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Proceedings of the National Academy of Sciences of the United States of America|November 6, 2019
Sec17 (α-SNAP) and Sec18 (NSF) restrict membrane fusion to R-SNAREs, Q-SNAREs, and SM proteins from identical compartmentsYoungsoo Jun, William WicknerMolecular Biology of the Cell|March 16, 2017
A cascade of multiple proteins and lipids catalyzes membrane fusionWilliam Wickner, Josep RizoScience (New York, N.Y.)|December 3, 2005
Protein translocation across biological membranesWilliam Wickner, Randy SchekmanMolecular Biology of the Cell|March 27, 2024
Sec18 binds the tethering/SM complex HOPS to engage the Qc-SNARE for membrane fusionAmy Orr, William WicknerThe Journal of Biological Chemistry|December 7, 2017
Assembly of intermediates for rapid membrane fusionMax Harner, William WicknerMolecular Biology of the Cell|October 4, 2013
The tethering complex HOPS catalyzes assembly of the soluble SNARE Vam7 into fusogenic trans-SNARE complexesMichael Zick, William WicknerProceedings of the National Academy of Sciences of the United States of America|August 1, 2007
Assays of vacuole fusion resolve the stages of docking, lipid mixing, and content mixingYoungsoo Jun, William WicknerMolecular Biology of the Cell|May 14, 2010
HOPS initiates vacuole docking by tethering membranes before trans-SNARE complex assemblyChristopher M Hickey, William WicknerThe Journal of Biological Chemistry|March 10, 2007
Distinct targeting and fusion functions of the PX and SNARE domains of yeast vacuolar Vam7pRutilio A Fratti, William WicknerBiorxiv : the Preprint Server for Biology|November 28, 2024
Membrane fusion reactions limited by defective SNARE zippering or stiff lipid fatty acyl composition have distinct requirements for Sec17, Sec18, and adenine nucleotideKarina Lopes, Amy Orr, William WicknerPageof 389