@phdthesis{dissertation,
	author = {Wehmer, Marc Alexander},
	title = {The conformational landscape of the AAA<sup>+</sup>-ATPase of the 26S proteasome studied by cryo-electron microscopy},
	year = {2017},
	school = {Technische Universität München},
	pages = {87},
	language = {en},
	abstract = {In eukaryotic cells selective protein degradation is mediated by the 26S proteasome. The proteasomal AAA<sup>+</sup>-ATPase unfolds substrates into the core particle, where proteolysis takes place. Applying single-particle cryo-electron microscopy and image classification to samples in the presence of different nucleotides and nucleotide analogs, we were able to observe four distinct conformational states. In a hitherto unobserved state (s4) the gate of the core particle is open. The resolution of the four conformers allowed for the construction of atomic models of the AAA<sup>+</sup>-ATPase module as it progresses through the functional cycle.},
	keywords = {},
	note = {},
	url = {https://mediatum.ub.tum.de/1364110},
}