Primary Literature
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- Yue P, et al. (2017) Sec3 promotes the initial binary t-SNARE complex assembly and membrane fusion. Nat Commun 8:14236 PMID: 28112172
- Hong W and Lev S (2014) Tethering the assembly of SNARE complexes. Trends Cell Biol 24(1):35-43 PMID: 24119662
- Wickner W (2010) Membrane fusion: five lipids, four SNAREs, three chaperones, two nucleotides, and a Rab, all dancing in a ring on yeast vacuoles. Annu Rev Cell Dev Biol 26:115-36 PMID: 20521906
- Mendonsa R and Engebrecht J (2009) Phosphatidylinositol-4,5-bisphosphate and phospholipase D-generated phosphatidic acid specify SNARE-mediated vesicle fusion for prospore membrane formation. Eukaryot Cell 8(8):1094-105 PMID: 19502581
- Liu S, et al. (2007) In vitro fusion catalyzed by the sporulation-specific t-SNARE light-chain Spo20p is stimulated by phosphatidic acid. Traffic 8(11):1630-43 PMID: 17714435
- Jahn R and Scheller RH (2006) SNAREs--engines for membrane fusion. Nat Rev Mol Cell Biol 7(9):631-43 PMID: 16912714
- Togneri J, et al. (2006) Specific SNARE complex binding mode of the Sec1/Munc-18 protein, Sec1p. Proc Natl Acad Sci U S A 103(47):17730-5 PMID: 17090679
- Marash M and Gerst JE (2001) t-SNARE dephosphorylation promotes SNARE assembly and exocytosis in yeast. EMBO J 20(3):411-21 PMID: 11157748
- McNew JA, et al. (2000) Compartmental specificity of cellular membrane fusion encoded in SNARE proteins. Nature 407(6801):153-9 PMID: 11001046
- Fiebig KM, et al. (1999) Folding intermediates of SNARE complex assembly. Nat Struct Biol 6(2):117-23 PMID: 10048921
- Lehman K, et al. (1999) Yeast homologues of tomosyn and lethal giant larvae function in exocytosis and are associated with the plasma membrane SNARE, Sec9. J Cell Biol 146(1):125-40 PMID: 10402465
- Nicholson KL, et al. (1998) Regulation of SNARE complex assembly by an N-terminal domain of the t-SNARE Sso1p. Nat Struct Biol 5(9):793-802 PMID: 9731774
- Rossi G, et al. (1997) Analysis of a yeast SNARE complex reveals remarkable similarity to the neuronal SNARE complex and a novel function for the C terminus of the SNAP-25 homolog, Sec9. J Biol Chem 272(26):16610-7 PMID: 9195974
- Brennwald P, et al. (1994) Sec9 is a SNAP-25-like component of a yeast SNARE complex that may be the effector of Sec4 function in exocytosis. Cell 79(2):245-58 PMID: 7954793
- Couve A and Gerst JE (1994) Yeast Snc proteins complex with Sec9. Functional interactions between putative SNARE proteins. J Biol Chem 269(38):23391-4 PMID: 8089101