메뉴 건너뛰기




Volumn 289, Issue 10, 2014, Pages 6763-6774

Perturbations of the straight transmembrane α-helical structure of the amyloid precursor protein affect its processing by γ-secretase

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVATION ANALYSIS; BIOLOGICAL MEMBRANES; CYTOLOGY;

EID: 84896692890     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.470781     Document Type: Article
Times cited : (36)

References (51)
  • 1
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease genes, proteins, and therapy
    • Selkoe, D. J. (2001) Alzheimer's disease. genes, proteins, and therapy. Physiol. Rev. 81, 741-766
    • (2001) Physiol. Rev. , vol.81 , pp. 741-766
    • Selkoe, D.J.1
  • 3
    • 51549106517 scopus 로고    scopus 로고
    • Structural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP). Does APP function as a cholesterol sensor?
    • Beel, A. J., Mobley, C. K., Kim, H. J., Tian, F., Hadziselimovic, A., Jap, B., Prestegard, J. H., and Sanders, C. R. (2008) Structural studies of the transmembrane C-terminal domain of the amyloid precursor protein (APP). Does APP function as a cholesterol sensor? Biochemistry 47, 9428-9446
    • (2008) Biochemistry , vol.47 , pp. 9428-9446
    • Beel, A.J.1    Mobley, C.K.2    Kim, H.J.3    Tian, F.4    Hadziselimovic, A.5    Jap, B.6    Prestegard, J.H.7    Sanders, C.R.8
  • 4
    • 71749085062 scopus 로고    scopus 로고
    • Structures of amyloid peptide 1-40, 1-42, and 1-55-the 672-726 fragment of APP-in a membrane environment with implications for interactions with secretase
    • Miyashita, N., Straub, J. E., and Thirumalai, D. (2009) Structures of amyloid peptide 1-40, 1-42, and 1-55-the 672-726 fragment of APP-in a membrane environment with implications for interactions with secretase. J. Am. Chem. Soc. 131, 17843-17852
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 17843-17852
    • Miyashita, N.1    Straub, J.E.2    Thirumalai, D.3
  • 5
    • 0034711953 scopus 로고    scopus 로고
    • TheGXXXGmotif. Aframework for transmembrane helix-helix association
    • Russ, W. P., and Engelman, D. M. (2000) TheGXXXGmotif.Aframework for transmembrane helix-helix association. J. Mol. Biol. 296, 911-919
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 7
    • 43949138917 scopus 로고    scopus 로고
    • Parametrization, molecular dynamics simulation, and calculation of electron spin resonance spectra of a nitroxide spin label on a polyalanine helix
    • Sezer, D., Freed, J. H., and Roux, B. (2008) Parametrization, molecular dynamics simulation, and calculation of electron spin resonance spectra of a nitroxide spin label on a polyalanine helix. J. Phys. Chem. B 112, 5755-5767
    • (2008) J. Phys. Chem. B , vol.112 , pp. 5755-5767
    • Sezer, D.1    Freed, J.H.2    Roux, B.3
  • 8
    • 77954359268 scopus 로고    scopus 로고
    • Aberrant amyloid precursor protein (APP) processing in hereditary forms of Alzheimer disease caused by APP familial Alzheimer disease mutations can be rescued by mutations in the APP GXXXG motif
    • Munter, L. M., Botev, A., Richter, L., Hildebrand, P. W., Althoff, V., Weise, C., Kaden, D., and Multhaup, G. (2010) Aberrant amyloid precursor protein (APP) processing in hereditary forms of Alzheimer disease caused by APP familial Alzheimer disease mutations can be rescued by mutations in the APP GXXXG motif. J. Biol. Chem. 285, 21636-21643
    • (2010) J. Biol. Chem. , vol.285 , pp. 21636-21643
    • Munter, L.M.1    Botev, A.2    Richter, L.3    Hildebrand, P.W.4    Althoff, V.5    Weise, C.6    Kaden, D.7    Multhaup, G.8
  • 9
    • 84896767610 scopus 로고    scopus 로고
    • Replica-exchange molecular dynamics simulations of amyloid precursor protein dimer in membrane
    • Miyashita, N., and Sugita, Y. (2010) Replica-exchange molecular dynamics simulations of amyloid precursor protein dimer in membrane. Qtm. Prob. Wht. Noi. 26, 361-368
    • (2010) Qtm. Prob. Wht. Noi. , vol.26 , pp. 361-368
    • Miyashita, N.1    Sugita, Y.2
  • 10
    • 84889045199 scopus 로고    scopus 로고
    • Structural and dynamic study of the transmembrane domain of the amyloid precursor protein
    • Nadezhdin, K. D., Bocharova, O. V., Bocharov, E. V., and Arseniev, A. S. (2011) Structural and dynamic study of the transmembrane domain of the amyloid precursor protein. Acta Naturae 3, 69-76
    • (2011) Acta Naturae , vol.3 , pp. 69-76
    • Nadezhdin, K.D.1    Bocharova, O.V.2    Bocharov, E.V.3    Arseniev, A.S.4
  • 18
    • 48749137581 scopus 로고
    • Stochastic boundary conditions for molecular dynamics simulations of ST2 water
    • Brunger, A., and Brooks, C. L. (1984) Stochastic boundary conditions for molecular dynamics simulations of ST2 water. Chem. Phys. Lett. 105, 495-500
    • (1984) Chem. Phys. Lett. , vol.105 , pp. 495-500
    • Brunger, A.1    Brooks, C.L.2
  • 19
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation. The Langevin piston method
    • Feller, S. E., Zhang, Y., Pastor, R. W., and Brooks, B. R. (1995) Constant pressure molecular dynamics simulation. The Langevin piston method. J. Chem. Phys. 103, 4613
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 21
    • 77950102787 scopus 로고    scopus 로고
    • Exploring multidimensional free energy landscapes using time-dependent biases on collective variables
    • Henin, J., Fiorin, G., Chipot, C., and Klein, M. L. (2010) Exploring multidimensional free energy landscapes using time-dependent biases on collective variables. J. Chem. Theory Comput. 6, 35-47
    • (2010) J. Chem. Theory Comput. , vol.6 , pp. 35-47
    • Henin, J.1    Fiorin, G.2    Chipot, C.3    Klein, M.L.4
  • 22
    • 0015680655 scopus 로고
    • Clustering using a similarity measure based on shared near neighbors
    • Jarvis, R. A., and Patrick, E. A. (1973) Clustering using a similarity measure based on shared near neighbors. In Computers, IEEE Transactions on C-22, pp. 1025-1034
    • (1973) Computers, IEEE Transactions on C-22 , pp. 1025-1034
    • Jarvis, R.A.1    Patrick, E.A.2
  • 24
    • 84857917265 scopus 로고    scopus 로고
    • MtsslWizard. in silico spin-labeling and generation of distance distributions in PyMOL
    • Hagelueken, G., Ward, R., Naismith, J. H., and Schiemann, O. (2012) MtsslWizard. In silico spin-labeling and generation of distance distributions in PyMOL. Appl. Magn. Reson. 42, 377-391
    • (2012) Appl. Magn. Reson. , vol.42 , pp. 377-391
    • Hagelueken, G.1    Ward, R.2    Naismith, J.H.3    Schiemann, O.4
  • 27
    • 84878382150 scopus 로고    scopus 로고
    • Highly efficient production of the Alzheimer's secretase integral membrane protease complex by a multi-gene stable integration approach
    • Alattia, J. R., Matasci, M., Dimitrov, M., Aeschbach, L., Balasubramanian, S., Hacker, D. L., Wurm, F. M., and Fraering, P. C. (2013) Highly efficient production of the Alzheimer's secretase integral membrane protease complex by a multi-gene stable integration approach. Biotechnol. Bioeng. 110, 1995-2005
    • (2013) Biotechnol. Bioeng. , vol.110 , pp. 1995-2005
    • Alattia, J.R.1    Matasci, M.2    Dimitrov, M.3    Aeschbach, L.4    Balasubramanian, S.5    Hacker, D.L.6    Wurm, F.M.7    Fraering, P.C.8
  • 28
    • 79960170037 scopus 로고    scopus 로고
    • Mercury is a direct and potent secretase inhibitor affecting Notch processing and development in Drosophila
    • Alattia, J. R., Kuraishi, T., Dimitrov, M., Chang, I., Lemaitre, B., and Fraering, P. C. (2011) Mercury is a direct and potent secretase inhibitor affecting Notch processing and development in Drosophila. FASEB J. 25, 2287-2295
    • (2011) FASEB J. , vol.25 , pp. 2287-2295
    • Alattia, J.R.1    Kuraishi, T.2    Dimitrov, M.3    Chang, I.4    Lemaitre, B.5    Fraering, P.C.6
  • 29
    • 0028710015 scopus 로고
    • Local elevation. A method for improving the searching properties of molecular-dynamics simulation
    • Huber, T., Torda, A. E., and van Gunsteren, W. F. (1994) Local elevation. A method for improving the searching properties of molecular-dynamics simulation. J. Comput. Aided Mol. Des. 8, 695-708
    • (1994) J. Comput. Aided Mol. Des. , vol.8 , pp. 695-708
    • Huber, T.1    Torda, A.E.2    Van Gunsteren, W.F.3
  • 30
  • 31
    • 84873508521 scopus 로고    scopus 로고
    • Assembly of the transmembrane domain of E coli PhoQ histidine kinase. Implications for signal transduction from molecular simulations
    • Lemmin, T., Soto, C. S., Clinthorne, G., DeGrado, W. F., and Dal Peraro, M. (2013) Assembly of the transmembrane domain of E. coli PhoQ histidine kinase. Implications for signal transduction from molecular simulations. PLoS Comput. Biol. 9, e1002878
    • (2013) PLoS Comput. Biol. , vol.9
    • Lemmin, T.1    Soto, C.S.2    Clinthorne, G.3    Degrado, W.F.4    Dal Peraro, M.5
  • 32
    • 0014601923 scopus 로고
    • Lipid composition of synaptic plasma membranes isolated from rat brain by zonal centrifugation
    • Cotman, C., Blank, M. L., Moehl, A., and Snyder, F. (1969) Lipid composition of synaptic plasma membranes isolated from rat brain by zonal centrifugation. Biochemistry 8, 4606-4612
    • (1969) Biochemistry , vol.8 , pp. 4606-4612
    • Cotman, C.1    Blank, M.L.2    Moehl, A.3    Snyder, F.4
  • 33
    • 34247129655 scopus 로고    scopus 로고
    • Quantitative molecular ensemble interpretation ofNMRdipolar couplings without restraints
    • Showalter, S. A., and Brüschweiler, R. (2007) Quantitative molecular ensemble interpretation ofNMRdipolar couplings without restraints. J. Am. Chem. Soc. 129, 4158-4159
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 4158-4159
    • Showalter, S.A.1    Brüschweiler, R.2
  • 34
    • 20544436458 scopus 로고    scopus 로고
    • Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins. Applications to C2 domains
    • Malmberg, N. J., and Falke, J. J. (2005) Use of EPR power saturation to analyze the membrane-docking geometries of peripheral proteins. Applications to C2 domains. Annu. Rev. Biophys. Biomol. Struct. 34, 71-90
    • (2005) Annu. Rev. Biophys. Biomol. Struct. , vol.34 , pp. 71-90
    • Malmberg, N.J.1    Falke, J.J.2
  • 36
    • 84859888767 scopus 로고    scopus 로고
    • DEER distance measurements on proteins
    • Jeschke, G. (2012) DEER distance measurements on proteins. Annu. Rev. Phys. Chem. 63, 419-446
    • (2012) Annu. Rev. Phys. Chem. , vol.63 , pp. 419-446
    • Jeschke, G.1
  • 37
    • 58149173445 scopus 로고    scopus 로고
    • Membrane-bound synuclein forms an extended helix. Long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles
    • Georgieva, E. R., Ramlall, T. F., Borbat, P. P., Freed, J. H., and Eliezer, D. (2008) Membrane-bound synuclein forms an extended helix. Long-distance pulsed ESR measurements using vesicles, bicelles, and rodlike micelles. J. Am. Chem. Soc. 130, 12856-12857
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 12856-12857
    • Georgieva, E.R.1    Ramlall, T.F.2    Borbat, P.P.3    Freed, J.H.4    Eliezer, D.5
  • 38
    • 0034836309 scopus 로고    scopus 로고
    • The secondary structure of a membrane-modifying peptide in a supramolecular assembly studied by PELDOR and CW-ESR spectroscopies
    • Milov, A. D., Tsvetkov, Y. D., Formaggio, F., Crisma, M., Toniolo, C., and Raap, J. (2001) The secondary structure of a membrane-modifying peptide in a supramolecular assembly studied by PELDOR and CW-ESR spectroscopies. J. Am. Chem. Soc. 123, 3784-3789
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 3784-3789
    • Milov, A.D.1    Tsvetkov, Y.D.2    Formaggio, F.3    Crisma, M.4    Toniolo, C.5    Raap, J.6
  • 39
    • 34147218123 scopus 로고    scopus 로고
    • Distance measurements on spinlabelled biomacromolecules by pulsed electron paramagnetic resonance
    • Jeschke, G., and Polyhach, Y. (2007) Distance measurements on spinlabelled biomacromolecules by pulsed electron paramagnetic resonance. PCCP 9, 1895-1910
    • (2007) PCCP , vol.9 , pp. 1895-1910
    • Jeschke, G.1    Polyhach, Y.2
  • 40
    • 0034132251 scopus 로고    scopus 로고
    • Deadtime free measurement of dipole-dipole interactions between electron spins
    • Pannier, M., Veit, S., Godt, A., Jeschke, G., and Spiess, H. W. (2000) Deadtime free measurement of dipole-dipole interactions between electron spins. J. Magn. Reson. 142, 331-340
    • (2000) J. Magn. Reson. , vol.142 , pp. 331-340
    • Pannier, M.1    Veit, S.2    Godt, A.3    Jeschke, G.4    Spiess, H.W.5
  • 41
    • 0032476844 scopus 로고    scopus 로고
    • Determination of end-to-end distances in a series of TEMPO diradicals of up to 2. 8 nm length with a new four-pulse double electron electron resonance experiment
    • Martin, R. E., Pannier, M., Diederich, F., Gramlich, V., Hubrich, M., and Spiess, H. W. (1998) Determination of end-to-end distances in a series of TEMPO diradicals of up to 2.8 nm length with a new four-pulse double electron electron resonance experiment. Angew. Chem. Int. Edit. 37, 2834-2837
    • (1998) Angew. Chem. Int. Edit. , vol.37 , pp. 2834-2837
    • Martin, R.E.1    Pannier, M.2    Diederich, F.3    Gramlich, V.4    Hubrich, M.5    Spiess, H.W.6
  • 42
    • 80855144806 scopus 로고    scopus 로고
    • Toward the fourth dimension of membrane protein structure. Insight into dynamics from spin-labeling EPR spectroscopy
    • McHaourab, H. S., Steed, P. R., and Kazmier, K. (2011) Toward the fourth dimension of membrane protein structure. Insight into dynamics from spin-labeling EPR spectroscopy. Structure 19, 1549-1561
    • (2011) Structure , vol.19 , pp. 1549-1561
    • McHaourab, H.S.1    Steed, P.R.2    Kazmier, K.3
  • 45
    • 78650882203 scopus 로고    scopus 로고
    • Shigella flexneri Spa15 crystal structure verified in solution by double electron electron resonance
    • Lillington, J. E., Lovett, J. E., Johnson, S., Roversi, P., Timmel, C. R., and Lea, S. M. (2011) Shigella flexneri Spa15 crystal structure verified in solution by double electron electron resonance. J. Mol. Biol. 405, 427-435
    • (2011) J. Mol. Biol. , vol.405 , pp. 427-435
    • Lillington, J.E.1    Lovett, J.E.2    Johnson, S.3    Roversi, P.4    Timmel, C.R.5    Lea, S.M.6
  • 46
    • 84879843809 scopus 로고    scopus 로고
    • Macromolecular symmetric assembly prediction using swarm intelligence dynamic modeling
    • Degiacomi, M. T., and Dal Peraro, M. (2013) Macromolecular symmetric assembly prediction using swarm intelligence dynamic modeling. Structure 21, 1097-1106
    • (2013) Structure , vol.21 , pp. 1097-1106
    • Degiacomi, M.T.1    Dal Peraro, M.2
  • 48
    • 0037155235 scopus 로고    scopus 로고
    • Cholesterol is an important factor affecting the membrane insertion of amyloid peptide (A1-40), which may potentially inhibit the fibril formation
    • Ji, S. R., Wu, Y., and Sui, S. F. (2002) Cholesterol is an important factor affecting the membrane insertion of amyloid peptide (A1-40), which may potentially inhibit the fibril formation. J. Biol. Chem. 277, 6273-6279
    • (2002) J. Biol. Chem. , vol.277 , pp. 6273-6279
    • Ji, S.R.1    Wu, Y.2    Sui, S.F.3
  • 49
    • 0347753786 scopus 로고    scopus 로고
    • Two types of Alzheimer's amyloid (1-40) peptide membrane interactions. Aggregation preventing transmembrane anchoring versus accelerated surface fibril formation
    • Bokvist, M., Lindström, F., Watts, A., and Gröbner, G. (2004) Two types of Alzheimer's amyloid (1-40) peptide membrane interactions. Aggregation preventing transmembrane anchoring versus accelerated surface fibril formation. J. Mol. Biol. 335, 1039-1049
    • (2004) J. Mol. Biol. , vol.335 , pp. 1039-1049
    • Bokvist, M.1    Lindström, F.2    Watts, A.3    Gröbner, G.4
  • 50
    • 0034576327 scopus 로고    scopus 로고
    • Alzheimer's disease. Its origin at the membrane, evidence and questions
    • Buchet, R., and Pikula, S. (2000) Alzheimer's disease. Its origin at the membrane, evidence and questions. Acta Biochim. Pol. 47, 725-733
    • (2000) Acta Biochim. Pol. , vol.47 , pp. 725-733
    • Buchet, R.1    Pikula, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.