메뉴 건너뛰기




Volumn 17, Issue 3, 2010, Pages 318-324

Single-molecule FRET-derived model of the synaptotagmin 1-SNARE fusion complex

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; SNARE PROTEIN; SYNAPTOTAGMIN I;

EID: 77949264921     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1763     Document Type: Article
Times cited : (169)

References (78)
  • 1
    • 0035282457 scopus 로고    scopus 로고
    • Synaptotagmin i functions as a calcium regulator of release probability
    • Fernandez-Chacon, R. et al. Synaptotagmin I functions as a calcium regulator of release probability. Nature 410, 41-49 (2001).
    • (2001) Nature , vol.410 , pp. 41-49
    • Fernandez-Chacon, R.1
  • 2
    • 33845234610 scopus 로고    scopus 로고
    • 2+-dependent soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex binding in synaptic exocytosis
    • 2+-dependent soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex binding in synaptic exocytosis. J. Neurosci. 26, 12556-12565 (2006).
    • (2006) J. Neurosci. , vol.26 , pp. 12556-12565
    • Pang, Z.P.1    Shin, O.H.2    Meyer, A.C.3    Rosenmund, C.4    Südhof, T.C.5
  • 3
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett, M.K., Calakos, N. & Scheller, R.H. Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science 257, 255-259 (1992).
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 4
    • 0028989281 scopus 로고
    • 2+-independent activities of neural and nonneural synaptotagmins
    • 2+-independent activities of neural and nonneural synaptotagmins. Nature 375, 594-599 (1995).
    • (1995) Nature , vol.375 , pp. 594-599
    • Li, C.1
  • 5
    • 0028970788 scopus 로고
    • 2+ regulates the interaction between synaptotagmin and syntaxin 1
    • 2+ regulates the interaction between synaptotagmin and syntaxin 1. J. Biol. Chem. 270, 23667-23671 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 23667-23671
    • Chapman, E.R.1    Hanson, P.I.2    An, S.3    Jahn, R.4
  • 6
    • 0037204063 scopus 로고    scopus 로고
    • Differential control of vesicle priming and short-term plasticity by Munc13 Isoforms
    • Rosenmund, C. et al. Differential control of vesicle priming and short-term plasticity by Munc13 Isoforms. Neuron 33, 411-424 (2002).
    • (2002) Neuron , vol.33 , pp. 411-424
    • Rosenmund, C.1
  • 7
    • 0030175394 scopus 로고    scopus 로고
    • Defnition of the readily releasable pool of vesicles at hippocampal synapses
    • Rosenmund, C. & Stevens, C.F. Defnition of the readily releasable pool of vesicles at hippocampal synapses. Neuron 16, 1197-1207 (1996).
    • (1996) Neuron , vol.16 , pp. 1197-1207
    • Rosenmund, C.1    Stevens, C.F.2
  • 8
    • 0028061861 scopus 로고
    • 2+ sensor for transmitter release at a central synapse
    • 2+ sensor for transmitter release at a central synapse. Cell 79, 717-727 (1994).
    • (1994) Cell , vol.79 , pp. 717-727
    • Geppert, M.1
  • 9
    • 33746852464 scopus 로고    scopus 로고
    • Protein kinase C regulatory domains: The art of decoding many different signals in membranes
    • Corbalan-Garcia, S. & Gomez-Fernandez, J.C. Protein kinase C regulatory domains: the art of decoding many different signals in membranes. Biochim. Biophys. Acta 1761, 633-654 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 633-654
    • Corbalan-Garcia, S.1    Gomez-Fernandez, J.C.2
  • 10
    • 34147190809 scopus 로고    scopus 로고
    • Interdependence of PKC-dependent and PKC-independent pathways for presynaptic plasticity
    • Wierda, K.D., Toonen, R.F., de Wit, H., Brussaard, A.B. & Verhage, M. Interdependence of PKC-dependent and PKC-independent pathways for presynaptic plasticity. Neuron 54, 275-290 (2007).
    • (2007) Neuron , vol.54 , pp. 275-290
    • Wierda, K.D.1    Toonen, R.F.2    De Wit, H.3    Brussaard, A.B.4    Verhage, M.5
  • 11
    • 18244389735 scopus 로고    scopus 로고
    • Phorbol ester-and DAG-induced augmentation of neurotransmitter release from hippocampal neurons is mediated by Munc13s and not by PKCs
    • Rhee, J.-S. et al. Phorbol ester-and DAG-induced augmentation of neurotransmitter release from hippocampal neurons is mediated by Munc13s and not by PKCs. Cell 108, 121-133 (2002).
    • (2002) Cell , vol.108 , pp. 121-133
    • Rhee, J.-S.1
  • 12
    • 33846794400 scopus 로고    scopus 로고
    • 1 domain activation lowers the energy barrier for synaptic vesicle fusion
    • 1 domain activation lowers the energy barrier for synaptic vesicle fusion. J. Neurosci. 27, 1200-1210 (2007).
    • (2007) J. Neurosci. , vol.27 , pp. 1200-1210
    • Basu, J.1    Betz, A.2    Brose, N.3    Rosenmund, C.4
  • 13
    • 0037179662 scopus 로고    scopus 로고
    • Curvature of clathrin-coated pits driven by epsin
    • Ford, M.G. et al. Curvature of clathrin-coated pits driven by epsin. Nature 419, 361-366 (2002).
    • (2002) Nature , vol.419 , pp. 361-366
    • Ford, M.G.1
  • 14
    • 29444436513 scopus 로고    scopus 로고
    • 2+ affnity of synaptotagmin 1
    • 2+ affnity of synaptotagmin 1. Proc. Natl. Acad. Sci. USA 102, 18664-18669 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18664-18669
    • Rhee, J.-S.1
  • 15
    • 0025811008 scopus 로고
    • Calcium promotes the accumulation of polyphosphoinositides in intact and permeabilized bovine adrenal Chromaffn cells
    • Eberhard, D.A. & Holz, R.W. Calcium promotes the accumulation of polyphosphoinositides in intact and permeabilized bovine adrenal Chromaffn cells. Cell. Mol. Neurobiol. 11, 357-370 (1991).
    • (1991) Cell. Mol. Neurobiol. , vol.11 , pp. 357-370
    • Eberhard, D.A.1    Holz, R.W.2
  • 16
    • 0034740730 scopus 로고    scopus 로고
    • 2 synthesizing enzyme at the synapse
    • 2 synthesizing enzyme at the synapse. Neuron 32, 79-88 (2001).
    • (2001) Neuron , vol.32 , pp. 79-88
    • Wenk, M.R.1
  • 17
    • 0034705455 scopus 로고    scopus 로고
    • Autophosphorylation of type i phosphatidylinositol phosphate kinase regulates its lipid kinase activity
    • Itoh, T., Ishihara, H., Shibasaki, Y., Oka, Y. & Takenawa, T. Autophosphorylation of type I phosphatidylinositol phosphate kinase regulates its lipid kinase activity. J. Biol. Chem. 275, 19389-19394 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 19389-19394
    • Itoh, T.1    Ishihara, H.2    Shibasaki, Y.3    Oka, Y.4    Takenawa, T.5
  • 18
    • 0035895910 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-phosphate 5-kinase type i is regulated through phosphorylation response by extracellular stimuli
    • Park, S.J., Itoh, T. & Takenawa, T. Phosphatidylinositol 4-phosphate 5-kinase type I is regulated through phosphorylation response by extracellular stimuli. J. Biol. Chem. 276, 4781-4787 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 4781-4787
    • Park, S.J.1    Itoh, T.2    Takenawa, T.3
  • 19
    • 0029026392 scopus 로고
    • The synaptic vesicle cycle: A cascade of protein-protein interactions
    • Südhof, T.C. The synaptic vesicle cycle: a cascade of protein-protein interactions. Nature 375, 645-653 (1995).
    • (1995) Nature , vol.375 , pp. 645-653
    • Südhof, T.C.1
  • 20
    • 51749100843 scopus 로고    scopus 로고
    • Conformational switch of syntaxin-1 controls synaptic vesicle fusion
    • Gerber, S.H. et al. Conformational switch of syntaxin-1 controls synaptic vesicle fusion. Science 321, 1507-1510 (2008).
    • (2008) Science , vol.321 , pp. 1507-1510
    • Gerber, S.H.1
  • 22
    • 34249933061 scopus 로고    scopus 로고
    • How synaptotagmin promotes membrane fusion
    • Martens, S., Kozlov, M.M. & McMahon, H.T. How synaptotagmin promotes membrane fusion. Science 316, 1205-1208 (2007).
    • (2007) Science , vol.316 , pp. 1205-1208
    • Martens, S.1    Kozlov, M.M.2    McMahon, H.T.3
  • 23
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on Unix pipes
    • Delaglio, F. et al. NMRPipe: a multidimensional spectral processing system based on Unix pipes. J. Biomol. NMR 6, 277-293 (1995).
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1
  • 24
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis of NMR data
    • Johnson, B.A. & Blevins, R.A. NMR View: a computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4, 603-614 (1994).
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 25
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. & Minor, W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276, 307-326 (1997).
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 26
    • 84920325457 scopus 로고
    • An automated package for molecular replacement
    • Navaza, J. Amore: an automated package for molecular replacement. Acta Crystallogr. A 50, 157-163 (1994).
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Amore, N.J.1
  • 29
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron-density maps and the location of errors in these models
    • Jones, T.A., Zou, J.Y., Cowan, S.W. & Kjeldgaard, M. Improved methods for building protein models in electron-density maps and the location of errors in these models. Acta Crystallogr. A 47, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 31
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr.
    • Collaborative Computational Project No. 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Collaborative Computational Project No. 4. , vol.50 , pp. 760-763
  • 32
    • 0036521872 scopus 로고    scopus 로고
    • The effects of temperature on vesicular supply and release in autaptic cultures of rat and mouse hippocampal neurons
    • Pyott, S.J. & Rosenmund, C. The effects of temperature on vesicular supply and release in autaptic cultures of rat and mouse hippocampal neurons. J. Physiol. (Lond.) 539, 523-535 (2002).
    • (2002) J. Physiol. (Lond.) , vol.539 , pp. 523-535
    • Pyott, S.J.1    Rosenmund, C.2
  • 33
    • 33847352925 scopus 로고    scopus 로고
    • Monitoring synaptic transmission in primary neuronal cultures using local extracellular stimulation
    • Maximov, A., Pang, Z., Tervo, D.G.R. & Südhof, T.C. Monitoring synaptic transmission in primary neuronal cultures using local extracellular stimulation. J. Neurosci. Methods 161, 75-87 (2007).
    • (2007) J. Neurosci. Methods , vol.161 , pp. 75-87
    • Maximov, A.1    Pang, Z.2    Tervo, D.G.R.3    Südhof, T.C.4
  • 34
    • 0035282457 scopus 로고    scopus 로고
    • Synaptotagmin i functions as a calcium regulator of release probability
    • Fernandez-Chacon, R. et al. Synaptotagmin I functions as a calcium regulator of release probability. Nature 410, 41-49 (2001).
    • (2001) Nature , vol.410 , pp. 41-49
    • Fernandez-Chacon, R.1
  • 35
    • 29444436513 scopus 로고    scopus 로고
    • Augmenting neurotransmitter release by enhancing the apparent Ca2+ affnity of synaptotagmin 1
    • Rhee, J.S. et al. Augmenting neurotransmitter release by enhancing the apparent Ca2+ affnity of synaptotagmin 1. Proc. Natl. Acad. Sci. USA 102, 18664-18669 (2005).
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 18664-18669
    • Rhee, J.S.1
  • 36
    • 33644770187 scopus 로고    scopus 로고
    • Structure and function of SNARE and SNARE-interacting proteins
    • Brunger, A.T. Structure and function of SNARE and SNARE-interacting proteins. Q. Rev. Biophys. 38, 1-47 (2005).
    • (2005) Q. Rev. Biophys. , vol.38 , pp. 1-47
    • Brunger, A.T.1
  • 38
    • 33748324514 scopus 로고    scopus 로고
    • Membrane binding and subcellular targeting of C2 domains
    • Cho, W. & Stahelin, R.V. Membrane binding and subcellular targeting of C2 domains. Biochim. Biophys. Acta 1761, 838-849 (2006).
    • (2006) Biochim. Biophys. Acta , vol.1761 , pp. 838-849
    • Cho, W.1    Stahelin, R.V.2
  • 39
    • 33845234610 scopus 로고    scopus 로고
    • 2+-dependent soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex binding in synaptic exocytosis
    • 2+-dependent soluble N-ethylmaleimide-sensitive factor attachment protein receptor complex binding in synaptic exocytosis. J. Neurosci. 26, 12556-12565 (2006).
    • (2006) J. Neurosci. , vol.26 , pp. 12556-12565
    • Pang, Z.P.1    Shin, O.H.2    Meyer, A.C.3    Rosenmund, C.4    Sudhof, T.C.5
  • 40
    • 58849105859 scopus 로고    scopus 로고
    • Alternative zippering as an on-off switch for SNARE-mediated fusion
    • Giraudo, C.G. et al. Alternative zippering as an on-off switch for SNARE-mediated fusion. Science 323, 512-516 (2009).
    • (2009) Science , vol.323 , pp. 512-516
    • Giraudo, C.G.1
  • 41
    • 58849164361 scopus 로고    scopus 로고
    • Complexin controls the force transfer from SNARE complexes to membranes in fusion
    • Maximov, A., Tang, J., Yang, X., Pang, Z.P. & Sudhof, T.C. Complexin controls the force transfer from SNARE complexes to membranes in fusion. Science 323, 516-521 (2009).
    • (2009) Science , vol.323 , pp. 516-521
    • Maximov, A.1    Tang, J.2    Yang, X.3    Pang, Z.P.4    Sudhof, T.C.5
  • 42
    • 0742324525 scopus 로고    scopus 로고
    • DNA-binding orientation and domain conformation of the E. coli rep helicase monomer bound to a partial duplex junction: Single-molecule studies of fuorescently labeled enzymes
    • Rasnik, I., Myong, S., Cheng, W., Lohman, T.M. & Ha, T. DNA-binding orientation and domain conformation of the E. coli rep helicase monomer bound to a partial duplex junction: single-molecule studies of fuorescently labeled enzymes. J. Mol. Biol. 336, 395-408 (2004).
    • (2004) J. Mol. Biol. , vol.336 , pp. 395-408
    • Rasnik, I.1    Myong, S.2    Cheng, W.3    Lohman, T.M.4    Ha, T.5
  • 44
    • 38349173560 scopus 로고    scopus 로고
    • Single-molecule tracking of mRNA exiting from RNA polymerase II
    • Andrecka, J. et al. Single-molecule tracking of mRNA exiting from RNA polymerase II. Proc. Natl. Acad. Sci. USA 105, 135-140 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 135-140
    • Andrecka, J.1
  • 45
    • 33847269603 scopus 로고    scopus 로고
    • 2+-phospholipid complex in neurotransmitter release
    • 2+-phospholipid complex in neurotransmitter release. J. Mol. Biol. 367, 848-863 (2007).
    • (2007) J. Mol. Biol. , vol.367 , pp. 848-863
    • Dai, H.1    Shen, N.2    Arac, D.3    Rizo, J.4
  • 47
    • 36348946234 scopus 로고    scopus 로고
    • Single-molecule biophysics: At the interface of biology, physics and chemistry
    • Deniz, A.A., Mukhopadhyay, S. & Lemke, E.A. Single-molecule biophysics: at the interface of biology, physics and chemistry. J. R. Soc. Interface 5, 15-45 (2008).
    • (2008) J. R. Soc. Interface , vol.5 , pp. 15-45
    • Deniz, A.A.1    Mukhopadhyay, S.2    Lemke, E.A.3
  • 48
    • 0035924571 scopus 로고    scopus 로고
    • Three-dimensional structure of the synaptotagmin 1 C2B-domain: Synaptotagmin 1 as a phospholipid binding machine
    • Fernandez, I. et al. Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine. Neuron 32, 1057-1069 (2001).
    • (2001) Neuron , vol.32 , pp. 1057-1069
    • Fernandez, I.1
  • 49
    • 0031019191 scopus 로고    scopus 로고
    • 2+-dependent electrostatic switch
    • 2+-dependent electrostatic switch. Neuron 18, 133-142 (1997).
    • (1997) Neuron , vol.18 , pp. 133-142
    • Shao, X.1
  • 50
    • 0032541943 scopus 로고    scopus 로고
    • 2+-free and Ca2+-bound C2A domain of synaptotagmin I: Does Ca2+ induce a conformational change?
    • 2+-free and Ca2+-bound C2A domain of synaptotagmin I: does Ca2+ induce a conformational change? Biochemistry 37, 16106-16115 (1998).
    • (1998) Biochemistry , vol.37 , pp. 16106-16115
    • Shao, X.1    Fernandez, I.2    Sudhof, T.C.3    Rizo, J.4
  • 52
    • 1842475284 scopus 로고    scopus 로고
    • Fusion pore dynamics are regulated by synaptotagmin*t-SNARE interactions
    • Bai, J., Wang, C.T., Richards, D.A., Jackson, M.B. & Chapman, E.R. Fusion pore dynamics are regulated by synaptotagmin*t-SNARE interactions. Neuron 41, 929-942 (2004).
    • (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
  • 53
    • 33748605056 scopus 로고    scopus 로고
    • A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis
    • Tang, J. et al. A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis. Cell 126, 1175-1187 (2006).
    • (2006) Cell , vol.126 , pp. 1175-1187
    • Tang, J.1
  • 56
    • 33644804207 scopus 로고    scopus 로고
    • 2+-dependent multivalent binding of synaptotagmin-1 to phospholipids
    • 2+-dependent multivalent binding of synaptotagmin-1 to phospholipids. Nat. Struct. Mol. Biol. 13, 209-217 (2006).
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 209-217
    • Arac, D.1
  • 57
    • 67649884533 scopus 로고    scopus 로고
    • Solution and membrane-bound conformations of the tandem C2A and C2B domains of synaptotagmin 1: Evidence for bilayer bridging
    • Herrick, D.Z. et al. Solution and membrane-bound conformations of the tandem C2A and C2B domains of synaptotagmin 1: evidence for bilayer bridging. J. Mol. Biol. 390, 913-923 (2009).
    • (2009) J. Mol. Biol. , vol.390 , pp. 913-923
    • Herrick, D.Z.1
  • 59
    • 33746713745 scopus 로고    scopus 로고
    • Real-time observation of RecA flament dynamics with single monomer resolution
    • Joo, C. et al. Real-time observation of RecA flament dynamics with single monomer resolution. Cell 126, 515-527 (2006).
    • (2006) Cell , vol.126 , pp. 515-527
    • Joo, C.1
  • 60
    • 0345166865 scopus 로고    scopus 로고
    • Single-molecule studies of SNARE complex assembly reveal parallel and antiparallel confgurations
    • Weninger, K., Bowen, M.E., Chu, S. & Brunger, A.T. Single-molecule studies of SNARE complex assembly reveal parallel and antiparallel confgurations. Proc. Natl. Acad. Sci. USA 100, 14800-14805 (2003).
    • (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
  • 61
    • 23144455040 scopus 로고    scopus 로고
    • Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex
    • Bowen, M.E., Weninger, K., Ernst, J., Chu, S. & Brunger, A.T. Single-molecule studies of synaptotagmin and complexin binding to the SNARE complex. Biophys. J. 89, 690-702 (2005).
    • (2005) Biophys. J. , vol.89 , pp. 690-702
    • Bowen, M.E.1    Weninger, K.2    Ernst, J.3    Chu, S.4    Brunger, A.T.5
  • 62
    • 56149121056 scopus 로고    scopus 로고
    • A nano-positioning system for macromolecular structural analysis
    • Muschielok, A. et al. A nano-positioning system for macromolecular structural analysis. Nat. Methods 5, 965-971 (2008).
    • (2008) Nat. Methods , vol.5 , pp. 965-971
    • Muschielok, A.1
  • 63
    • 34547880034 scopus 로고    scopus 로고
    • Single-molecule FRET reveals sugar-induced conformational dynamics in LacY
    • Majumdar, D.S. et al. Single-molecule FRET reveals sugar-induced conformational dynamics in LacY. Proc. Natl. Acad. Sci. USA 104, 12640-12645 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12640-12645
    • Majumdar, D.S.1
  • 64
    • 46449093538 scopus 로고    scopus 로고
    • How does synaptotagmin trigger neurotransmitter release?
    • Chapman, E.R. How does synaptotagmin trigger neurotransmitter release? Annu. Rev. Biochem. 77, 615-641 (2008).
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 615-641
    • Chapman, E.R.1
  • 65
    • 30044443686 scopus 로고    scopus 로고
    • Conserved prefusion protein assembly in regulated exocytosis
    • Rickman, C. et al. Conserved prefusion protein assembly in regulated exocytosis. Mol. Biol. Cell 17, 283-294 (2006).
    • (2006) Mol. Biol. Cell , vol.17 , pp. 283-294
    • Rickman, C.1
  • 66
    • 69449108209 scopus 로고    scopus 로고
    • Synaptotagmin 1 docks secretory vesicles to syntaxin 1-SNAP-25 acceptor complexes
    • de Wit, H. et al. Synaptotagmin 1 docks secretory vesicles to syntaxin 1-SNAP-25 acceptor complexes. Cell 138, 935-946 (2009).
    • (2009) Cell , vol.138 , pp. 935-946
    • De Wit, H.1
  • 67
    • 55549100557 scopus 로고    scopus 로고
    • The Janus-faced nature of the C(2)B domain is fundamental for synaptotagmin-1 function
    • Xue, M., Ma, C., Craig, T.K., Rosenmund, C. & Rizo, J. The Janus-faced nature of the C(2)B domain is fundamental for synaptotagmin-1 function. Nat. Struct. Mol. Biol. 15, 1160-1168 (2008).
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 1160-1168
    • Xue, M.1    Ma, C.2    Craig, T.K.3    Rosenmund, C.4    Rizo, J.5
  • 68
    • 64949163287 scopus 로고    scopus 로고
    • Direct interaction of SNARE complex binding protein synaphin/complexin with calcium sensor synaptotagmin 1
    • Tokumaru, H., Shimizu-Okabe, C. & Abe, T. Direct interaction of SNARE complex binding protein synaphin/complexin with calcium sensor synaptotagmin 1. Brain Cell Biol. 36, 173-189 (2008).
    • (2008) Brain Cell Biol. , vol.36 , pp. 173-189
    • Tokumaru, H.1    Shimizu-Okabe, C.2    Abe, T.3
  • 69
    • 60749096805 scopus 로고    scopus 로고
    • Concurrent binding of complexin and synaptotagmin to liposome-embedded SNARE complexes (dagger)
    • Chicka, M.C. & Chapman, E.R. Concurrent binding of complexin and synaptotagmin to liposome-embedded SNARE complexes (dagger). Biochemistry 48, 657-659 (2009).
    • (2009) Biochemistry , vol.48 , pp. 657-659
    • Chicka, M.C.1    Chapman, E.R.2
  • 70
    • 51049114297 scopus 로고    scopus 로고
    • Distinct domains of complexins bind SNARE complexes and clamp fusion in vitro
    • Giraudo, C.G. et al. Distinct domains of complexins bind SNARE complexes and clamp fusion in vitro. J. Biol. Chem. 283, 21211-21219 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 21211-21219
    • Giraudo, C.G.1
  • 71
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution
    • Sutton, R.B., Fasshauer, D., Jahn, R. & Brunger, A.T. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution. Nature 395, 347-353 (1998).
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 72
    • 37249032102 scopus 로고    scopus 로고
    • Dynamic personalities of proteins
    • Henzler-Wildman, K. & Kern, D. Dynamic personalities of proteins. Nature 450, 964-972 (2007).
    • (2007) Nature , vol.450 , pp. 964-972
    • Henzler-Wildman, K.1    Kern, D.2
  • 73
    • 38949211822 scopus 로고    scopus 로고
    • Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin-SNAP-25 complex
    • Weninger, K., Bowen, M.E., Choi, U.B., Chu, S. & Brunger, A.T. Accessory proteins stabilize the acceptor complex for synaptobrevin, the 1:1 syntaxin-SNAP-25 complex. Structure 16, 308-320 (2008).
    • (2008) Structure , vol.16 , pp. 308-320
    • Weninger, K.1    Bowen, M.E.2    Choi, U.B.3    Chu, S.4    Brunger, A.T.5
  • 74
    • 7544225920 scopus 로고    scopus 로고
    • Vesicle encapsulation studies reveal that single molecule ribozyme heterogeneities are intrinsic
    • Okumus, B., Wilson, T.J., Lilley, D.M.J. & Ha, T. Vesicle encapsulation studies reveal that single molecule ribozyme heterogeneities are intrinsic. Biophys. J. 87, 2798-2806 (2004).
    • (2004) Biophys. J. , vol.87 , pp. 2798-2806
    • Okumus, B.1    Wilson, T.J.2    Lilley, D.M.J.3    Ha, T.4
  • 75
    • 0035819204 scopus 로고    scopus 로고
    • Immobilization in surface-tethered lipid vesicles as a new tool for single biomolecule spectroscopy
    • Boukobza, E., Sonnenfeld, A. & Haran, G. Immobilization in surface-tethered lipid vesicles as a new tool for single biomolecule spectroscopy. J. Phys. Chem. B 105, 12165-12170 (2001).
    • (2001) J. Phys. Chem. B , vol.105 , pp. 12165-12170
    • Boukobza, E.1    Sonnenfeld, A.2    Haran, G.3
  • 76
    • 34547877610 scopus 로고    scopus 로고
    • Fueling protein-DNA interactions inside porous nanocontainers
    • Cisse, I., Okumus, B., Joo, C. & Ha, T.J. Fueling protein-DNA interactions inside porous nanocontainers. Proc. Natl. Acad. Sci. USA 104, 12646-12650 (2007).
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 12646-12650
    • Cisse, I.1    Okumus, B.2    Joo, C.3    Ha, T.J.4
  • 77
    • 34548792937 scopus 로고    scopus 로고
    • Kinetics of complexin binding to the SNARE complex: Correcting single molecule FRET measurements for hidden events
    • Li, Y., Augustine, G.J. & Weninger, K. Kinetics of complexin binding to the SNARE complex: correcting single molecule FRET measurements for hidden events. Biophys. J. 93, 2178-2187 (2007).
    • (2007) Biophys. J. , vol.93 , pp. 2178-2187
    • Li, Y.1    Augustine, G.J.2    Weninger, K.3
  • 78
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the crystallography and NMR system
    • Brunger, A.T. Version 1.2 of the Crystallography and NMR System. Nat. Protoc. 2, 2728-2733 (2007).
    • (2007) Nat. Protoc. , vol.2 , pp. 2728-2733
    • Brunger, A.T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.