamily of large GTPases comprises specialized members that catalyze fusion and fission of biological membranes. While fission-specific proteins such as dynamin work as homo-oligomeric complexes, many fusion catalysts such as mitofusins or bacterial dynamin-like proteins (DLPs) act as hetero-oligomers. However, so far it was unclear how these hetero-oligomeric DLPs assemble and how they function in membrane remodeling. The group of Harry Low report now on the structure of a DLP pair from Campylobacter jejuni , allowing detailed insight into the assembly mechanism and membrane tethering activity." @default.
- W2893703076 created "2018-10-05" @default.
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- W2893703076 date "2018-09-28" @default.
- W2893703076 modified "2023-10-12" @default.
- W2893703076 title "Bacterial dynamin-like proteins reveal mechanism for membrane fusion" @default.
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- W2893703076 doi "https://doi.org/10.1038/s41467-018-06559-6" @default.
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