메뉴 건너뛰기




Volumn 111, Issue 36, 2014, Pages 13069-13074

Direct single-molecule observation of calcium-dependent misfolding in human neuronal calcium sensor-1

Author keywords

Conformational dynamics; NCS 1; Off pathway intermediate; Optical trapping; Protein folding

Indexed keywords

CALCIUM; FREQUENIN CALCIUM SENSOR PROTEINS; NEURONAL CALCIUM SENSOR; NEUROPEPTIDE;

EID: 84907001202     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1401065111     Document Type: Article
Times cited : (43)

References (63)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75:333-366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 84873105668 scopus 로고    scopus 로고
    • Frustration in the energy landscapes of multidomain protein misfolding
    • Zheng W, Schafer NP, Wolynes PG (2013) Frustration in the energy landscapes of multidomain protein misfolding. Proc Natl Acad Sci USA 110(5):1680-1685.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.5 , pp. 1680-1685
    • Zheng, W.1    Schafer, N.P.2    Wolynes, P.G.3
  • 3
    • 79959830883 scopus 로고    scopus 로고
    • Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins
    • Borgia MB, et al. (2011) Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins. Nature 474(7353):662-665.
    • (2011) Nature , vol.474 , Issue.7353 , pp. 662-665
    • Borgia, M.B.1
  • 4
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M (2011) Molecular chaperones in protein folding and proteostasis. Nature 475(7356):324-332.
    • (2011) Nature , vol.475 , Issue.7356 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 5
    • 0037264120 scopus 로고    scopus 로고
    • Unfolding the role of protein misfolding in neurodegenerative diseases
    • Soto C (2003) Unfolding the role of protein misfolding in neurodegenerative diseases. Nat Rev Neurosci 4(1):49-60.
    • (2003) Nat Rev Neurosci , vol.4 , Issue.1 , pp. 49-60
    • Soto, C.1
  • 6
    • 84861357149 scopus 로고    scopus 로고
    • Protein aggregation and misfolding: Good or evil?
    • Pastore A, Temussi P (2012) Protein aggregation and misfolding: Good or evil? J Phys Condens Matter 24(24):244101.
    • (2012) J Phys Condens Matter , vol.24 , Issue.24 , pp. 244101
    • Pastore, A.1    Temussi, P.2
  • 7
    • 70849113863 scopus 로고    scopus 로고
    • Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization
    • Teilum K, et al. (2009) Transient structural distortion of metal-free Cu/Zn superoxide dismutase triggers aberrant oligomerization. Proc Natl Acad Sci USA 106(43):18273-18278.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.43 , pp. 18273-18278
    • Teilum, K.1
  • 8
    • 57749098600 scopus 로고    scopus 로고
    • Amyloid formation by globular proteins under native conditions
    • Chiti F, Dobson CM (2009) Amyloid formation by globular proteins under native conditions. Nat Chem Biol 5(1):15-22.
    • (2009) Nat Chem Biol , vol.5 , Issue.1 , pp. 15-22
    • Chiti, F.1    Dobson, C.M.2
  • 9
    • 84874588889 scopus 로고    scopus 로고
    • Global structural motions from the strain of a single hydrogen bond
    • Danielsson J, et al. (2013) Global structural motions from the strain of a single hydrogen bond. Proc Natl Acad Sci USA 110(10):3829-3834.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.10 , pp. 3829-3834
    • Danielsson, J.1
  • 10
    • 78651468727 scopus 로고    scopus 로고
    • Conformational conversion during amyloid formation at atomic resolution
    • Eichner T, Kalverda AP, Thompson GS, Homans SW, Radford SE (2011) Conformational conversion during amyloid formation at atomic resolution. Mol Cell 41(2): 161-172.
    • (2011) Mol Cell , vol.41 , Issue.2 , pp. 161-172
    • Eichner, T.1    Kalverda, A.P.2    Thompson, G.S.3    Homans, S.W.4    Radford, S.E.5
  • 11
    • 1442330474 scopus 로고    scopus 로고
    • From conversion to aggregation: Protofibril formation of the prion protein
    • DeMarco ML, Daggett V (2004) From conversion to aggregation: Protofibril formation of the prion protein. Proc Natl Acad Sci USA 101(8):2293-2298.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.8 , pp. 2293-2298
    • DeMarco, M.L.1    Daggett, V.2
  • 12
    • 28444454101 scopus 로고    scopus 로고
    • Amyloid fibril formation can proceed from different conformations of a partially unfolded protein
    • Calamai M, Chiti F, Dobson CM (2005) Amyloid fibril formation can proceed from different conformations of a partially unfolded protein. Biophys J 89(6):4201-4210.
    • (2005) Biophys J , vol.89 , Issue.6 , pp. 4201-4210
    • Calamai, M.1    Chiti, F.2    Dobson, C.M.3
  • 13
    • 78649885501 scopus 로고    scopus 로고
    • Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain
    • Gianni S, et al. (2010) Structural characterization of a misfolded intermediate populated during the folding process of a PDZ domain. Nat Struct Mol Biol 17(12): 1431-1437.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.12 , pp. 1431-1437
    • Gianni, S.1
  • 14
    • 84873525793 scopus 로고    scopus 로고
    • Force as a single molecule probe of multidimensional protein energy landscapes
    • Zoldák G, Rief M (2013) Force as a single molecule probe of multidimensional protein energy landscapes. Curr Opin Struct Biol 23(1):48-57.
    • (2013) Curr Opin Struct Biol , vol.23 , Issue.1 , pp. 48-57
    • Zoldák, G.1    Rief, M.2
  • 16
    • 25444512161 scopus 로고    scopus 로고
    • Direct observation of the three-state folding of a single protein molecule
    • Cecconi C, Shank EA, Bustamante C, Marqusee S (2005) Direct observation of the three-state folding of a single protein molecule. Science 309(5743):2057-2060.
    • (2005) Science , vol.309 , Issue.5743 , pp. 2057-2060
    • Cecconi, C.1    Shank, E.A.2    Bustamante, C.3    Marqusee, S.4
  • 18
    • 77956549614 scopus 로고    scopus 로고
    • Complex unfolding kinetics of single-domain proteins in the presence of force
    • Schlierf M, Yew ZT, Rief M, Paci E (2010) Complex unfolding kinetics of single-domain proteins in the presence of force. Biophys J 99(5):1620-1627.
    • (2010) Biophys J , vol.99 , Issue.5 , pp. 1620-1627
    • Schlierf, M.1    Yew, Z.T.2    Rief, M.3    Paci, E.4
  • 19
    • 84881480267 scopus 로고    scopus 로고
    • Reshaping of the conformational search of a protein by the chaperone trigger factor
    • Mashaghi A, et al. (2013) Reshaping of the conformational search of a protein by the chaperone trigger factor. Nature 500(7460):98-101.
    • (2013) Nature , vol.500 , Issue.7460 , pp. 98-101
    • Mashaghi, A.1
  • 20
    • 84859465192 scopus 로고    scopus 로고
    • Direct observation of multiple misfolding pathways in a single prion protein molecule
    • Yu H, et al. (2012) Direct observation of multiple misfolding pathways in a single prion protein molecule. Proc Natl Acad Sci USA 109(14):5283-5288.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.14 , pp. 5283-5288
    • Yu, H.1
  • 21
    • 80055087629 scopus 로고    scopus 로고
    • The complex folding network of single calmodulin molecules
    • Stigler J, Ziegler F, Gieseke A, Gebhardt JC, Rief M (2011) The complex folding network of single calmodulin molecules. Science 334(6055):512-516.
    • (2011) Science , vol.334 , Issue.6055 , pp. 512-516
    • Stigler, J.1    Ziegler, F.2    Gieseke, A.3    Gebhardt, J.C.4    Rief, M.5
  • 22
    • 84859577753 scopus 로고    scopus 로고
    • Single-molecule observation of helix staggering, sliding, and coiled coil misfolding
    • Xi Z, Gao Y, Sirinakis G, Guo H, Zhang Y (2012) Single-molecule observation of helix staggering, sliding, and coiled coil misfolding. Proc Natl Acad Sci USA 109(15): 5711-5716.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.15 , pp. 5711-5716
    • Xi, Z.1    Gao, Y.2    Sirinakis, G.3    Guo, H.4    Zhang, Y.5
  • 23
    • 79952837043 scopus 로고    scopus 로고
    • Relating form and function of EF-hand calcium binding proteins
    • Chazin WJ (2011) Relating form and function of EF-hand calcium binding proteins. Acc Chem Res 44(3):171-179.
    • (2011) Acc Chem Res , vol.44 , Issue.3 , pp. 171-179
    • Chazin, W.J.1
  • 24
    • 79151471605 scopus 로고    scopus 로고
    • Neuronal calcium sensor-1 regulation of calcium channels, secretion, and neuronal outgrowth
    • Weiss JL, Hui H, Burgoyne RD (2010) Neuronal calcium sensor-1 regulation of calcium channels, secretion, and neuronal outgrowth. Cell Mol Neurobiol 30(8):1283-1292.
    • (2010) Cell Mol Neurobiol , vol.30 , Issue.8 , pp. 1283-1292
    • Weiss, J.L.1    Hui, H.2    Burgoyne, R.D.3
  • 25
    • 84871311574 scopus 로고    scopus 로고
    • The neuronal calcium sensor protein Acrocalcin: A potential target of calmodulin regulation during development in the coral Acropora millepora
    • Reyes-Bermudez A, Miller DJ, Sprungala S (2012) The neuronal calcium sensor protein Acrocalcin: A potential target of calmodulin regulation during development in the coral Acropora millepora. PLoS ONE 7(12):e51689.
    • (2012) PLoS ONE , vol.7 , Issue.12 , pp. e51689
    • Reyes-Bermudez, A.1    Miller, D.J.2    Sprungala, S.3
  • 26
    • 0034744301 scopus 로고    scopus 로고
    • Ca2+ signaling via the neuronal calcium sensor-1 regulates associative learning and memory in C. elegans
    • Gomez M, et al. (2001) Ca2+ signaling via the neuronal calcium sensor-1 regulates associative learning and memory in C. elegans. Neuron 30(1):241-248.
    • (2001) Neuron , vol.30 , Issue.1 , pp. 241-248
    • Gomez, M.1
  • 27
    • 69949092092 scopus 로고    scopus 로고
    • NCS-1 in the dentate gyrus promotes exploration, synaptic plasticity, and rapid acquisition of spatial memory
    • Saab BJ, et al. (2009) NCS-1 in the dentate gyrus promotes exploration, synaptic plasticity, and rapid acquisition of spatial memory. Neuron 63(5):643-656.
    • (2009) Neuron , vol.63 , Issue.5 , pp. 643-656
    • Saab, B.J.1
  • 28
    • 0027219753 scopus 로고
    • Frequenin - A novel calcium-binding protein that modulates synaptic efficacy in the Drosophila nervous system
    • Pongs O, et al. (1993) Frequenin - A novel calcium-binding protein that modulates synaptic efficacy in the Drosophila nervous system. Neuron 11(1):15-28.
    • (1993) Neuron , vol.11 , Issue.1 , pp. 15-28
    • Pongs, O.1
  • 29
    • 0032575378 scopus 로고    scopus 로고
    • Neuronal Ca2+ sensor 1, the mammalian homologue of frequenin, is expressed in chromaffin and PC12 cells and regulates neurosecretion from dense-core granules
    • McFerran BW, Graham ME, Burgoyne RD (1998) Neuronal Ca2+ sensor 1, the mammalian homologue of frequenin, is expressed in chromaffin and PC12 cells and regulates neurosecretion from dense-core granules. J Biol Chem 273(35):22768-22772.
    • (1998) J Biol Chem , vol.273 , Issue.35 , pp. 22768-22772
    • McFerran, B.W.1    Graham, M.E.2    Burgoyne, R.D.3
  • 30
    • 84859313675 scopus 로고    scopus 로고
    • NCS-1 associates with adenosine A(2A) receptors and modulates receptor function
    • Navarro G, et al. (2012) NCS-1 associates with adenosine A(2A) receptors and modulates receptor function. Front Mol Neurosci 5(5):53.
    • (2012) Front Mol Neurosci , vol.5 , Issue.5 , pp. 53
    • Navarro, G.1
  • 31
    • 0036813090 scopus 로고    scopus 로고
    • Interaction with neuronal calcium sensor NCS-1 mediates desensitization of the D2 dopamine receptor
    • Kabbani N, Negyessy L, Lin R, Goldman-Rakic P, Levenson R (2002) Interaction with neuronal calcium sensor NCS-1 mediates desensitization of the D2 dopamine receptor. J Neurosci 22(19):8476-8486.
    • (2002) J Neurosci , vol.22 , Issue.19 , pp. 8476-8486
    • Kabbani, N.1    Negyessy, L.2    Lin, R.3    Goldman-Rakic, P.4    Levenson, R.5
  • 32
    • 0037422584 scopus 로고    scopus 로고
    • Up-regulation of neuronal calcium sensor-1 (NCS-1) in the prefrontal cortex of schizophrenic and bipolar patients
    • Koh PO, et al. (2003) Up-regulation of neuronal calcium sensor-1 (NCS-1) in the prefrontal cortex of schizophrenic and bipolar patients. Proc Natl Acad Sci USA 100(1): 313-317.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.1 , pp. 313-317
    • Koh, P.O.1
  • 33
    • 57049170205 scopus 로고    scopus 로고
    • Mutations in the calcium-related gene IL1RAPL1 are associated with autism
    • Piton A, et al.; S2D team (2008) Mutations in the calcium-related gene IL1RAPL1 are associated with autism. Hum Mol Genet 17(24):3965-3974.
    • (2008) Hum Mol Genet , vol.17 , Issue.24 , pp. 3965-3974
    • Piton, A.1
  • 34
    • 77956289293 scopus 로고    scopus 로고
    • Structural and functional deficits in a neuronal calcium sensor-1 mutant identified in a case of autistic spectrum disorder
    • Handley MT, Lian LY, Haynes LP, Burgoyne RD (2010) Structural and functional deficits in a neuronal calcium sensor-1 mutant identified in a case of autistic spectrum disorder. PLoS ONE 5(5):e10534.
    • (2010) PLoS ONE , vol.5 , Issue.5 , pp. e10534
    • Handley, M.T.1    Lian, L.Y.2    Haynes, L.P.3    Burgoyne, R.D.4
  • 35
    • 39049105983 scopus 로고    scopus 로고
    • Regulatory and structural EF-hand motifs of neuronal calcium sensor-1: Mg 2+ modulates Ca 2+ binding, Ca 2+ -induced conformational changes, and equilibrium unfolding transitions
    • Aravind P, et al. (2008) Regulatory and structural EF-hand motifs of neuronal calcium sensor-1: Mg 2+ modulates Ca 2+ binding, Ca 2+ -induced conformational changes, and equilibrium unfolding transitions. J Mol Biol 376(4):1100-1115.
    • (2008) J Mol Biol , vol.376 , Issue.4 , pp. 1100-1115
    • Aravind, P.1
  • 36
    • 84868095059 scopus 로고    scopus 로고
    • Calcium-dependent folding of single calmodulin molecules
    • Stigler J, Rief M (2012) Calcium-dependent folding of single calmodulin molecules. Proc Natl Acad Sci USA 109(44):17814-17819.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.44 , pp. 17814-17819
    • Stigler, J.1    Rief, M.2
  • 37
    • 34548510353 scopus 로고    scopus 로고
    • Energetics of the native energy landscape of a two-domain calcium sensor protein: Distinct folding features of the two domains
    • Mukherjee S, Mohan PM, Kuchroo K, Chary KV (2007) Energetics of the native energy landscape of a two-domain calcium sensor protein: Distinct folding features of the two domains. Biochemistry 46(35):9911-9919.
    • (2007) Biochemistry , vol.46 , Issue.35 , pp. 9911-9919
    • Mukherjee, S.1    Mohan, P.M.2    Kuchroo, K.3    Chary, K.V.4
  • 38
    • 84856752266 scopus 로고    scopus 로고
    • 2+- activated state
    • 2+- activated state. J Mol Biol 417(1-2): 51-64.
    • (2012) J Mol Biol , vol.417 , Issue.1-2 , pp. 51-64
    • Heidarsson, P.O.1
  • 39
    • 84885431553 scopus 로고    scopus 로고
    • Single-molecule folding mechanism of an EF-hand neuronal calcium sensor
    • Heidarsson PO, et al. (2013) Single-molecule folding mechanism of an EF-hand neuronal calcium sensor. Structure 21(10):1812-1821.
    • (2013) Structure , vol.21 , Issue.10 , pp. 1812-1821
    • Heidarsson, P.O.1
  • 40
    • 84867498851 scopus 로고    scopus 로고
    • A highly compliant protein native state with a sponta-neous- like mechanical unfolding pathway
    • Heidarsson PO, et al. (2012) A highly compliant protein native state with a sponta-neous- like mechanical unfolding pathway. J Am Chem Soc 134(41):17068-17075.
    • (2012) J Am Chem Soc , vol.134 , Issue.41 , pp. 17068-17075
    • Heidarsson, P.O.1
  • 41
    • 0028071373 scopus 로고
    • Entropic elasticity of lambdaphage DNA
    • Bustamante C, Marko JF, Siggia ED, Smith S (1994) Entropic elasticity of lambdaphage DNA. Science 265(5178):1599-1600.
    • (1994) Science , vol.265 , Issue.5178 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.F.2    Siggia, E.D.3    Smith, S.4
  • 42
    • 0141987862 scopus 로고    scopus 로고
    • Local calcium signaling in neurons
    • Augustine GJ, Santamaria F, Tanaka K (2003) Local calcium signaling in neurons. Neuron 40(2):331-346.
    • (2003) Neuron , vol.40 , Issue.2 , pp. 331-346
    • Augustine, G.J.1    Santamaria, F.2    Tanaka, K.3
  • 43
    • 33847103184 scopus 로고    scopus 로고
    • Neuronal calcium sensor proteins: Generating diversity in neuronal Ca2+ signalling
    • Burgoyne RD (2007) Neuronal calcium sensor proteins: Generating diversity in neuronal Ca2+ signalling. Nat Rev Neurosci 8(3):182-193.
    • (2007) Nat Rev Neurosci , vol.8 , Issue.3 , pp. 182-193
    • Burgoyne, R.D.1
  • 44
    • 80053560141 scopus 로고    scopus 로고
    • Sensing change: The emerging role of calcium sensors in neuronal disease
    • Seaton G, Hogg EL, Jo J, Whitcomb DJ, Cho K (2011) Sensing change: The emerging role of calcium sensors in neuronal disease. Semin Cell Dev Biol 22(5):530-535.
    • (2011) Semin Cell Dev Biol , vol.22 , Issue.5 , pp. 530-535
    • Seaton, G.1    Hogg, E.L.2    Jo, J.3    Whitcomb, D.J.4    Cho, K.5
  • 46
    • 33746747438 scopus 로고    scopus 로고
    • Analysis of single-molecule FRET trajectories using hidden Markov modeling
    • McKinney SA, Joo C, Ha T (2006) Analysis of single-molecule FRET trajectories using hidden Markov modeling. Biophys J 91(5):1941-1951.
    • (2006) Biophys J , vol.91 , Issue.5 , pp. 1941-1951
    • McKinney, S.A.1    Joo, C.2    Ha, T.3
  • 47
    • 80051580720 scopus 로고    scopus 로고
    • Highly anisotropic stability and folding kinetics of a single coiled coil protein under mechanical tension
    • Gao Y, Sirinakis G, Zhang Y (2011) Highly anisotropic stability and folding kinetics of a single coiled coil protein under mechanical tension. J Am Chem Soc 133(32): 12749-12757.
    • (2011) J Am Chem Soc , vol.133 , Issue.32 , pp. 12749-12757
    • Gao, Y.1    Sirinakis, G.2    Zhang, Y.3
  • 48
    • 0018101150 scopus 로고
    • Models for the specific adhesion of cells to cells
    • Bell GI (1978) Models for the specific adhesion of cells to cells. Science 200(4342): 618-627.
    • (1978) Science , vol.200 , Issue.4342 , pp. 618-627
    • Bell, G.I.1
  • 49
    • 76649093956 scopus 로고    scopus 로고
    • Full distance-resolved folding energy landscape of one single protein molecule
    • Gebhardt JC, Bornschlögl T, Rief M (2010) Full distance-resolved folding energy landscape of one single protein molecule. Proc Natl Acad Sci USA 107(5):2013-2018.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.5 , pp. 2013-2018
    • Gebhardt, J.C.1    Bornschlögl, T.2    Rief, M.3
  • 50
    • 84861563520 scopus 로고    scopus 로고
    • Direct observation of the interconversion of normal and toxic forms of á-synuclein
    • Cremades N, et al. (2012) Direct observation of the interconversion of normal and toxic forms of á-synuclein. Cell 149(5):1048-1059.
    • (2012) Cell , vol.149 , Issue.5 , pp. 1048-1059
    • Cremades, N.1
  • 51
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • Dobson CM (2003) Protein folding and misfolding. Nature 426(6968):884- 890.
    • (2003) Nature , vol.426 , Issue.6968 , pp. 884-890
    • Dobson, C.M.1
  • 52
    • 34249855274 scopus 로고    scopus 로고
    • Real-time control of the energy landscape by force directs the folding of RNA molecules
    • Li PT, Bustamante C, Tinoco I, Jr (2007) Real-time control of the energy landscape by force directs the folding of RNA molecules. Proc Natl Acad Sci USA 104(17):7039-7044.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.17 , pp. 7039-7044
    • Li, P.T.1    Bustamante, C.2    Tinoco, I.3
  • 53
    • 77953231020 scopus 로고    scopus 로고
    • The folding cooperativity of a protein is controlled by its chain topology
    • Shank EA, Cecconi C, Dill JW, Marqusee S, Bustamante C (2010) The folding cooperativity of a protein is controlled by its chain topology. Nature 465(7298):637-640.
    • (2010) Nature , vol.465 , Issue.7298 , pp. 637-640
    • Shank, E.A.1    Cecconi, C.2    Dill, J.W.3    Marqusee, S.4    Bustamante, C.5
  • 54
    • 34447511416 scopus 로고    scopus 로고
    • Protein folding through kinetic discrimination
    • Linse S, Linse B (2007) Protein folding through kinetic discrimination. J Am Chem Soc 129(27):8481-8486.
    • (2007) J Am Chem Soc , vol.129 , Issue.27 , pp. 8481-8486
    • Linse, S.1    Linse, B.2
  • 56
    • 79959511957 scopus 로고    scopus 로고
    • Calcium signaling in cognition and aging-dependent cognitive decline
    • Oliveira AM, Bading H (2011) Calcium signaling in cognition and aging-dependent cognitive decline. Biofactors 37(3):168-174.
    • (2011) Biofactors , vol.37 , Issue.3 , pp. 168-174
    • Oliveira, A.M.1    Bading, H.2
  • 57
    • 84950375413 scopus 로고
    • The role of calcium regulation in brain aging: Reexamination of a hypothesis
    • Khachaturian ZS (1989) The role of calcium regulation in brain aging: Reexamination of a hypothesis. Aging (Milano) 1(1):17-34.
    • (1989) Aging (Milano) , vol.1 , Issue.1 , pp. 17-34
    • Khachaturian, Z.S.1
  • 58
    • 77549086301 scopus 로고    scopus 로고
    • Calcium and normal brain ageing
    • Toescu EC, Vreugdenhil M (2010) Calcium and normal brain ageing. Cell Calcium 47(2):158-164.
    • (2010) Cell Calcium , vol.47 , Issue.2 , pp. 158-164
    • Toescu, E.C.1    Vreugdenhil, M.2
  • 59
    • 84859313330 scopus 로고    scopus 로고
    • Calcium signalling remodelling and disease
    • Berridge MJ (2012) Calcium signalling remodelling and disease. Biochem Soc Trans 40(2):297-309.
    • (2012) Biochem Soc Trans , vol.40 , Issue.2 , pp. 297-309
    • Berridge, M.J.1
  • 60
    • 84874318986 scopus 로고    scopus 로고
    • Dysregulation of neural calcium signaling in Alzheimer disease, bipolar disorder and schizophrenia
    • Berridge MJ (2013) Dysregulation of neural calcium signaling in Alzheimer disease, bipolar disorder and schizophrenia. Prion 7(1):2-13.
    • (2013) Prion , vol.7 , Issue.1 , pp. 2-13
    • Berridge, M.J.1
  • 61
    • 13344283407 scopus 로고    scopus 로고
    • Role of intracellular calcium signaling in the pathophysiology and pharmacotherapy of bipolar disorder: Current status
    • Warsh JJ, Andreopoulos S, Li PP (2004) Role of intracellular calcium signaling in the pathophysiology and pharmacotherapy of bipolar disorder: Current status. Clin Neurosci Res 4(3-4):201-213.
    • (2004) Clin Neurosci Res , vol.4 , Issue.3-4 , pp. 201-213
    • Warsh, J.J.1    Andreopoulos, S.2    Li, P.P.3
  • 62
    • 45849099139 scopus 로고    scopus 로고
    • Protein-DNA chimeras for single molecule mechanical folding studies with the optical tweezers
    • Cecconi C, Shank EA, Dahlquist FW, Marqusee S, Bustamante C (2008) Protein-DNA chimeras for single molecule mechanical folding studies with the optical tweezers. Eur Biophys J 37(6):729-738.
    • (2008) Eur Biophys J , vol.37 , Issue.6 , pp. 729-738
    • Cecconi, C.1    Shank, E.A.2    Dahlquist, F.W.3    Marqusee, S.4    Bustamante, C.5
  • 63
    • 0035957720 scopus 로고    scopus 로고
    • Reversible unfolding of single RNA molecules by mechanical force
    • Liphardt J, Onoa B, Smith SB, Tinoco I, Jr, Bustamante C (2001) Reversible unfolding of single RNA molecules by mechanical force. Science 292(5517):733-737.
    • (2001) Science , vol.292 , Issue.5517 , pp. 733-737
    • Liphardt, J.1    Onoa, B.2    Smith, S.B.3    Tinoco, I.4    Bustamante, C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.