메뉴 건너뛰기




Volumn 7, Issue 10, 2012, Pages

Negative Coupling as a Mechanism for Signal Propagation between C2 Domains of Synaptotagmin I

Author keywords

[No Author keywords available]

Indexed keywords

SYNAPTOTAGMIN I;

EID: 84867150473     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0046748     Document Type: Article
Times cited : (10)

References (57)
  • 1
    • 0036304982 scopus 로고    scopus 로고
    • Synaptotagmin: A Ca2+ sensor that triggers exocytosis?
    • Chapman ER, (2002) Synaptotagmin: A Ca2+ sensor that triggers exocytosis? Nat Rev Mol Cell Biol 3: 1-11.
    • (2002) Nat Rev Mol Cell Biol , vol.3 , pp. 1-11
    • Chapman, E.R.1
  • 2
    • 0028880456 scopus 로고
    • Complexins: cytosolic proteins that regulate SNAP receptor function
    • McMahon HT, Missler M, Li C, Südhof TC, (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
  • 3
    • 0042858417 scopus 로고    scopus 로고
    • Cell biology of the presynaptic terminal
    • Murthy VN, De Camili P, (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 Camili, P.2
  • 4
    • 2942556680 scopus 로고    scopus 로고
    • The synaptic vesicle cycle
    • Südhof TC, (2004) The synaptic vesicle cycle. Annu Rev Neurosci 27: 509-547.
    • (2004) Annu Rev Neurosci , vol.27 , pp. 509-547
    • Südhof, T.C.1
  • 5
    • 33748605056 scopus 로고    scopus 로고
    • A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis
    • Tang J, Maximov A, Shin OH, Dai H, Rizo J, et al. (2006) A complexin/synaptotagmin 1 switch controls fast synaptic vesicle exocytosis. Cell 126: 1175-1187.
    • (2006) Cell , vol.126 , pp. 1175-1187
    • Tang, J.1    Maximov, A.2    Shin, O.H.3    Dai, H.4    Rizo, J.5
  • 6
    • 0026631563 scopus 로고
    • Synaptotagmin: a calcium sensor on the synaptic vesicle surface
    • Brose N, Petrenko AG, Südhof TC, Jahn R, (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
  • 8
    • 0027974130 scopus 로고
    • Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants
    • Littleton JT, Stern M, Perin M, Bellen HJ, (1994) Calcium dependence of neurotransmitter release and rate of spontaneous vesicle fusions are altered in Drosophila synaptotagmin mutants. Proc Natl Acad Sci USA 91: 10888-10892.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10888-10892
    • Littleton, J.T.1    Stern, M.2    Perin, M.3    Bellen, H.J.4
  • 9
    • 33644804207 scopus 로고    scopus 로고
    • Close membrane-membrane proximity induced by Ca2+-dependent multivalent binding of synaptotagmin-1 to phospholipids
    • Araç D, Chen X, Khant HA, Ubach J, Ludtke SJ, et al. (2006) Close membrane-membrane proximity induced by Ca2+-dependent multivalent binding of synaptotagmin-1 to phospholipids. Nat Struct Mol Biol 13: 209-217.
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 209-217
    • Araç, D.1    Chen, X.2    Khant, H.A.3    Ubach, J.4    Ludtke, S.J.5
  • 10
    • 0035924571 scopus 로고    scopus 로고
    • Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine
    • Fernandez I, Araç D, Ubach J, Gerber SH, Shin O, et al. (2001) Three-dimensional structure of the synaptotagmin 1 C2B-domain: synaptotagmin 1 as a phospholipid binding machine. Neuron 32: 1057-1069.
    • (2001) Neuron , vol.32 , pp. 1057-1069
    • Fernandez, I.1    Araç, D.2    Ubach, J.3    Gerber, S.H.4    Shin, O.5
  • 11
    • 0028986240 scopus 로고
    • Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold
    • Sutton RB, Davletov BA, Berghuis AM, Südhof TC, Sprang SR, (1995) Structure of the first C2 domain of synaptotagmin I: a novel Ca2+/phospholipid-binding fold. Cell 80: 929-938.
    • (1995) Cell , vol.80 , pp. 929-938
    • Sutton, R.B.1    Davletov, B.A.2    Berghuis, A.M.3    Südhof, T.C.4    Sprang, S.R.5
  • 12
    • 0032497406 scopus 로고    scopus 로고
    • Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I
    • Zhang X, Rizo J, Südhof TC, (1998) Mechanism of phospholipid binding by the C2A-domain of synaptotagmin I. Biochemistry. 37: 12385-12403.
    • (1998) Biochemistry , vol.37 , pp. 12385-12403
    • Zhang, X.1    Rizo, J.2    Südhof, T.C.3
  • 14
    • 0028970788 scopus 로고
    • Ca2+ regulates the interaction between synaptotagmin and syntaxin 1
    • Chapman ER, Hanson PI, An S, Jahn R, (1995) Ca2+ regulates the interaction between synaptotagmin and syntaxin 1. J Biol Chem 270: 23667-23671.
    • (1995) J Biol Chem , vol.270 , pp. 23667-23671
    • Chapman, E.R.1    Hanson, P.I.2    An, S.3    Jahn, R.4
  • 15
    • 0035904238 scopus 로고    scopus 로고
    • The tandem C2 domains of synaptotagmin contain redundant Ca2+ binding sites that cooperate to engage t-SNAREs and trigger exocytosis
    • Earles CA, Bai J, Wang P, Chapman ER, (2001) The tandem C2 domains of synaptotagmin contain redundant Ca2+ binding sites that cooperate to engage t-SNAREs and trigger exocytosis. J Cell Biol 154: 1117-1123.
    • (2001) J Cell Biol , vol.154 , pp. 1117-1123
    • Earles, C.A.1    Bai, J.2    Wang, P.3    Chapman, E.R.4
  • 16
    • 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 JE, Söllner TH, (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
  • 17
    • 0037117938 scopus 로고    scopus 로고
    • Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis
    • Zhang X, Kim-Miller MJ, Fukuda M, Kowalchyk JA, Martin TFJ, (2002) Ca2+-dependent synaptotagmin binding to SNAP-25 is essential for Ca2+-triggered exocytosis. Neuron 34: 599-611.
    • (2002) Neuron , vol.34 , pp. 599-611
    • Zhang, X.1    Kim-Miller, M.J.2    Fukuda, M.3    Kowalchyk, J.A.4    Martin, T.F.J.5
  • 18
    • 36049007184 scopus 로고    scopus 로고
    • Structure of human synaptotagmin 1 C2AB in the absence of Ca2+ reveals a novel domain association
    • Fuson KL, Montes M, Robert JJ, Sutton RB, (2007) Structure of human synaptotagmin 1 C2AB in the absence of Ca2+ reveals a novel domain association. Biochemistry 46: 13041-13048.
    • (2007) Biochemistry , vol.46 , pp. 13041-13048
    • Fuson, K.L.1    Montes, M.2    Robert, J.J.3    Sutton, R.B.4
  • 19
    • 0034705042 scopus 로고    scopus 로고
    • Calcium triggers an intramolecular association of the C2 domains in synaptotagmin
    • Garcia RA, Forde CE, Godwin HA, (2000) Calcium triggers an intramolecular association of the C2 domains in synaptotagmin. Proc Natl Acad Sci USA 97: 5883-5888.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5883-5888
    • Garcia, R.A.1    Forde, C.E.2    Godwin, H.A.3
  • 20
    • 33747453911 scopus 로고    scopus 로고
    • Position of synaptotagmin I at the membrane interface: cooperative interactions of tandem C2 domains
    • Herrick DZ, Sterbling S, Rasch KA, Hinderliter A, Cafiso DS, (2006) Position of synaptotagmin I at the membrane interface: cooperative interactions of tandem C2 domains. Biochemistry 45: 9668-9674.
    • (2006) Biochemistry , vol.45 , pp. 9668-9674
    • Herrick, D.Z.1    Sterbling, S.2    Rasch, K.A.3    Hinderliter, A.4    Cafiso, D.S.5
  • 21
    • 56749117908 scopus 로고    scopus 로고
    • Conformation and membrane position of the region linking the two C2 domains in synaptotagmin 1 by site-directed spin labeling
    • Huang H, Cafiso DS, (2008) Conformation and membrane position of the region linking the two C2 domains in synaptotagmin 1 by site-directed spin labeling. Biochemistry 47: 12380-12388.
    • (2008) Biochemistry , vol.47 , pp. 12380-12388
    • Huang, H.1    Cafiso, D.S.2
  • 22
    • 0344012489 scopus 로고    scopus 로고
    • Mutations in the effector binding loops in the C2A and C2B domains of synaptotagmin I disrupt exocytosis in a nonadditive manner
    • Wang P, Wang C-T, Bai J, Jackson MB, Chapman ER, (2003) Mutations in the effector binding loops in the C2A and C2B domains of synaptotagmin I disrupt exocytosis in a nonadditive manner. J Biol Chem 278: 47030-47037.
    • (2003) J Biol Chem , vol.278 , pp. 47030-47037
    • Wang, P.1    Wang, C.-T.2    Bai, J.3    Jackson, M.B.4    Chapman, E.R.5
  • 23
    • 38549092474 scopus 로고    scopus 로고
    • Membrane recognition by phospholipid-binding domains
    • Lemmon MA, (2008) Membrane recognition by phospholipid-binding domains. Nat Rev Mol Cell Biol 9: 99-111.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 99-111
    • Lemmon, M.A.1
  • 24
    • 34347235156 scopus 로고    scopus 로고
    • Intrinsic disorder as a mechanism to optomize allosteric coupling in proteins
    • Hilser VJ, Thompson EB, (2007) Intrinsic disorder as a mechanism to optomize allosteric coupling in proteins. Proc Natl Acad Sci USA 104: 8311-8314.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 8311-8314
    • Hilser, V.J.1    Thompson, E.B.2
  • 25
    • 0036088602 scopus 로고    scopus 로고
    • The linkage between protein folding and functional cooperativity: two sides of the same coin?
    • Luque I, Leavitt SA, Freire E, (2002) The linkage between protein folding and functional cooperativity: two sides of the same coin? Annu Rev Biophys Biomol Struct 31: 235-256.
    • (2002) Annu Rev Biophys Biomol Struct , vol.31 , pp. 235-256
    • Luque, I.1    Leavitt, S.A.2    Freire, E.3
  • 26
    • 84864779620 scopus 로고    scopus 로고
    • Mechanism for Calcium Ion Sensing by the C2A Domain of Synaptotagmin I
    • Gauer JW, Sisk R, Murphy JR, Jacobsen H, Sutton RB, et al. (2012) Mechanism for Calcium Ion Sensing by the C2A Domain of Synaptotagmin I. Biophys J. 103: 238-246.
    • (2012) Biophys J , vol.103 , pp. 238-246
    • Gauer, J.W.1    Sisk, R.2    Murphy, J.R.3    Jacobsen, H.4    Sutton, R.B.5
  • 27
    • 0029198941 scopus 로고
    • Differential scanning calorimetry
    • Freire E, (1995) Differential scanning calorimetry. Methods Mol Biol 40: 191-218.
    • (1995) Methods Mol Biol , vol.40 , pp. 191-218
    • Freire, E.1
  • 28
    • 0035231610 scopus 로고    scopus 로고
    • The thermodynamic linkage between protein structure, stability, and function
    • Freire E, (2001) The thermodynamic linkage between protein structure, stability, and function. Methods Mol Biol 168: 37-68.
    • (2001) Methods Mol Biol , vol.168 , pp. 37-68
    • Freire, E.1
  • 29
    • 0029789901 scopus 로고    scopus 로고
    • Calcium-dependent self-association of synaptotagmin I
    • Damer CK, Creutz CE, (1996) Calcium-dependent self-association of synaptotagmin I. J Neurochem. 67: 1661-1668.
    • (1996) J Neurochem , vol.67 , pp. 1661-1668
    • Damer, C.K.1    Creutz, C.E.2
  • 30
    • 0037197677 scopus 로고    scopus 로고
    • Maximal stabilities of reversible two-state proteins
    • Kumar S, Tsai C-J, Nussinov R, (2002) Maximal stabilities of reversible two-state proteins. Biochemistry 41: 5359-5374.
    • (2002) Biochemistry , vol.41 , pp. 5359-5374
    • Kumar, S.1    Tsai, C.-J.2    Nussinov, R.3
  • 31
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study
    • Privalov PL, Khechinashvili NN, (1974) A thermodynamic approach to the problem of stabilization of globular protein structure: a calorimetric study. J Mol Biol 86: 665-684.
    • (1974) J Mol Biol , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 32
    • 0345593605 scopus 로고    scopus 로고
    • A comparison of the energetics of annexin I and annexin V
    • Rosengarth A, Rösgen J, Hinz H-J, Gerke V, (1999) A comparison of the energetics of annexin I and annexin V. J Mol Biol. 288: 1013-1025.
    • (1999) J Mol Biol , vol.288 , pp. 1013-1025
    • Rosengarth, A.1    Rösgen, J.2    Hinz, H.-J.3    Gerke, V.4
  • 33
    • 84864545860 scopus 로고    scopus 로고
    • Thermodynamic dissection of the intrinsically disordered N-terminal domain of human glucocorticoid receptor
    • Li J, Motlagh HN, Chakuroff C, Thompson EB, Hilser VJ, (2012) Thermodynamic dissection of the intrinsically disordered N-terminal domain of human glucocorticoid receptor. J Biol Chem 287: 26777-26787.
    • (2012) J Biol Chem , vol.287 , pp. 26777-26787
    • Li, J.1    Motlagh, H.N.2    Chakuroff, C.3    Thompson, E.B.4    Hilser, V.J.5
  • 34
    • 79955685287 scopus 로고    scopus 로고
    • Allostery in a disordered protein: oxidative modifications to α-synuclein act distally to regulate membrane binding
    • Sevcsik E, Trexler AJ, Dunn JM, Rhoades E, (2011) Allostery in a disordered protein: oxidative modifications to α-synuclein act distally to regulate membrane binding. J Am Chem Soc 133: 7152-7158.
    • (2011) J Am Chem Soc , vol.133 , pp. 7152-7158
    • Sevcsik, E.1    Trexler, A.J.2    Dunn, J.M.3    Rhoades, E.4
  • 36
    • 77954256912 scopus 로고    scopus 로고
    • Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity
    • Garcia-Pino A, Balasubramanian S, Wyns L, Gazit E, De Greve H, et al. (2010) Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity. Cell 142: 101-111.
    • (2010) Cell , vol.142 , pp. 101-111
    • Garcia-Pino, A.1    Balasubramanian, S.2    Wyns, L.3    Gazit, E.4    De Greve, H.5
  • 37
    • 79960066455 scopus 로고    scopus 로고
    • TBP binding-induced folding of the glucocorticoid receptor AF1 domain facilitates its interaction with steroid receptor coactivator-1
    • Khan SH, Ling J, Kumar R, (2011) TBP binding-induced folding of the glucocorticoid receptor AF1 domain facilitates its interaction with steroid receptor coactivator-1. PLoS One 6: e21939.
    • (2011) PLoS One , vol.6
    • Khan, S.H.1    Ling, J.2    Kumar, R.3
  • 40
    • 0032516433 scopus 로고    scopus 로고
    • Toward understanding tryptophan fluorescence in proteins
    • Chen Y, Barkley MD, (1998) Toward understanding tryptophan fluorescence in proteins. Biochemistry 37: 9976-9982.
    • (1998) Biochemistry , vol.37 , pp. 9976-9982
    • Chen, Y.1    Barkley, M.D.2
  • 41
    • 84860871594 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate increases the Ca2+ affinity of synaptotagmin-1 40-fold
    • van den Bogaart G, Meyenberg K, Diederichsen U, Jahn R, (2012) Phosphatidylinositol 4,5-bisphosphate increases the Ca2+ affinity of synaptotagmin-1 40-fold. J Biol Chem 287: 16447-16453.
    • (2012) J Biol Chem , vol.287 , pp. 16447-16453
    • van den Bogaart, G.1    Meyenberg, K.2    Diederichsen, U.3    Jahn, R.4
  • 42
    • 0027180569 scopus 로고
    • Synaptic transmission persists in synaptotagmin mutants of Drosophila
    • DiAntonio A, Parfitt KD, Schwarz TL, (1993) Synaptic transmission persists in synaptotagmin mutants of Drosophila. Cell 73: 1281-1290.
    • (1993) Cell , vol.73 , pp. 1281-1290
    • DiAntonio, A.1    Parfitt, K.D.2    Schwarz, T.L.3
  • 43
    • 0027438591 scopus 로고
    • Mutational analysis of Drosophila synaptotagmin demonstrates its essential role in Ca2+-activated neurotransmitter release
    • Littleton JT, Stern M, Schulze K, Perin M, Bellen HJ, (1993) Mutational analysis of Drosophila synaptotagmin demonstrates its essential role in Ca2+-activated neurotransmitter release. Cell 74: 1125-1134.
    • (1993) Cell , vol.74 , pp. 1125-1134
    • Littleton, J.T.1    Stern, M.2    Schulze, K.3    Perin, M.4    Bellen, H.J.5
  • 44
    • 79961082568 scopus 로고    scopus 로고
    • In vitro system capable of differentiating fast Ca2+-triggered content mixing from lipid exchange for mechanistic studies of neurotransmitter release
    • Kyoung M, Srivastava A, Zhang Y, Diao J, Vrljic M, et al. (2011) In vitro system capable of differentiating fast Ca2+-triggered content mixing from lipid exchange for mechanistic studies of neurotransmitter release. Proc Natl Acad Sci USA 108: 304-313.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 304-313
    • Kyoung, M.1    Srivastava, A.2    Zhang, Y.3    Diao, J.4    Vrljic, M.5
  • 45
    • 77949264921 scopus 로고    scopus 로고
    • Single-molecule FRET-derived model of the synaptotagmin 1-SNARE fusion complex
    • Choi UB, Strop P, Vrljic M, Chu S, Brunger AT, et al. (2010) Single-molecule FRET-derived model of the synaptotagmin 1-SNARE fusion complex. Nat Struct Mol Biol 17: 318-324.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 318-324
    • Choi, U.B.1    Strop, P.2    Vrljic, M.3    Chu, S.4    Brunger, A.T.5
  • 46
    • 78650913081 scopus 로고    scopus 로고
    • Synaptotagmin 1 and SNAREs form a complex that is structurally heterogeneous
    • Lai AL, Huang H, Herrick DZ, Epp N, Cafiso DS, (2011) Synaptotagmin 1 and SNAREs form a complex that is structurally heterogeneous. J Mol Biol 405: 696-706.
    • (2011) J Mol Biol , vol.405 , pp. 696-706
    • Lai, A.L.1    Huang, H.2    Herrick, D.Z.3    Epp, N.4    Cafiso, D.S.5
  • 47
    • 46449093538 scopus 로고    scopus 로고
    • How does synaptotagmin trigger neurotransmitter release?
    • Chapman ER, (2008) How does synaptotagmin trigger neurotransmitter release? Annu Rev Biochem 77: 615-641.
    • (2008) Annu Rev Biochem , vol.77 , pp. 615-641
    • Chapman, E.R.1
  • 48
    • 0141960930 scopus 로고    scopus 로고
    • Synaptotagmin I, a Ca2+ sensor for neurotransmitter release
    • Koh TW, Bellen HJ, (2003) Synaptotagmin I, a Ca2+ sensor for neurotransmitter release. Trends Neurosci 26: 413-422.
    • (2003) Trends Neurosci , vol.26 , pp. 413-422
    • Koh, T.W.1    Bellen, H.J.2
  • 49
    • 33745938170 scopus 로고    scopus 로고
    • Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release
    • Rizo J, Chen X, Araç D, (2006) Unraveling the mechanisms of synaptotagmin and SNARE function in neurotransmitter release. Trends Cell Biol 16: 339-350.
    • (2006) Trends Cell Biol , vol.16 , pp. 339-350
    • Rizo, J.1    Chen, X.2    Araç, D.3
  • 50
    • 79951905332 scopus 로고    scopus 로고
    • Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes
    • Uversky VN, (2011) Multitude of binding modes attainable by intrinsically disordered proteins: a portrait gallery of disorder-based complexes. Chem Soc Rev 40: 1623-1634.
    • (2011) Chem Soc Rev , vol.40 , pp. 1623-1634
    • Uversky, V.N.1
  • 51
    • 79951529500 scopus 로고    scopus 로고
    • Membrane penetration by synaptotagmin is required for coupling calcium binding to vesicle fusion in vivo
    • Paddock BE, Wang Z, Biela LM, Chen K, Getzy MD, et al. (2011) Membrane penetration by synaptotagmin is required for coupling calcium binding to vesicle fusion in vivo. J Neurosci 31: 2248-2257.
    • (2011) J Neurosci , vol.31 , pp. 2248-2257
    • Paddock, B.E.1    Wang, Z.2    Biela, L.M.3    Chen, K.4    Getzy, M.D.5
  • 52
    • 0000914811 scopus 로고
    • The synthesis of a perdeuterated phospholipid: 1,2-dimyristoyl-sn-glycero-3-phosphocholine-d72
    • Kingsley PB, Feigenson GW, (1979) The synthesis of a perdeuterated phospholipid: 1,2-dimyristoyl-sn-glycero-3-phosphocholine-d72. Chem Phys Lipids 24: 135-147.
    • (1979) Chem Phys Lipids , vol.24 , pp. 135-147
    • Kingsley, P.B.1    Feigenson, G.W.2
  • 54
    • 33846811335 scopus 로고    scopus 로고
    • The cooperative response of synaptotagmin 1 C2A. A hypothesis for a Ca2+-driven molecular hammer
    • Kertz JA, Almeida PFF, Frazier AA, Berg AK, Hinderliter A, (2007) The cooperative response of synaptotagmin 1 C2A. A hypothesis for a Ca2+-driven molecular hammer. Biophys J 92: 1409-1418.
    • (2007) Biophys J , vol.92 , pp. 1409-1418
    • Kertz, J.A.1    Almeida, P.F.F.2    Frazier, A.A.3    Berg, A.K.4    Hinderliter, A.5
  • 55
    • 33947209951 scopus 로고    scopus 로고
    • Unfolding thermodynamics of Trp-cage, a 20 residue miniprotein, studied by differential scanning calorimetry and circular dichroism spectroscopy
    • Streicher WW, Makhatadze GI, (2007) Unfolding thermodynamics of Trp-cage, a 20 residue miniprotein, studied by differential scanning calorimetry and circular dichroism spectroscopy. Biochemistry 46: 2876-2880.
    • (2007) Biochemistry , vol.46 , pp. 2876-2880
    • Streicher, W.W.1    Makhatadze, G.I.2
  • 56
    • 0026684671 scopus 로고
    • Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water
    • Spolar RS, Livingstone JR, Record MT, (1992) Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water. Biochemistry 31: 3947-3955.
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar, R.S.1    Livingstone, J.R.2    Record, M.T.3
  • 57
    • 0346156183 scopus 로고    scopus 로고
    • Estimating parameter precision in nonlinear least squares with excel's solver
    • De Levie R, (1999) Estimating parameter precision in nonlinear least squares with excel's solver. J Chem Educ 76: 1594-1598.
    • (1999) J Chem Educ , vol.76 , pp. 1594-1598
    • De Levie, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.