title: Force generation: ATP-powered proteasomes pull the rope.
abstract: Recently, single-molecule force spectroscopy techniques have provided unprecedented opportunities to apply and to quantify forces that guide protein (un-)folding. A new study provides fascinating insights into the sophisticated mechanism by which an ATP-fueled proteolytic machine generates mechanical forces to unfold and translocate multidomain substrates.
authors.affiliation: Institute of Condensed Matter and Nanosciences, Université catholique de Louvain, Croix du Sud 2/18, B-1348 Louvain-la-Neuve, Belgium. Yves.Dufrene@uclouvain.be
authors.forename: Yves F
authors.initials: YF
authors.lastname: Dufrêne
authors.forename: Daniel J
authors.initials: DJ
authors.lastname: Müller
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D049071:Endopeptidase Clp / Q000502:physiology*; D008954:Models, Biological; D046988:Proteasome Endopeptidase Complex / Q000502:physiology*; D021381:Protein Transport; D058767:Protein Unfolding; D015398:Signal Transduction
chemical_list: D000255:Adenosine Triphosphate; D049071:Endopeptidase Clp; D046988:Proteasome Endopeptidase Complex