[1] 诺贝尔奖官方网站:http://www.nobelprize.com.[2] Novick P, Ferro S, Schekman R. Order of events in the yeast secretory pathway[J]. Cell, 1981, 25(2): 461-469.[3] Novick P, Field C, Schekman R. Identification of 23 complementation groups required for post-translational events in the yeast secretory pathway[J]. Cell, 1980, 21(1): 205-215.[4] Novick P,Schekman R. Secretion and cell-surface growth are blocked in a temperature-sensitive mutant of Saccharomyces cerevisiae[J]. Proc Natl Acad Sci U S A, 1979, 76(4): 1858-1862.[5] Kaiser C A,Schekman R. Distinct sets of SEC genes govern transport vesicle formation and fusion early in the secretory pathway[J]. Cell, 1990, 61(4): 723-733.[6] Balch W E, Dunphy W G, Braell W A,et al. Reconstitution of the transport of protein between successive compartments of the Golgi measured by the coupled incorporation of N-acetylglucosamine[J]. Cell, 1984, 39(2 Pt 1): 405-416.[7] Balch W E, Glick B S, Rothman J E. Sequential intermediates in the pathway of intercompartmental transport in a cell-free system[J]. Cell, 1984, 39(3 Pt 2): 525-536.[8] Braell W A, Balch W E, Dobbertin D C,et al. The glycoprotein that is transported between successive compartments of the Golgi in a cell-free system resides in stacks of cisternae[J]. Cell, 1984, 39(3 Pt 2): 511-524.[9] Fries E,Rothman J E. Transport of vesicular stomatitis virus glycoprotein in a cell-free extract[J]. Proc Natl Acad Sci U S A, 1980, 77(7): 3870-3874.[10] Block M R, Glick B S, Wilcox C A,et al. Purification of an N-ethylmaleimide-sensitive protein catalyzing vesicular transport[J]. Proc Natl Acad Sci U S A, 1988, 85(21): 7852-7856.[11] Glick B S,Rothman J E. Possible role for fatty acyl-coenzyme A in intracellular protein transport[J]. Nature, 1987, 326(6110): 309-312.[12] Malhotra V, Orci L, Glick B S,et al. Role of an N-ethylmaleimide-sensitive transport component in promoting fusion of transport vesicles with cisternae of the Golgi stack[J]. Cell, 1988, 54(2): 221-227.[13] Clary D O, Griff I C, Rothman J E. SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast[J]. Cell, 1990, 61(4): 709-721.[14] Eakle K A, Bernstein M, Emr S D. Characterization of a component of the yeast secretion machinery: identification of the SEC18 gene product[J]. Mol Cell Biol, 1988, 8(10): 4098-4109.[15] Wilson D W, Wilcox C A, Flynn G C,et al. A fusion protein required for vesicle-mediated transport in both mammalian cells and yeast[J]. Nature, 1989, 339(6223): 355-359.[16] Griff I C, Schekman R, Rothman J E,et al. The yeast SEC17 gene product is functionally equivalent to mammalian alpha-SNAP protein[J]. J Biol Chem, 1992, 267(17): 12106-12115.[17] Sollner T, Whiteheart S W, Brunner M,et al. SNAP receptors implicated in vesicle targeting and fusion[J]. Nature, 1993, 362(6418): 318-324.[18] Weber T, Zemelman B V, McNew J A,et al. SNAREpins: minimal machinery for membrane fusion[J]. Cell, 1998, 92(6): 759-772.[19] McNew J A, Parlati F, Fukuda R,et al. Compartmental specificity of cellular membrane fusion encoded in SNARE proteins[J]. Nature, 2000, 407(6801): 153-159.[20] McMahon H T, Missler M, Li C,et al. Complexins: cytosolic proteins that regulate SNAP receptor function[J]. Cell, 1995, 83(1): 111-119.[21] Reim K, Mansour M, Varoqueaux F,et al. Complexins regulate a late step in Ca2+-dependent neurotransmitter release[J]. Cell, 2001, 104(1): 71-81.[22] Perin M S, Fried V A, Mignery G A,et al. Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C[J]. Nature, 1990, 345(6272): 260-263.[23] Geppert M, Goda Y, Hammer R E,et al. Synaptotagmin I: a major Ca2+ sensor for transmitter release at a central synapse[J]. Cell, 1994, 79(4): 717-727.[24] Fernandez-Chacon R, Konigstorfer A, Gerber S H,et al. Synaptotagmin I functions as a calcium regulator of release probability[J]. Nature, 2001, 410(6824): 41-49.[25] Hata Y, Slaughter C A, Sudhof T C. Synaptic vesicle fusion complex contains unc-18 homologue bound to syntaxin[J]. Nature, 1993, 366(6453): 347-351.[26] Verhage M, Maia A S, Plomp J J,et al. Synaptic assembly of the brain in the absence of neurotransmitter secretion[J]. Science, 2000, 287(5454): 864-869.[27] Schiavo G, Benfenati F, Poulain B,et al. Tetanus and botulinum-B neurotoxins block neurotransmitter release by proteolytic cleavage of synaptobrevin[J]. Nature, 1992, 359(6398): 832-835. |