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Volumn 89, Issue 1, 2005, Pages 690-702

Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEXIN; SNARE PROTEIN; SYNAPTOTAGMIN; UNCLASSIFIED DRUG;

EID: 23144455040     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.054064     Document Type: Article
Times cited : (85)

References (73)
  • 2
    • 0033616580 scopus 로고    scopus 로고
    • Single-pair fluorescence resonance energy transfer on freely diffusing molecules: Observation of Förster distance dependence and subpopulations
    • Deniz, A. A., M. Dahan, J. R. Grunwell, T. Ha, A. E. Faulhaber, D. S. Chemla, S. Weiss, and P. G. Schultz. 1999. Single-pair fluorescence resonance energy transfer on freely diffusing molecules: observation of Förster distance dependence and subpopulations. Proc. Natl. Acad. Sci. USA. 96:3670-3675.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3670-3675
    • Deniz, A.A.1    Dahan, M.2    Grunwell, J.R.3    Ha, T.4    Faulhaber, A.E.5    Chemla, D.S.6    Weiss, S.7    Schultz, P.G.8
  • 3
    • 14544283620 scopus 로고    scopus 로고
    • Polyproline and the "spectroscopic ruler" revisited with single-molecule fluorescence
    • Schuler, B., E. A. Lipman, P. J. Steinbach, M. Kumke, and W. A. Eaton. 2005. Polyproline and the "spectroscopic ruler" revisited with single-molecule fluorescence. Proc. Natl. Acad. Sci. USA. 102:2754-2759.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2754-2759
    • Schuler, B.1    Lipman, E.A.2    Steinbach, P.J.3    Kumke, M.4    Eaton, W.A.5
  • 4
    • 0036180593 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer (FRET) and competing processes in donor-acceptor substituted DNA strands: A comparative study of ensemble and single-molecule data
    • Dietrich, A., V. Buschmann, C. Muller, and M. Sauer. 2002. Fluorescence resonance energy transfer (FRET) and competing processes in donor-acceptor substituted DNA strands: a comparative study of ensemble and single-molecule data. Rev. Mol. Biotechnol. 82:211-231.
    • (2002) Rev. Mol. Biotechnol. , vol.82 , pp. 211-231
    • Dietrich, A.1    Buschmann, V.2    Muller, C.3    Sauer, M.4
  • 7
    • 3042735586 scopus 로고    scopus 로고
    • Placing single-molecule T4 lysozyme enzymes on a bacterial cell surface: Toward probing single-molecule enzymatic reaction in living cells
    • Hu, D., and H. P. Lu. 2004. Placing single-molecule T4 lysozyme enzymes on a bacterial cell surface: toward probing single-molecule enzymatic reaction in living cells. Biophys. J. 87:656-661.
    • (2004) Biophys. J. , vol.87 , pp. 656-661
    • Hu, D.1    Lu, H.P.2
  • 9
    • 1542501215 scopus 로고    scopus 로고
    • Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy
    • Talaga, D. S., W. L. Lau, H. Roder, J. Tang, Y. Jia, W. F. DeGrado, and R. M. Hochstrasser. 2000. Dynamics and folding of single two-stranded coiled-coil peptides studied by fluorescent energy transfer confocal microscopy. Proc. Natl. Acad. Sci. USA. 97:13021-13026.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13021-13026
    • Talaga, D.S.1    Lau, W.L.2    Roder, H.3    Tang, J.4    Jia, Y.5    Degrado, W.F.6    Hochstrasser, R.M.7
  • 10
    • 0345166865 scopus 로고    scopus 로고
    • Single-molecule studies of SNARE complex assembly reveal parallel and antiparallel configurations
    • Weninger, K., M. E. Bowen, S. Chu, and A. T. Brunger. 2003. Single-molecule studies of SNARE complex assembly reveal parallel and antiparallel configurations. Proc. Natl. Acad. Sci. USA. 100:14800-14805.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 14800-14805
    • Weninger, K.1    Bowen, M.E.2    Chu, S.3    Brunger, A.T.4
  • 11
    • 0041923728 scopus 로고    scopus 로고
    • The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer
    • Yasuda, R., T. Masaike, K. Adachi, H. Noji, H. Itoh, and K. Kinosita, Jr. 2003. The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. USA. 100:9314-9318.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 9314-9318
    • Yasuda, R.1    Masaike, T.2    Adachi, K.3    Noji, H.4    Itoh, H.5    Kinosita Jr., K.6
  • 12
    • 0042858417 scopus 로고    scopus 로고
    • Cell biology of the presynaptic terminal
    • Murthy, V. N., and P. De Camilli. 2003. Cell biology of the presynaptic terminal. Annu. Rev. Neurosci. 26:701-728.
    • (2003) Annu. Rev. Neurosci. , vol.26 , pp. 701-728
    • Murthy, V.N.1    De Camilli, P.2
  • 13
    • 0037459076 scopus 로고    scopus 로고
    • Membrane fusion
    • Jahn, R., T. Lang, and T. C. Sudhof. 2003. Membrane fusion. Cell. 112:519-533.
    • (2003) Cell , vol.112 , pp. 519-533
    • Jahn, R.1    Lang, T.2    Sudhof, T.C.3
  • 14
    • 0029990813 scopus 로고    scopus 로고
    • Timing of neurotransmission at fast synapses in the mammalian brain
    • Sabatini, B. L., and W. G. Regehr. 1996. Timing of neurotransmission at fast synapses in the mammalian brain. Nature. 384:170-172.
    • (1996) Nature , vol.384 , pp. 170-172
    • Sabatini, B.L.1    Regehr, W.G.2
  • 15
    • 0027263007 scopus 로고
    • Synaptic vesicle traffic: Rush hour in the nerve terminal
    • Jahn, R., and T. C. Südhof. 1993. Synaptic vesicle traffic: rush hour in the nerve terminal. J. Neurochem. 61:12-21.
    • (1993) J. Neurochem. , vol.61 , pp. 12-21
    • Jahn, R.1    Südhof, T.C.2
  • 16
    • 0019350409 scopus 로고
    • Relationship between presynaptic calcium current and postsynaptic potential in squid giant synapse
    • Llinas, R., I. Z. Steinberg, and K. Walton. 1981. Relationship between presynaptic calcium current and postsynaptic potential in squid giant synapse. Biophys. J. 33:323-351.
    • (1981) Biophys. J. , vol.33 , pp. 323-351
    • Llinas, R.1    Steinberg, I.Z.2    Walton, K.3
  • 17
    • 0014078590 scopus 로고
    • The timing of calcium action during neuromuscular transmission
    • Katz, B., and R. Miledi. 1967. The timing of calcium action during neuromuscular transmission. J. Physiol. 189:535-544.
    • (1967) J. Physiol. , vol.189 , pp. 535-544
    • Katz, B.1    Miledi, R.2
  • 20
    • 0036680512 scopus 로고    scopus 로고
    • Sealed with a twist: Complexin and the synaptic SNARE complex
    • Marz, K. E., and P. I. Hanson. 2002. Sealed with a twist: complexin and the synaptic SNARE complex. Trends Neurosci. 25:381-383.
    • (2002) Trends Neurosci. , vol.25 , pp. 381-383
    • Marz, K.E.1    Hanson, P.I.2
  • 21
    • 0030222771 scopus 로고    scopus 로고
    • Synaptotagmins: C2-domain proteins that regulate membrane traffic
    • Südhof, T. C., and J. Rizo. 1996. Synaptotagmins: C2-domain proteins that regulate membrane traffic. Neuron. 17:379-388.
    • (1996) Neuron. , vol.17 , pp. 379-388
    • Südhof, T.C.1    Rizo, J.2
  • 22
  • 23
    • 1542286172 scopus 로고    scopus 로고
    • The C2 domains of synaptotagmin-partners in exocytosis
    • Bai, J., and E. R. Chapman. 2004. The C2 domains of synaptotagmin- partners in exocytosis. Trends Biochem. Sci. 29:143-151.
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 143-151
    • Bai, J.1    Chapman, E.R.2
  • 24
    • 0028880456 scopus 로고
    • Complexins: Cytosolic proteins that regulate SNAP receptor function
    • McMahon, H. T., M. Missler, C. Li, and T. C. Südhof. 1995. Complexins: cytosolic proteins that regulate SNAP receptor function. Cell. 83:111-119.
    • (1995) Cell , vol.83 , pp. 111-119
    • McMahon, H.T.1    Missler, M.2    Li, C.3    Südhof, T.C.4
  • 25
    • 0037040873 scopus 로고    scopus 로고
    • Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis
    • Pabst, S., M. Margittai, D. Vainius, R. Langen, R. Jahn, and D. Fasshauer. 2002. Rapid and selective binding to the synaptic SNARE complex suggests a modulatory role of complexins in neuroexocytosis. J. Biol. Chem. 277:7838-7848.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7838-7848
    • Pabst, S.1    Margittai, M.2    Vainius, D.3    Langen, R.4    Jahn, R.5    Fasshauer, D.6
  • 26
    • 0034733545 scopus 로고    scopus 로고
    • Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions
    • Pabst, S., J. W. Hazzard, W. Antonin, T. C. Südhof, R. Jahn, J. Rizo, and D. Fasshauer. 2000. Selective interaction of complexin with the neuronal SNARE complex. Determination of the binding regions. J. Biol. Chem. 275:19808-19818.
    • (2000) J. Biol. Chem. , vol.275 , pp. 19808-19818
    • Pabst, S.1    Hazzard, J.W.2    Antonin, W.3    Südhof, T.C.4    Jahn, R.5    Rizo, J.6    Fasshauer, D.7
  • 28
    • 0037135615 scopus 로고    scopus 로고
    • X-ray structure of a neuronal complexin-SNARE complex from squid
    • Bracher, A., J. Kadlec, H. Betz, and W. Weissenhorn. 2002. X-ray structure of a neuronal complexin-SNARE complex from squid. J. Biol. Chem. 277:26517-26523.
    • (2002) J. Biol. Chem. , vol.277 , pp. 26517-26523
    • Bracher, A.1    Kadlec, J.2    Betz, H.3    Weissenhorn, W.4
  • 29
    • 0025270739 scopus 로고
    • Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C
    • Perin, M. S., V. A. Fried, G. A. Mignery, R. Jahn, and T. C. Südhof. 1990. Phospholipid binding by a synaptic vesicle protein homologous to the regulatory region of protein kinase C. Nature. 345:260-263.
    • (1990) Nature , vol.345 , pp. 260-263
    • Perin, M.S.1    Fried, V.A.2    Mignery, G.A.3    Jahn, R.4    Südhof, T.C.5
  • 31
    • 0026631563 scopus 로고
    • Synaptotagmin: A calcium sensor on the synaptic vesicle surface
    • Brose, N., A. G. Petrenko, T. C. Südhof, and R. Jahn. 1992. Synaptotagmin: a calcium sensor on the synaptic vesicle surface. Science. 256:1021-1025.
    • (1992) Science , vol.256 , pp. 1021-1025
    • Brose, N.1    Petrenko, A.G.2    Südhof, T.C.3    Jahn, R.4
  • 33
    • 0028068586 scopus 로고
    • Calcium-dependent interaction of the cytoplasmic region of synaptotagmin with membranes. Autonomous function of a single C2-homologous domain
    • Chapman, E. R., and R. Jahn. 1994. Calcium-dependent interaction of the cytoplasmic region of synaptotagmin with membranes. Autonomous function of a single C2-homologous domain. J. Biol. Chem. 269:5735-5741.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5735-5741
    • Chapman, E.R.1    Jahn, R.2
  • 34
    • 0035924571 scopus 로고    scopus 로고
    • Three-dimensional structure of the synaptotagmin I C2B-domain: Synaptotagmin I as a phospholipid binding machine
    • Fernandez, I., D. Arac, J. Ubach, S. H. Gerber, O. Shin, Y. Gao, R. G. Anderson, T. C. Südhof, and J. Rizo. 2001. Three-dimensional structure of the synaptotagmin I C2B-domain: synaptotagmin I as a phospholipid binding machine. Neuron. 32:1057-1069.
    • (2001) Neuron. , vol.32 , pp. 1057-1069
    • Fernandez, I.1    Arac, D.2    Ubach, J.3    Gerber, S.H.4    Shin, O.5    Gao, Y.6    Anderson, R.G.7    Südhof, T.C.8    Rizo, J.9
  • 35
    • 0842291506 scopus 로고    scopus 로고
    • PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane
    • Bai, J., W. C. Tucker, and E. R. Chapman. 2004. PIP2 increases the speed of response of synaptotagmin and steers its membrane-penetration activity toward the plasma membrane. Nat. Struct. Mol. Biol. 11:36-44.
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 36-44
    • Bai, J.1    Tucker, W.C.2    Chapman, E.R.3
  • 36
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett, M. K., N. Calakos, and R. H. Scheller. 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
  • 37
    • 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., M. K. Bennett, S. W. Whiteheart, R. H. Scheller, and J. E. Rothman. 1993. 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
  • 38
  • 39
    • 0029917101 scopus 로고    scopus 로고
    • Localization of synaptotagmin-binding domains on syntaxin
    • Kee, Y., and R. H. Scheller. 1996. Localization of synaptotagmin-binding domains on syntaxin. J. Neurosci. 16:1975-1981.
    • (1996) J. Neurosci. , vol.16 , pp. 1975-1981
    • Kee, Y.1    Scheller, R.H.2
  • 40
    • 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., G. Stenbeck, J. E. Rothman, and T. H. Söllner. 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. Natl. Acad. Sci. USA. 94:997-1001.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 997-1001
    • Schiavo, G.1    Stenbeck, G.2    Rothman, J.E.3    Söllner, T.H.4
  • 41
    • 0037458711 scopus 로고    scopus 로고
    • Mechanism of calcium-independent synaptotagmin binding to target SNAREs
    • Rickman, C., and B. Davletov. 2003. Mechanism of calcium-independent synaptotagmin binding to target SNAREs. J. Biol. Chem. 278:5501-5504.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5501-5504
    • Rickman, C.1    Davletov, B.2
  • 42
    • 0037424295 scopus 로고    scopus 로고
    • High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex
    • Ernst, J. A., and A. T. Brunger. 2003. High resolution structure, stability, and synaptotagmin binding of a truncated neuronal SNARE complex. J. Biol. Chem. 278:8630-8636.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8630-8636
    • Ernst, J.A.1    Brunger, A.T.2
  • 44
    • 0037427025 scopus 로고    scopus 로고
    • 2+ binding site of the synaptotagmin 1 C2B domain triggers fast exocytosis without stimulating SNARE interactions
    • 2+ binding site of the synaptotagmin 1 C2B domain triggers fast exocytosis without stimulating SNARE interactions. Neuron. 37:99-108.
    • (2003) Neuron. , vol.37 , pp. 99-108
    • Shin, O.H.1    Rhee, J.S.2    Tang, J.3    Sugita, S.4    Rosenmund, C.5    Südhof, T.C.6
  • 45
    • 0141704073 scopus 로고    scopus 로고
    • Controversies in synaptic vesicle exocytosis
    • Weimer, R. M., and E. M. Jorgensen. 2003. Controversies in synaptic vesicle exocytosis. J. Cell Sci. 116:3661-3666.
    • (2003) J. Cell Sci. , vol.116 , pp. 3661-3666
    • Weimer, R.M.1    Jorgensen, E.M.2
  • 46
    • 0037452955 scopus 로고    scopus 로고
    • Facile detection of protein-protein interactions by one-dimensional NMR spectroscopy
    • Arac, D., T. Murphy, and J. Rizo. 2003. Facile detection of protein-protein interactions by one-dimensional NMR spectroscopy. Biochemistry. 42:2774-2780.
    • (2003) Biochemistry , vol.42 , pp. 2774-2780
    • Arac, D.1    Murphy, T.2    Rizo, J.3
  • 47
    • 1842475284 scopus 로고    scopus 로고
    • Fusion pore dynamics are regulated by synaptotagmin*t-SNARE interactions
    • Bai, J., C. T. Wang, D. A. Richards, M. B. Jackson, and E. R. Chapman. 2004. Fusion pore dynamics are regulated by synaptotagmin*t-SNARE interactions. Neuron. 41:929-942.
    • (2004) Neuron. , vol.41 , pp. 929-942
    • Bai, J.1    Wang, C.T.2    Richards, D.A.3    Jackson, M.B.4    Chapman, E.R.5
  • 48
    • 1942520207 scopus 로고    scopus 로고
    • 2+-regulated membrane fusion by synaptotagmin and SNAREs
    • 2+-regulated membrane fusion by synaptotagmin and SNAREs. Science. 304:435-438.
    • (2004) Science , vol.304 , pp. 435-438
    • Tucker, W.C.1    Weber, T.2    Chapman, E.R.3
  • 50
    • 0037165996 scopus 로고    scopus 로고
    • Correlating structural dynamics and function in single ribozyme molecules
    • Zhuang, X., H. Kim, M. J. Pereira, H. P. Babcock, N. G. Walter, and S. Chu. 2002. Correlating structural dynamics and function in single ribozyme molecules. Science. 296:1473-1476.
    • (2002) Science , vol.296 , pp. 1473-1476
    • Zhuang, X.1    Kim, H.2    Pereira, M.J.3    Babcock, H.P.4    Walter, N.G.5    Chu, S.6
  • 51
    • 0037207101 scopus 로고    scopus 로고
    • Mutational analysis of synaptobrevin transmembrane domain oligomerization
    • Bowen, M. E., D. M. Engelman, and A. T. Brunger. 2002. Mutational analysis of synaptobrevin transmembrane domain oligomerization. Biochemistry. 41:15861-15866.
    • (2002) Biochemistry , vol.41 , pp. 15861-15866
    • Bowen, M.E.1    Engelman, D.M.2    Brunger, A.T.3
  • 54
    • 0032555126 scopus 로고    scopus 로고
    • Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly
    • Fasshauer, D., W. K. Eliason, A. T. Brunger, and R. Jahn. 1998. Identification of a minimal core of the synaptic SNARE complex sufficient for reversible assembly and disassembly. Biochemistry. 37:10354-10362.
    • (1998) Biochemistry , vol.37 , pp. 10354-10362
    • Fasshauer, D.1    Eliason, W.K.2    Brunger, A.T.3    Jahn, R.4
  • 55
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton, R. B., D. Fasshauer, R. Jahn, and A. T. Brunger. 1998. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature. 395:347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 57
    • 0037119362 scopus 로고    scopus 로고
    • Vesicle-associated membrane protein-2/synaptobrevin binding to synaptotagmin I promotes O-glycosylation of synaptotagmin I
    • Fukuda, M. 2002. Vesicle-associated membrane protein-2/synaptobrevin binding to synaptotagmin I promotes O-glycosylation of synaptotagmin I. J. Biol. Chem. 277:30351-30358.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30351-30358
    • Fukuda, M.1
  • 58
    • 16344389389 scopus 로고    scopus 로고
    • Single molecule observation of liposome-bilayer fusion thermally induced by SNAREs
    • Bowen, M. E., K. Weninger, A. T. Brunger, and S. Chu. 2004. Single molecule observation of liposome-bilayer fusion thermally induced by SNAREs. Biophys. J. 87:3569-3585.
    • (2004) Biophys. J. , vol.87 , pp. 3569-3585
    • Bowen, M.E.1    Weninger, K.2    Brunger, A.T.3    Chu, S.4
  • 59
    • 0033413080 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer between single fluorophores attached to a coiled-coil protein in aqueous solution
    • Ishii, Y., T. Yoshida, T. Funatsu, T. Wazawa, and T. Yanagida. 1999. Fluorescence resonance energy transfer between single fluorophores attached to a coiled-coil protein in aqueous solution. Chem. Phys. 247:163-173.
    • (1999) Chem. Phys. , vol.247 , pp. 163-173
    • Ishii, Y.1    Yoshida, T.2    Funatsu, T.3    Wazawa, T.4    Yanagida, T.5
  • 61
    • 0036835759 scopus 로고    scopus 로고
    • Efficiencies of fluorescence resonance energy transfer and contact-mediated quenching in oligonucleotide probes
    • Marras, S. A., F. R. Kramer, and S. Tyagi. 2002. Efficiencies of fluorescence resonance energy transfer and contact-mediated quenching in oligonucleotide probes. Nucleic Acids Res. 30:e122.
    • (2002) Nucleic Acids Res. , vol.30
    • Marras, S.A.1    Kramer, F.R.2    Tyagi, S.3
  • 62
    • 0037462084 scopus 로고    scopus 로고
    • Investigations of bivalent antibody binding on fluid-supported phospholipid membranes: The effect of hapten density
    • Yang, T., O. K. Baryshnikova, H. Mao, M. A. Holden, and P. S. Cremer. 2003. Investigations of bivalent antibody binding on fluid-supported phospholipid membranes: the effect of hapten density. J. Am. Chem. Soc. 125:4779-4784.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4779-4784
    • Yang, T.1    Baryshnikova, O.K.2    Mao, H.3    Holden, M.A.4    Cremer, P.S.5
  • 64
    • 0033229735 scopus 로고    scopus 로고
    • Crystal structure of the cytosolic C2A-C2B domains of synaptotagmin III. Implications for Ca+2-independent snare complex interaction
    • Sutton, R. B., J. A. Ernst, and A. T. Brunger. 1999. Crystal structure of the cytosolic C2A-C2B domains of synaptotagmin III. Implications for Ca+2-independent snare complex interaction. J. Cell Biol. 147:589-598.
    • (1999) J. Cell Biol. , vol.147 , pp. 589-598
    • Sutton, R.B.1    Ernst, J.A.2    Brunger, A.T.3
  • 66
    • 0024971458 scopus 로고
    • Phenomenological theory of gel electrophoresis of protein-nucleic acid complexes
    • Cann, J. R. 1989. Phenomenological theory of gel electrophoresis of protein-nucleic acid complexes. J. Biol. Chem. 264:17032-17040.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17032-17040
    • Cann, J.R.1
  • 71
    • 0033584339 scopus 로고    scopus 로고
    • Synaptic function modulated by changes in the ratio of synaptotagmin I and IV
    • Littleton, J. T., T. L. Serano, G. M. Rubin, B. Ganetzky, and E. R. Chapman. 1999. Synaptic function modulated by changes in the ratio of synaptotagmin I and IV. Nature. 400:757-760.
    • (1999) Nature , vol.400 , pp. 757-760
    • Littleton, J.T.1    Serano, T.L.2    Rubin, G.M.3    Ganetzky, B.4    Chapman, E.R.5
  • 72
    • 0347383758 scopus 로고    scopus 로고
    • MODELLER: Generation and refinement of homology-based protein structure models
    • Fiser, A., and A. Sali. 2003. MODELLER: generation and refinement of homology-based protein structure models. Methods Enzymol. 374:461-491.
    • (2003) Methods Enzymol. , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2


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