The Docking of Primed Vacuoles Can Be Reversibly Arrested by Excess Sec17p (α-SNAP)

This publication has 30 references indexed in Scilit:

• Three v-SNAREs and Two t-SNAREs, Present in a Pentameric cis-SNARE Complex on Isolated Vacuoles, Are Essential for Homotypic Fusion
  The Journal of cell biology, 1999
• Membrane Fusion and Exocytosis
  Annual Review of Biochemistry, 1999
• The Rab5 effector EEA1 is a core component of endosome docking
  Nature, 1999
• Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
  Nature, 1998
• Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion
  The EMBO Journal, 1998
• A Vacuolar v–t-SNARE Complex, the Predominant Form In Vivo and on Isolated Vacuoles, Is Disassembled and Activated for Docking and Fusion
  The Journal of cell biology, 1998
• The diversity of Rab proteins in vesicle transport
  Current Opinion in Cell Biology, 1997
• Homotypic vacuolar fusion mediated by t- and v-SNAREs
  Nature, 1997
• Sec18p (NSF)-Driven Release of Sec17p (α-SNAP) Can Precede Docking and Fusion of Yeast Vacuoles
  Published by Elsevier ,1996
• A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
  Cell, 1993