Three αSNAP and 10 ATP Molecules Are Used in SNARE Complex Disassembly byN-ethylmaleimide-sensitive Factor (NSF)

Disassembly of All SNARE Complexes byN-Ethylmaleimide-sensitive Factor (NSF) Is Initiated by a Conserved 1:1 Interaction between α-Soluble NSF Attachment Protein (SNAP) and SNARE Complex

(2013) Sandro Vivona et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Processive ATP-driven Substrate Disassembly by theN-Ethylmaleimide-sensitive Factor (NSF) Molecular Machine

(2013) Daniel J. Cipriano et al.   JOURNAL OF BIOLOGICAL CHEMISTRY

Nucleotide-dependent conformational changes in the N-Ethylmaleimide Sensitive Factor (NSF) and their potential role in SNARE complex disassembly

(2012) Arne Moeller et al.   JOURNAL OF STRUCTURAL BIOLOGY

Structural characterization of full-length NSF and 20S particles

(2012) Lei-Fu Chang et al.   NATURE STRUCTURAL & MOLECULAR BIOLOGY

Single Reconstituted Neuronal SNARE Complexes Zipper in Three Distinct Stages

(2012) Y. Gao et al.   SCIENCE

A Conserved Membrane Attachment Site in α-SNAP FacilitatesN-Ethylmaleimide-sensitive Factor (NSF)-driven SNARE Complex Disassembly

(2009) Ulrike Winter et al.   JOURNAL OF BIOLOGICAL CHEMISTRY