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Volumn 113, Issue 10, 2000, Pages 1783-1791

Disassembly of membrane-associated NSF 20S complexes is slow relative to vesicle fusion and is Ca2+-independent

Author keywords

AAA; Exocytosis; Fusion; SNARE; Synaptic vesicle

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CALCIUM ION; HYBRID PROTEIN; N ETHYLMALEIMIDE;

EID: 0034029072     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (9)

References (58)
  • 1
    • 0030682481 scopus 로고    scopus 로고
    • Stimulation of NSF ATPase activity by α-SNAP is required for SNARE complex disassembly and exocytosis
    • Barnard, R. O., Morgan, A. and Burgoyne, R. D. (1997). Stimulation of NSF ATPase activity by α-SNAP is required for SNARE complex disassembly and exocytosis. J. Cell Biol. 139, 875-883.
    • (1997) J. Cell Biol. , vol.139 , pp. 875-883
    • Barnard, R.O.1    Morgan, A.2    Burgoyne, R.D.3
  • 2
    • 0024366008 scopus 로고
    • Synaptobrevin: An integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain
    • Baumert, M., Maycox, P. R., Navone, F., De Camilli, P. and Jahn, R. (1989). Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain. EMBO J. 8, 379-384.
    • (1989) EMBO J. , vol.8 , pp. 379-384
    • Baumert, M.1    Maycox, P.R.2    Navone, F.3    De Camilli, P.4    Jahn, R.5
  • 3
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett, M. K., Calakos, N. and Scheller, R. H. (1992). Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 257, 255-259.
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 5
    • 0030009722 scopus 로고    scopus 로고
    • Use of photocrosslinkers in cell biology
    • Brunner, J. (1996). Use of photocrosslinkers in cell biology. Trends Cell Biol. 6, 154-157.
    • (1996) Trends Cell Biol. , vol.6 , pp. 154-157
    • Brunner, J.1
  • 6
    • 0028978441 scopus 로고
    • Real-time measurement of transmitter release from single synaptic vesicles
    • Bruns, D. and Jahn, R. (1995). Real-time measurement of transmitter release from single synaptic vesicles. Nature 377, 62-65.
    • (1995) Nature , vol.377 , pp. 62-65
    • Bruns, D.1    Jahn, R.2
  • 7
    • 0032054866 scopus 로고    scopus 로고
    • Analysis of regulated exocytosis in adrenal chromaffin cells: Insights into NSF/SNAP/SNARE function
    • Burgoyne, R. D. and Morgan, A. (1998). Analysis of regulated exocytosis in adrenal chromaffin cells: insights into NSF/SNAP/SNARE function. BioEssays 20, 328-335.
    • (1998) BioEssays , vol.20 , pp. 328-335
    • Burgoyne, R.D.1    Morgan, A.2
  • 9
    • 0025359065 scopus 로고
    • SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast
    • Clary, D. O., Griff, I. C. and Rothman, J. E. (1990). SNAPs, a family of NSF attachment proteins involved in intracellular membrane fusion in animals and yeast. Cell 61, 709-721.
    • (1990) Cell , vol.61 , pp. 709-721
    • Clary, D.O.1    Griff, I.C.2    Rothman, J.E.3
  • 11
    • 0030735370 scopus 로고    scopus 로고
    • Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation
    • Fasshauer, D., Otto, H., Eliason, W. K., Jahn, R. and Brünger, A. T. (1997). Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation. J. Biol. Chem. 272, 28036-28041.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28036-28041
    • Fasshauer, D.1    Otto, H.2    Eliason, W.K.3    Jahn, R.4    Brünger, A.T.5
  • 12
    • 0032430423 scopus 로고    scopus 로고
    • Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs
    • Fasshauer, D., Sutton, R. B., Brunger, A. T. and Jahn, R. (1998). Conserved structural features of the synaptic fusion complex: SNARE proteins reclassified as Q- and R-SNAREs. Proc. Nat. Acad. Sci. USA 95, 15781-15786.
    • (1998) Proc. Nat. Acad. Sci. USA , vol.95 , pp. 15781-15786
    • Fasshauer, D.1    Sutton, R.B.2    Brunger, A.T.3    Jahn, R.4
  • 13
    • 0025986155 scopus 로고
    • Probing the molecular environment of translocating polypeptide chains by cross-linking
    • Görlich, D., Kurzchalia, T. V., Wiedmann, M. and Rapoport, T. A. (1991). Probing the molecular environment of translocating polypeptide chains by cross-linking. Meth. Cell Biol. 34, 241-262.
    • (1991) Meth. Cell Biol. , vol.34 , pp. 241-262
    • Görlich, D.1    Kurzchalia, T.V.2    Wiedmann, M.3    Rapoport, T.A.4
  • 14
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P. I., Roth, R., Morisaki, R., Jahn, R. and Heuser, J. E. (1997). Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell 90, 523-536.
    • (1997) Cell , vol.90 , pp. 523-536
    • Hanson, P.I.1    Roth, R.2    Morisaki, R.3    Jahn, R.4    Heuser, J.E.5
  • 15
    • 0030796026 scopus 로고    scopus 로고
    • SNAREs and NSF in targeted membrane fusion
    • Hay, J. C. and Scheller, R. H. (1997). SNAREs and NSF in targeted membrane fusion. Curr. Opin. Cell Biol. 9, 505-512.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 505-512
    • Hay, J.C.1    Scheller, R.H.2
  • 16
    • 0028130728 scopus 로고
    • Synaptic vesicle membrane fusion complex: Action of clostridial neurotoxins on assembly
    • Hayashi, T., McMahon, H., Yamasaki, S., Binz, T., Hata, Y., Südhof, T. C. and Niemann, H. (1994). Synaptic vesicle membrane fusion complex: action of clostridial neurotoxins on assembly. EMBO J. 13, 5051-5061.
    • (1994) EMBO J. , vol.13 , pp. 5051-5061
    • Hayashi, T.1    McMahon, H.2    Yamasaki, S.3    Binz, T.4    Hata, Y.5    Südhof, T.C.6    Niemann, H.7
  • 17
    • 0029004741 scopus 로고
    • Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro
    • Hayashi, T., Yamasaki, S., Nauenburg, S., Binz, T. and Niemann, H. (1995). Disassembly of the reconstituted synaptic vesicle membrane fusion complex in vitro. EMBO J. 14, 2317-2325.
    • (1995) EMBO J. , vol.14 , pp. 2317-2325
    • Hayashi, T.1    Yamasaki, S.2    Nauenburg, S.3    Binz, T.4    Niemann, H.5
  • 18
    • 0032566741 scopus 로고    scopus 로고
    • Stimulation of NSF ATPase activity during t-SNARE priming
    • Haynes, L. P., Barnard, R. J. O., Morgan, A. and Burgoyne, R. D. (1998). Stimulation of NSF ATPase activity during t-SNARE priming. FEBS Lett. 436, 1-5.
    • (1998) FEBS Lett. , vol.436 , pp. 1-5
    • Haynes, L.P.1    Barnard, R.J.O.2    Morgan, A.3    Burgoyne, R.D.4
  • 19
    • 0028023444 scopus 로고
    • Calcium dependence of the rate of exocytosis in a synaptic terminal
    • Heidelberger, R., Heinemann, C., Neher, E. and Matthews, G. (1994). Calcium dependence of the rate of exocytosis in a synaptic terminal. Nature 371, 513-515.
    • (1994) Nature , vol.371 , pp. 513-515
    • Heidelberger, R.1    Heinemann, C.2    Neher, E.3    Matthews, G.4
  • 20
    • 0033361978 scopus 로고    scopus 로고
    • Coupling calcium to SNARE-mediated synaptic vesicle fusion
    • Hilfiker, S., Greengard, P. and Augustine, G. J. (1999). Coupling calcium to SNARE-mediated synaptic vesicle fusion. Nature Neurosci. 2, 104-106.
    • (1999) Nature Neurosci. , vol.2 , pp. 104-106
    • Hilfiker, S.1    Greengard, P.2    Augustine, G.J.3
  • 21
    • 0032214690 scopus 로고    scopus 로고
    • Arrangement of subunits in 20S particles consisting of NSF, SNAPs, and SNARE complexes
    • Hohl, T. M., Parlati, F., Wimmer, C., Rothman, J. E., Söllner, T. H. and Engelhardt, H. (1998). Arrangement of subunits in 20S particles consisting of NSF, SNAPs, and SNARE complexes. Mol. Cell 2, 539-548.
    • (1998) Mol. Cell , vol.2 , pp. 539-548
    • Hohl, T.M.1    Parlati, F.2    Wimmer, C.3    Rothman, J.E.4    Söllner, T.H.5    Engelhardt, H.6
  • 22
    • 0033611492 scopus 로고    scopus 로고
    • Membrane fusion: Structure snared at last
    • Hughson, F. M. (1999). Membrane fusion: structure snared at last. Curr. Biol. 9, R49-R52.
    • (1999) Curr. Biol. , vol.9
    • Hughson, F.M.1
  • 23
    • 0033366466 scopus 로고    scopus 로고
    • Snapin: A SNARE-associated protein implicated in synaptic transmission
    • Ilardi, J. M., Mochida, S. and Sheng, Z.-H. (1999). Snapin: a SNARE-associated protein implicated in synaptic transmission. Nature Neurosci. 2, 119-124.
    • (1999) Nature Neurosci. , vol.2 , pp. 119-124
    • Ilardi, J.M.1    Mochida, S.2    Sheng, Z.-H.3
  • 24
    • 0005614190 scopus 로고
    • Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle
    • Krieg, U. C., Walter, P. and Johnson, A. E. (1986). Photocrosslinking of the signal sequence of nascent preprolactin to the 54-kilodalton polypeptide of the signal recognition particle. Proc. Nat. Acad. Sci. USA 83, 8604-8608.
    • (1986) Proc. Nat. Acad. Sci. USA , vol.83 , pp. 8604-8608
    • Krieg, U.C.1    Walter, P.2    Johnson, A.E.3
  • 25
    • 0033163807 scopus 로고    scopus 로고
    • Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein
    • May, A. P., Misura, K. M. S., Whiteheart, S. W. and Weiss, W. I. (1999). Crystal structure of the amino-terminal domain of N-ethylmaleimide-sensitive fusion protein. Nature Cell Biol. 1, 175-182.
    • (1999) Nature Cell Biol. , vol.1 , pp. 175-182
    • May, A.P.1    Misura, K.M.S.2    Whiteheart, S.W.3    Weiss, W.I.4
  • 26
    • 0029980441 scopus 로고    scopus 로고
    • SEC18p (NSF) - Driven release of SEC17p (α-SNAP) can precede docking and fusion of yeast vacuoles
    • Mayer, A., Wickner, W. and Haas, A. (1996). SEC18p (NSF) - driven release of SEC17p (α-SNAP) can precede docking and fusion of yeast vacuoles. Cell 85, 83-94.
    • (1996) Cell , vol.85 , pp. 83-94
    • Mayer, A.1    Wickner, W.2    Haas, A.3
  • 31
    • 0030860083 scopus 로고    scopus 로고
    • The diversity of Rab proteins in vesicle transport
    • Novick, P. and Zerial, M. (1997). The diversity of Rab proteins in vesicle transport. Curr. Opin. Cell Biol. 9, 496-504.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 496-504
    • Novick, P.1    Zerial, M.2
  • 32
    • 0028294018 scopus 로고
    • Synaptic vesicle exocytosis: Molecules and models
    • O'Connor, V., Augustine, G. J. and Betz, H. (1994). Synaptic vesicle exocytosis: molecules and models. Cell 76, 785-787.
    • (1994) Cell , vol.76 , pp. 785-787
    • O'Connor, V.1    Augustine, G.J.2    Betz, H.3
  • 33
    • 0033560750 scopus 로고    scopus 로고
    • Cytosolic ATPases, p97 and NSF, are sufficient to mediate rapid membrane fusion
    • Otter-Nilsson, M., Hendriks, R., Pecheur-Huet, E.-I., Hoekstra, D. and Nilsson, T. (1999). Cytosolic ATPases, p97 and NSF, are sufficient to mediate rapid membrane fusion. EMBO J. 18, 2074-2083.
    • (1999) EMBO J. , vol.18 , pp. 2074-2083
    • Otter-Nilsson, M.1    Hendriks, R.2    Pecheur-Huet, E.-I.3    Hoekstra, D.4    Nilsson, T.5
  • 34
    • 0030954439 scopus 로고    scopus 로고
    • Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesicles
    • Otto, H., Hanson, P. I. and Jahn, R. (1997). Assembly and disassembly of a ternary complex of synaptobrevin, syntaxin, and SNAP-25 in the membrane of synaptic vesicles. Proc. Nat. Acad. Sci. USA 94, 6197-6120.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 6197-16120
    • Otto, H.1    Hanson, P.I.2    Jahn, R.3
  • 35
    • 0024828306 scopus 로고
    • The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations
    • Oyler, G. A., Higgins, G. A., Hart, R. A., Battenberg, E., Billingsley, M., Bloom, F. E. and Wilson, M. C. (1989). The identification of a novel synaptosomal-associated protein, SNAP-25, differentially expressed by neuronal subpopulations. J. Cell Biol. 109, 3039-3052.
    • (1989) J. Cell Biol. , vol.109 , pp. 3039-3052
    • Oyler, G.A.1    Higgins, G.A.2    Hart, R.A.3    Battenberg, E.4    Billingsley, M.5    Bloom, F.E.6    Wilson, M.C.7
  • 36
    • 0026680746 scopus 로고
    • Mutational analysis of a DEAD box RNA helicase: The mammalian translation initiation factor eIF-4A
    • Pause, A. and Sonenberg, N. (1992). Mutational analysis of a DEAD box RNA helicase: the mammalian translation initiation factor eIF-4A. EMBO J. 11, 2643-2654.
    • (1992) EMBO J. , vol.11 , pp. 2643-2654
    • Pause, A.1    Sonenberg, N.2
  • 37
    • 0027946206 scopus 로고
    • Fusion complex formation protects synaptobrevin against proteolysis by tetanus toxin light chain
    • Pellegrini, L. L., O'Connor, V. and Betz, H. (1994). Fusion complex formation protects synaptobrevin against proteolysis by tetanus toxin light chain. FEBS Lett. 353, 319-323.
    • (1994) FEBS Lett. , vol.353 , pp. 319-323
    • Pellegrini, L.L.1    O'Connor, V.2    Betz, H.3
  • 38
    • 0032506349 scopus 로고    scopus 로고
    • 2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion
    • 2+/calmodulin signals the completion of docking and triggers a late step of vacuole fusion. Nature 396, 575-580.
    • (1998) Nature , vol.396 , pp. 575-580
    • Peters, C.1    Mayer, A.2
  • 39
    • 0033130103 scopus 로고    scopus 로고
    • Transport-vesicle targeting: Tethers before SNAREs
    • Pfeffer, S. R. (1999). Transport-vesicle targeting: tethers before SNAREs. Nature Cell Biol. 1, E17-E22.
    • (1999) Nature Cell Biol. , vol.1
    • Pfeffer, S.R.1
  • 41
    • 0028143698 scopus 로고
    • Mechanism of intracellular protein transport
    • Rothman, J. E. (1994). Mechanism of intracellular protein transport. Nature 372, 55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 42
    • 0028385277 scopus 로고
    • Implications of the SNARE hypothesis for intracellular membrane topology and dynamics
    • Rothman, J. E. and Warren, G. (1994). Implications of the SNARE hypothesis for intracellular membrane topology and dynamics. Curr. Biol. 4, 220-223.
    • (1994) Curr. Biol. , vol.4 , pp. 220-223
    • Rothman, J.E.1    Warren, G.2
  • 43
    • 0031019926 scopus 로고    scopus 로고
    • Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses
    • Schiavo, G., Stenbeck, G., Rothman, J. E. and Söllner, T. H. (1997). Binding of the synaptic vesicle v-SNARE, synaptotagmin, to the plasma membrane t-SNARE, SNAP-25, can explain docked vesicles at neurotoxin-treated synapses. Proc. Nat. Acad. Sci. USA 94, 997-1001.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 997-1001
    • Schiavo, G.1    Stenbeck, G.2    Rothman, J.E.3    Söllner, T.H.4
  • 44
    • 0026635622 scopus 로고
    • CHELATOR: An improved method for computing metal ion concentrations in physiological solutions
    • Schoenmakers, T. J. M., Visser, G. J., Flik, G. and Theuvenet, A. P. R. (1992). CHELATOR: an improved method for computing metal ion concentrations in physiological solutions. BioTechniques 12, 870-879.
    • (1992) BioTechniques , vol.12 , pp. 870-879
    • Schoenmakers, T.J.M.1    Visser, G.J.2    Flik, G.3    Theuvenet, A.P.R.4
  • 46
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular and viral membrane fusion
    • Skehel, J. J. and Wiley, D. C. (1998). Coiled coils in both intracellular and viral membrane fusion. Cell 95, 871-874.
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 47
    • 0027517462 scopus 로고
    • A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion
    • Söllner, T., Bennett, M. K., Whiteheart, S. W., Scheller, R. H. and Rothman, J. E. (1993a). A protein assembly-disassembly pathway in vitro that may correspond to sequential steps of synaptic vesicle docking, activation, and fusion. Cell 75, 409-418.
    • (1993) Cell , vol.75 , pp. 409-418
    • Söllner, T.1    Bennett, M.K.2    Whiteheart, S.W.3    Scheller, R.H.4    Rothman, J.E.5
  • 49
    • 0029143193 scopus 로고
    • SNAREs and targeted membrane fusion
    • Söllner, T. (1995). SNAREs and targeted membrane fusion. FEBS Letts. 369, 80-83.
    • (1995) FEBS Letts. , vol.369 , pp. 80-83
    • Söllner, T.1
  • 50
    • 0031847684 scopus 로고    scopus 로고
    • Formation and turnover of NSF- and SNAP-containing "fusion" complexes occur on undocked, clathrin-coated vesicle-derived membranes
    • Swanton, E., Sheehan, J., Bishop, N., High, S. and Woodman, P. (1998). Formation and turnover of NSF- and SNAP-containing "fusion" complexes occur on undocked, clathrin-coated vesicle-derived membranes. Mol. Biol. Cell 9, 1633-1647.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1633-1647
    • Swanton, E.1    Sheehan, J.2    Bishop, N.3    High, S.4    Woodman, P.5
  • 51
    • 0032509210 scopus 로고    scopus 로고
    • Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion
    • Tahara, M., Coorsen, J. R., Timmers, K., Blank, P. S., Whalley, T., Scheller, R. and Zimmerberg, J. (1998). Calcium can disrupt the SNARE protein complex on sea urchin egg secretory vesicles without irreversibly blocking fusion. J. Biol. Chem. 273, 33667-33673.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33667-33673
    • Tahara, M.1    Coorsen, J.R.2    Timmers, K.3    Blank, P.S.4    Whalley, T.5    Scheller, R.6    Zimmerberg, J.7
  • 52
    • 0006602702 scopus 로고
    • VAMP-1: A synaptic vesicle-associated integral membrane protein
    • Trimble, W. S., Cowan, D. M. and Scheller, R. H. (1988). VAMP-1: A synaptic vesicle-associated integral membrane protein. Proc. Nat. Acad. Sci. USA 85, 4538-4542.
    • (1988) Proc. Nat. Acad. Sci. USA , vol.85 , pp. 4538-4542
    • Trimble, W.S.1    Cowan, D.M.2    Scheller, R.H.3
  • 53
    • 0032506543 scopus 로고    scopus 로고
    • Defining the functions of trans-SNARE pairs
    • Ungermann, C., Sato, K. and Wickner, W. (1998). Defining the functions of trans-SNARE pairs. Nature 396, 543-548.
    • (1998) Nature , vol.396 , pp. 543-548
    • Ungermann, C.1    Sato, K.2    Wickner, W.3
  • 55
    • 0028132782 scopus 로고
    • N-ethylmaleimide-sensitive fusion protein: A trimeric ATPase whose hydrolysis of ATP is required for membrane fusion
    • ??-??
    • Whiteheart, S. W., Rossnagel, K., Buhrow, S. A., Brunner, M., Jaenicke, R. and Rothman, J. E. (1994). N-ethylmaleimide-sensitive fusion protein: a trimeric ATPase whose hydrolysis of ATP is required for membrane fusion. J. Cell Biol. 126, ??-??.
    • (1994) J. Cell Biol. , vol.126
    • Whiteheart, S.W.1    Rossnagel, K.2    Buhrow, S.A.3    Brunner, M.4    Jaenicke, R.5    Rothman, J.E.6
  • 56
    • 0030992881 scopus 로고    scopus 로고
    • The roles of NSF, SNAPs and SNAREs during membrane fusion
    • Woodman, P. G. (1997). The roles of NSF, SNAPs and SNAREs during membrane fusion. Biochem. Biophys. Acta 1357, 155-172.
    • (1997) Biochem. Biophys. Acta , vol.1357 , pp. 155-172
    • Woodman, P.G.1
  • 57
    • 33644681150 scopus 로고    scopus 로고
    • Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity
    • Xu, T., Binz, T., Niemann, H. and Neher, E. (1998). Multiple kinetic components of exocytosis distinguished by neurotoxin sensitivity. Nature Neurosci. 1, 192-200.
    • (1998) Nature Neurosci. , vol.1 , pp. 192-200
    • Xu, T.1    Binz, T.2    Niemann, H.3    Neher, E.4
  • 58
    • 0033564814 scopus 로고    scopus 로고
    • Early requirement for α-SNAP and NSF in the secretory cascade in chromaffin cells
    • Xu, T., Ashery, U., Burgoyne, R. D. and Neher, E. (1999). Early requirement for α-SNAP and NSF in the secretory cascade in chromaffin cells. EMBO J. 18, 3293-3304.
    • (1999) EMBO J. , vol.18 , pp. 3293-3304
    • Xu, T.1    Ashery, U.2    Burgoyne, R.D.3    Neher, E.4


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