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001     1049088
005     20260108204822.0
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024 7 _ |a 10.34734/FZJ-2025-05180
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100 1 _ |a Hudina, Esther
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245 _ _ |a Plastizität bakterieller ESCRT-III-Strukturen bei der Membranremodellierung
260 _ _ |a Heidelberg
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520 _ _ |a Bacterial ESCRT-III proteins protect and maintain the structural integrity of prokaryotic membranes. Cryo-electron microscopy studies of ESCRT-III family members PspA and Vipp1 revealed the structural basis of helical rod, ring and stacked ring assembly formation. Although the basic ESCRT-III fold remained conserved in the observed structures, monomers adopted a remarkable degree of structural plasticity. Minor conformational changes resulted in major shifts in assembly architectures and are important for the ability to remodel membranes.
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700 1 _ |a Junglas, Benedikt
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700 1 _ |a Sachse, Carsten
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773 _ _ |a 10.1007/s12268-025-2597-3
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856 4 _ |u https://juser.fz-juelich.de/record/1049088/files/Hudina%2C%20Plastizit%C3%A4t%20bakterieller%20ESCRT-III-Strukturen.pdf
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