The N-terminal domain of the t-SNARE Vam3p coordinates priming and docking in yeast vacuole fusion.
Laage R, Ungermann C, Mol Biol Cell, 2001 Nov - link

A new role for a SNARE protein as a regulator of the Ypt7/Rab-dependent stage of docking.
Ungermann C, Price A, Wickner W, Proc Natl Acad Sci U S A, 2000 Aug 1 - link

The docking of primed vacuoles can be reversibly arrested by excess Sec17p (alpha-SNAP).
Wang L, Ungermann C, Wickner W, J Biol Chem, 2000 Jul 28 - link

The docking stage of yeast vacuole fusion requires the transfer of proteins from a cis-SNARE complex to a Rab/Ypt protein.
Price A, Seals D, Wickner W, Ungermann C, J Cell Biol, 2000 Mar 20 - link

Proteins needed for vesicle budding from the Golgi complex are also required for the docking step of homotypic vacuole fusion.
Price A, Wickner W, Ungermann C, J Cell Biol, 2000 Mar 20 - link

Vam7p, a vacuolar SNAP-25 homolog, is required for SNARE complex integrity and vacuole docking and fusion.
Ungermann C, Wickner W, EMBO J, 1998 Jun 15 - link

A vacuolar v-t-SNARE complex, the predominant form in vivo and on isolated vacuoles, is disassembled and activated for docking and fusion.
Ungermann C, Nichols BJ, Pelham HR, Wickner W, J Cell Biol, 1998 Jan 12 - link