메뉴 건너뛰기




Volumn 10, Issue 2-3, 2006, Pages 277-290

Presenilin structure in mechanisms leading to Alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; PRESENILIN 1; PRESENILIN 2;

EID: 33751088006     PISSN: 13872877     EISSN: None     Source Type: Journal    
DOI: 10.3233/JAD-2006-102-312     Document Type: Review
Times cited : (10)

References (99)
  • 1
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • G.G. Glenner and C.W. Wong, Alzheimer's disease: initial report of the purification and characterization of a novel cerebrovascular amyloid protein, Biochemical and Biophysical Research Communications 120 (1984), 885-890.
    • (1984) Biochemical and Biophysical Research Communications , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 2
    • 31944449691 scopus 로고    scopus 로고
    • Perutz's Cylindrical double - β - Stranded subunit structure for β-amyloids in water also applies to their channel-forming structures in membranes
    • S.J. Singer and N.N. Dewji, Perutz's Cylindrical double - β - stranded subunit structure for β-amyloids in water also applies to their channel-forming structures in membranes, Proc Natl Acad Sci USA 103 (2006), 1546-1550.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1546-1550
    • Singer, S.J.1    Dewji, N.N.2
  • 3
    • 0028170818 scopus 로고
    • Cell biology of the amyloid β-protein precursor and the mechanisms of Alzheimer's disease
    • D. Selkoe, Cell biology of the amyloid β-protein precursor and the mechanisms of Alzheimer's disease, Annual Review of Cell Biology 10 (1994), 373-403.
    • (1994) Annual Review of Cell Biology , vol.10 , pp. 373-403
    • Selkoe, D.1
  • 6
    • 0030033587 scopus 로고    scopus 로고
    • Genetic clues to Alzheimer's disease
    • N.N. Dewji and S.J. Singer, Genetic clues to Alzheimer's disease, Science 271 (1996), 159-160.
    • (1996) Science , vol.271 , pp. 159-160
    • Dewji, N.N.1    Singer, S.J.2
  • 7
    • 0025916146 scopus 로고
    • Interaction of bride of sevenless membrane - Bound ligand and the sevenless tyrosine-kinase receptor
    • H. Kramer, R.L. Cagan and S.L. Zipursky, Interaction of bride of sevenless membrane - bound ligand and the sevenless tyrosine-kinase receptor, Nature 352 (1991), 207-212.
    • (1991) Nature , vol.352 , pp. 207-212
    • Kramer, H.1    Cagan, R.L.2    Zipursky, S.L.3
  • 8
    • 0026632816 scopus 로고
    • The bride of sevenless and sevenless interaction: Internalization of a transmembrane ligand
    • R.L. Cagan, H. Kramer, A.C. Hart and S.L. Zipursky, The bride of sevenless and sevenless interaction: internalization of a transmembrane ligand, Cell 69 (1992), 393-399.
    • (1992) Cell , vol.69 , pp. 393-399
    • Cagan, R.L.1    Kramer, H.2    Hart, A.C.3    Zipursky, S.L.4
  • 9
    • 0029116848 scopus 로고
    • Facilitation of lin-12-mediated signaling by Sel-12, a Caenorhabdtis elegans 5182 Alzheimer's disease gene
    • D. Levitan and I. Greenwald, Facilitation of lin-12-mediated signaling by Sel-12, a Caenorhabdtis elegans 5182 Alzheimer's disease gene, Nature 377 (1995), 351-354.
    • (1995) Nature , vol.377 , pp. 351-354
    • Levitan, D.1    Greenwald, I.2
  • 10
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing β-secretase and presenilin-1 requires APP
    • A. Kamal, A. Almenar-Queralt, J.F. LeBlanc, E.A. Roberts and L.S.B. Goldstein, Kinesin-mediated axonal transport of a membrane compartment containing β-secretase and presenilin-1 requires APP, Nature 414 (2001), 643-648.
    • (2001) Nature , vol.414 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    Leblanc, J.F.3    Roberts, E.A.4    Goldstein, L.S.B.5
  • 11
    • 0026735070 scopus 로고
    • Targeting of cell-surface β-amyloid precursor protein to lysosomes: Alternative processing into amyloid-bearing fragments
    • C. Haass, E.H. Koo, A. Mellon, A.Y. Hung and D.J. Selkoe, Targeting of cell-surface β-amyloid precursor protein to lysosomes: alternative processing into amyloid-bearing fragments, Nature 357 (1992), 500-503.
    • (1992) Nature , vol.357 , pp. 500-503
    • Haass, C.1    Koo, E.H.2    Mellon, A.3    Hung, A.Y.4    Selkoe, D.J.5
  • 12
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid beta-protein involves the endoctyic pathway
    • E.H. Koo and S.L. Squazzo, Evidence that production and release of amyloid beta-protein involves the endoctyic pathway, Journal of Biological Chemistry 269 (1994), 17386-17389.
    • (1994) Journal of Biological Chemistry , vol.269 , pp. 17386-17389
    • Koo, E.H.1    Squazzo, S.L.2
  • 19
    • 0030890399 scopus 로고    scopus 로고
    • Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells
    • T.-W. Kim, W.H. Pettingill, O.G. Hallmark, R.D. Moir, W. Wasco and R.E. Tanzi, Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells, J Biol Chem 272 (1997), 11006-11010.
    • (1997) J Biol Chem , vol.272 , pp. 11006-11010
    • Kim, T.-W.1    Pettingill, W.H.2    Hallmark, O.G.3    Moir, R.D.4    Wasco, W.5    Tanzi, R.E.6
  • 22
    • 0030761059 scopus 로고    scopus 로고
    • Potter, Alzheimer presenilins in the nuclear membrane, interphase kinethochores, and centrosomes suggest a role in chromosome segregation
    • J. Li, M. Xu, H. Zhou, J. Ma and H. Potter, Alzheimer presenilins in the nuclear membrane, interphase kinethochores, and centrosomes suggest a role in chromosome segregation, Cell 90 (1997), 917-927.
    • (1997) Cell , vol.90 , pp. 917-927
    • Li, J.1    Xu, M.2    Zhou, H.3    Ma, J.4    Potter, H.5
  • 24
    • 0030924177 scopus 로고    scopus 로고
    • Cell surface expression of the Alzheimer disease-related presenilin proteins
    • N.N. Dewji and S.J. Singer, Cell surface expression of the Alzheimer disease-related presenilin proteins, Proc Natl Acad Sci USA 94 (1997), 9926-9931.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9926-9931
    • Dewji, N.N.1    Singer, S.J.2
  • 25
    • 0028204224 scopus 로고
    • Calcium ionophore increases amyloid beta peptide production by cultured cells
    • H.W. Querfurth and D.J. Selkoe, Calcium ionophore increases amyloid beta peptide production by cultured cells, Biochemistry 33 (1994), 4450-4461.
    • (1994) Biochemistry , vol.33 , pp. 4450-4461
    • Querfurth, H.W.1    Selkoe, D.J.2
  • 30
    • 10344255689 scopus 로고    scopus 로고
    • Processing of Notch and amyloid precursor protein by γ-secretase distinct
    • L. Tarassishin, Y.I. Yin, B. Bassit and Y.-M. Li, Processing of Notch and amyloid precursor protein by γ-secretase distinct, Proc Natl Acad Sci USA 101 (2004), 17050-17055.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17050-17055
    • Tarassishin, L.1    Yin, Y.I.2    Bassit, B.3    Li, Y.-M.4
  • 31
    • 0036327098 scopus 로고    scopus 로고
    • Presenilin-1 affects trafficking and processing of β-APP and is targeted in a complex with nicastrin to the plasma membrane
    • C. Kaether, S. Lammich, D. Edbauer, M. Ertl, J. Rietdorf, A. Caell, H. Steiner and C. Haass, Presenilin-1 affects trafficking and processing of β-APP and is targeted in a complex with nicastrin to the plasma membrane, JCB 158 (2002), 551-561.
    • (2002) JCB , vol.158 , pp. 551-561
    • Kaether, C.1    Lammich, S.2    Edbauer, D.3    Ertl, M.4    Rietdorf, J.5    Caell, A.6    Steiner, H.7    Haass, C.8
  • 33
    • 4644367903 scopus 로고    scopus 로고
    • Presenilins and gamma-secretase inhibitors affect intracellular trafficking and cell surface localization of the gamma-secretase complex components
    • H. Wang, W.J. Luo, Y.W. Zhang, Y.M. Li, G. Thinakaran, P. Greengard and H. Xu, Presenilins and gamma-secretase inhibitors affect intracellular trafficking and cell surface localization of the gamma-secretase complex components, J Biol Chem 279 (2004), 40560-40566.
    • (2004) J Biol Chem , vol.279 , pp. 40560-40566
    • Wang, H.1    Luo, W.J.2    Zhang, Y.W.3    Li, Y.M.4    Thinakaran, G.5    Greengard, P.6    Xu, H.7
  • 34
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte and R.F. Doolittle, A simple method for displaying the hydropathic character of a protein, Journal of Molecular Biology 157 (1982), 105-132.
    • (1982) Journal of Molecular Biology , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 35
  • 36
    • 0031442678 scopus 로고    scopus 로고
    • The seven-transmembrane spanning topography of the Alzheimer disease-related presenilin proteins in the plasma membranes of cultured cells
    • N.N. Dewji and S.J. Singer, The seven-transmembrane spanning topography of the Alzheimer disease-related presenilin proteins in the plasma membranes of cultured cells, Proc Natl Acad Sci USA 94 (1997), 14025-14030.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14025-14030
    • Dewji, N.N.1    Singer, S.J.2
  • 38
    • 0742305674 scopus 로고    scopus 로고
    • The presenilins turned inside out: Implications for their structures and functions
    • N.N. Dewji, D. Valdez and S.J. Singer, The presenilins turned inside out: implications for their structures and functions, Proc Natl Acad Sci USA 101 (2004), 1057-1062.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1057-1062
    • Dewji, N.N.1    Valdez, D.2    Singer, S.J.3
  • 40
    • 0028926860 scopus 로고
    • Insertion of the polytopic membrane protein lactose permease occurs by multiple mechanisms
    • K.H. Zen, T.G. Consler and H.R. Kaback, Insertion of the polytopic membrane protein lactose permease occurs by multiple mechanisms, Biochemistry 34 (1995), 3430-3437.
    • (1995) Biochemistry , vol.34 , pp. 3430-3437
    • Zen, K.H.1    Consler, T.G.2    Kaback, H.R.3
  • 41
    • 0029997381 scopus 로고    scopus 로고
    • Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation
    • K. Nishiyama, T. Suzuki and H. Tokuda, Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation, Cell 85 (1996), 71-81.
    • (1996) Cell , vol.85 , pp. 71-81
    • Nishiyama, K.1    Suzuki, T.2    Tokuda, H.3
  • 42
    • 0037301459 scopus 로고    scopus 로고
    • Evidence for mixed membrane topology of the Newcastle disease virus fusion protein
    • L.W. NcGinnes, J.N. Reitter, K. Gravel and G. Marrison, Evidence for mixed membrane topology of the Newcastle disease virus fusion protein, J Virol 77 (2003), 1951-1963.
    • (2003) J Virol , vol.77 , pp. 1951-1963
    • Ncginnes, L.W.1    Reitter, J.N.2    Gravel, K.3    Marrison, G.4
  • 43
    • 0030937576 scopus 로고    scopus 로고
    • Topological rules for membrane protein assembly in eurkaryotic cells
    • G. Gafvelin, M. Sakaguchi, H. Andersson and G. Von Heijne, Topological rules for membrane protein assembly in eurkaryotic cells. J Biol Chem 272 (1997), 6119-6127.
    • (1997) J Biol Chem , vol.272 , pp. 6119-6127
    • Gafvelin, G.1    Sakaguchi, M.2    Andersson, H.3    Von Heijne, G.4
  • 44
    • 0027512232 scopus 로고
    • Evidence for an alternate model of human P-glycoprotein structure and biogenesis
    • W.R. Skach, M.C. Clayg and V.R. Lingappa, Evidence for an alternate model of human P-glycoprotein structure and biogenesis, J Biol Chem 268 (1993), 6903-6908.
    • (1993) J Biol Chem , vol.268 , pp. 6903-6908
    • Skach, W.R.1    Clayg, M.C.2    Lingappa, V.R.3
  • 45
    • 33751072463 scopus 로고    scopus 로고
    • Co- and posttranslational translocation mechanisms direct cystic fibrosis transmembrane conductance regulator N terminus transmembrane assembly
    • Y. Lu, X.M. Xiong, A. Helm, K. Kimani, A. Bragin and W.R. Skach, Co- and posttranslational translocation mechanisms direct cystic fibrosis transmembrane conductance regulator N terminus transmembrane assembly, J Biol Chem 270 (1998), 1742-1746.
    • (1998) J Biol Chem , vol.270 , pp. 1742-1746
    • Lu, Y.1    Xiong, X.M.2    Helm, A.3    Kimani, K.4    Bragin, A.5    Skach, W.R.6
  • 46
    • 0028938775 scopus 로고
    • Topological determinants of internal transmembrane segments in Pglycoprotein sequences
    • J.-T. Zhang, C.H. Lee, M. Duthie and V. Ling, Topological determinants of internal transmembrane segments in Pglycoprotein sequences, J Biol Chem 270 (1995), 1742-1746.
    • (1995) J Biol Chem , vol.270 , pp. 1742-1746
    • Zhang, J.-T.1    Lee, C.H.2    Duthie, M.3    Ling, V.4
  • 47
    • 0029988492 scopus 로고    scopus 로고
    • Membrane insertion, processin, and topology of cystic fibrosis transmembrane conductance regulator (CFTR) in microsomal membranes
    • M. Chen and J.-T. Zhang, Membrane insertion, processin, and topology of cystic fibrosis transmembrane conductance regulator (CFTR) in microsomal membranes, Mol Membr Biol 13 (1996), 33-40.
    • (1996) Mol Membr Biol , vol.13 , pp. 33-40
    • Chen, M.1    Zhang, J.-T.2
  • 48
    • 33751084675 scopus 로고    scopus 로고
    • Forced transmembrane orientation of hydrophilic of presenilin 1 and accumulation of processed derivatives in vivo
    • K. Ota, M. Von Sakaguchi, G. Heijne, N. Hamasaki and K. Mihara, Forced transmembrane orientation of hydrophilic of presenilin 1 and accumulation of processed derivatives in vivo, Neuron 17 (1996), 181-190.
    • (1996) Neuron , vol.17 , pp. 181-190
    • Ota, K.1    Von Sakaguchi, M.2    Heijne, G.3    Hamasaki, N.4    Mihara, K.5
  • 50
    • 0030890399 scopus 로고    scopus 로고
    • Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells
    • T.-W. Kim, W.H. Pettingill, O.G. Hallmark, R.D. Moir, W. Wasco and R.E. Tanzi, Endoproteolytic cleavage and proteasomal degradation of presenilin 2 in transfected cells, J Biol Chem 272 (1997), 11006-11010.
    • (1997) J Biol Chem , vol.272 , pp. 11006-11010
    • Kim, T.-W.1    Pettingill, W.H.2    Hallmark, O.G.3    Moir, R.D.4    Wasco, W.5    Tanzi, R.E.6
  • 53
    • 0030761059 scopus 로고    scopus 로고
    • Alzheimer presenilins in the nuclear membrane, interphase kinethochores, and centrosomes suggest a role in chromosome segregation
    • J. Li, M. Xu, H. Zhou, J. Ma and H. Potter, Alzheimer presenilins in the nuclear membrane, interphase kinethochores, and centrosomes suggest a role in chromosome segregation, Cell 90 (1997), 917-927.
    • (1997) Cell , vol.90 , pp. 917-927
    • Li, J.1    Xu, M.2    Zhou, H.3    Ma, J.4    Potter, H.5
  • 55
    • 0030924177 scopus 로고    scopus 로고
    • Cell surface expression of the Alzheimer disease-related presenilin proteins
    • N.N. Dewji and S.J. Singer, Cell surface expression of the Alzheimer disease-related presenilin proteins, Proc Natl Acad Sci USA 94 (1997), 9926-9931.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 9926-9931
    • Dewji, N.N.1    Singer, S.J.2
  • 56
    • 0028204224 scopus 로고
    • Calcium ionophore increases amyloid beta peptide production by cultured cells
    • H.W. Querfurth and D.J. Selkoe, Calcium ionophore increases amyloid beta peptide production by cultured cells, Biochemistry 33 (1994), 4450-4461.
    • (1994) Biochemistry , vol.33 , pp. 4450-4461
    • Querfurth, H.W.1    Selkoe, D.J.2
  • 61
    • 10344255689 scopus 로고    scopus 로고
    • Processing of Notch and amyloid precursor protein by γ-secretase distinct
    • L. Tarassishin, Y.I. Yin, B. Bassit and Y.-M. Li, Processing of Notch and amyloid precursor protein by γ-secretase distinct, Proc Natl Acad Sci USA 101 (2004), 17050-17055.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 17050-17055
    • Tarassishin, L.1    Yin, Y.I.2    Bassit, B.3    Li, Y.-M.4
  • 62
    • 0036327098 scopus 로고    scopus 로고
    • Presenilin-1 affects trafficking and processing of β-APP and is targeted in a complex with nicastrin to the plasma membrane
    • C. Kaether, S. Lammich, D. Edbauer, M. Ertl, J. Rietdorf, A. Caell, H. Steiner and C. Haass, Presenilin-1 affects trafficking and processing of β-APP and is targeted in a complex with nicastrin to the plasma membrane, JCB 158 (2002), 551-561.
    • (2002) JCB , vol.158 , pp. 551-561
    • Kaether, C.1    Lammich, S.2    Edbauer, D.3    Ertl, M.4    Rietdorf, J.5    Caell, A.6    Steiner, H.7    Haass, C.8
  • 64
    • 4644367903 scopus 로고    scopus 로고
    • Presenilins and gamma-secretase inhibitors affect intracellular trafficking and cell surface localization of the gamma-secretase complex components
    • H. Wang, W.J. Luo, Y.W. Zhang, Y.M. Li, G. Thinakaran, P. Greengard and H. Xu, Presenilins and gamma-secretase inhibitors affect intracellular trafficking and cell surface localization of the gamma-secretase complex components, J Biol Chem 279 (2004), 40560-40566.
    • (2004) J Biol Chem , vol.279 , pp. 40560-40566
    • Wang, H.1    Luo, W.J.2    Zhang, Y.W.3    Li, Y.M.4    Thinakaran, G.5    Greengard, P.6    Xu, H.7
  • 65
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • J. Kyte and R.F. Doolittle, A simple method for displaying the hydropathic character of a protein, Journal of Molecular Biology 157 (1982), 105-132.
    • (1982) Journal of Molecular Biology , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 66
  • 67
    • 0031442678 scopus 로고    scopus 로고
    • The seven-transmembrane spanning topography of the Alzheimer disease-related presenilin proteins in the plasma membranes of cultured cells
    • N.N. Dewji and S.J. Singer, The seven-transmembrane spanning topography of the Alzheimer disease-related presenilin proteins in the plasma membranes of cultured cells, Proc Natl Acad Sci USA 94 (1997), 14025-14030.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14025-14030
    • Dewji, N.N.1    Singer, S.J.2
  • 69
    • 0742305674 scopus 로고    scopus 로고
    • The presenilins turned inside out: Implications for their structures and functions
    • N.N. Dewji, D. Valdez and S.J. Singer, The presenilins turned inside out: implications for their structures and functions, Proc Natl Acad Sci USA 101 (2004), 1057-1062.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 1057-1062
    • Dewji, N.N.1    Valdez, D.2    Singer, S.J.3
  • 71
    • 0028926860 scopus 로고
    • Insertion of the polytopic membrane protein lactose permease occurs by multiple mechanisms
    • K.H. Zen, T.G. Consler and H.R. Kaback, Insertion of the polytopic membrane protein lactose permease occurs by multiple mechanisms, Biochemistry 34 (1995), 3430-3437.
    • (1995) Biochemistry , vol.34 , pp. 3430-3437
    • Zen, K.H.1    Consler, T.G.2    Kaback, H.R.3
  • 72
    • 0029997381 scopus 로고    scopus 로고
    • Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation
    • K. Nishiyama, T. Suzuki and H. Tokuda, Inversion of the membrane topology of SecG coupled with SecA-dependent preprotein translocation, Cell 85 (1996), 71-81.
    • (1996) Cell , vol.85 , pp. 71-81
    • Nishiyama, K.1    Suzuki, T.2    Tokuda, H.3
  • 73
    • 0037301459 scopus 로고    scopus 로고
    • Evidence for mixed membrane topology of the Newcastle disease virus fusion protein
    • L.W. NcGinnes, J.N. Reitter, K. Gravel and G. Marrison, Evidence for mixed membrane topology of the Newcastle disease virus fusion protein, J Virol 77 (2003), 1951-1963.
    • (2003) J Virol , vol.77 , pp. 1951-1963
    • NcGinnes, L.W.1    Reitter, J.N.2    Gravel, K.3    Marrison, G.4
  • 74
    • 0030937576 scopus 로고    scopus 로고
    • Topological rules for membrane protein assembly in eurkaryotic cells
    • G. Gafvelin, M. Sakaguchi, H. Andersson and G. Von Heijne, Topological rules for membrane protein assembly in eurkaryotic cells. J Biol Chem 272 (1997), 6119-6127.
    • (1997) J Biol Chem , vol.272 , pp. 6119-6127
    • Gafvelin, G.1    Sakaguchi, M.2    Andersson, H.3    Von Heijne, G.4
  • 75
    • 0027512232 scopus 로고
    • Evidence for an alternate model of human P-glycoprotein structure and biogenesis
    • W.R. Skach, M.C. Clayg and V.R. Lingappa, Evidence for an alternate model of human P-glycoprotein structure and biogenesis, J Biol Chem 268 (1993), 6903-6908.
    • (1993) J Biol Chem , vol.268 , pp. 6903-6908
    • Skach, W.R.1    Clayg, M.C.2    Lingappa, V.R.3
  • 76
    • 33751072463 scopus 로고    scopus 로고
    • Co- and posttranslational translocation mechanisms direct cystic fibrosis transmembrane conductance regulator N terminus transmembrane assembly
    • Y. Lu, X.M. Xiong, A. Helm, K. Kimani, A. Bragin and W.R. Skach, Co- and posttranslational translocation mechanisms direct cystic fibrosis transmembrane conductance regulator N terminus transmembrane assembly, J Biol Chem 270 (1998), 1742-1746.
    • (1998) J Biol Chem , vol.270 , pp. 1742-1746
    • Lu, Y.1    Xiong, X.M.2    Helm, A.3    Kimani, K.4    Bragin, A.5    Skach, W.R.6
  • 77
    • 0028938775 scopus 로고
    • Topological determinants of internal transmembrane segments in Pglycoprotein sequences
    • J.-T. Zhang, C.H. Lee, M. Duthie and V. Ling, Topological determinants of internal transmembrane segments in Pglycoprotein sequences, J Biol Chem 270 (1995), 1742-1746.
    • (1995) J Biol Chem , vol.270 , pp. 1742-1746
    • Zhang, J.-T.1    Lee, C.H.2    Duthie, M.3    Ling, V.4
  • 78
    • 0029988492 scopus 로고    scopus 로고
    • Membrane insertion, processin, and topology of cystic fibrosis transmembrane conductance regulator (CFTR) in microsomal membranes
    • M. Chen and J.-T. Zhang, Membrane insertion, processin, and topology of cystic fibrosis transmembrane conductance regulator (CFTR) in microsomal membranes, Mol Membr Biol 13 (1996), 33-40.
    • (1996) Mol Membr Biol , vol.13 , pp. 33-40
    • Chen, M.1    Zhang, J.-T.2
  • 79
    • 0032185234 scopus 로고    scopus 로고
    • Forced transmembrane orientation of hydrophilic polypeptide segments in multispanning membrane proteins
    • K. Ota, M. Von Sakaguchi, G. Heijne, N. Hamasaki and K. Mihara, Forced transmembrane orientation of hydrophilic polypeptide segments in multispanning membrane proteins, Mol Cell 2 (1998), 495-503.
    • (1998) Mol Cell , vol.2 , pp. 495-503
    • Ota, K.1    Von Sakaguchi, M.2    Heijne, G.3    Hamasaki, N.4    Mihara, K.5
  • 80
    • 0001207024 scopus 로고    scopus 로고
    • N-Tail translocation in a eurkaryotic polytopic membrane protein
    • M. Monne, G. Gafvelin, R. Nilsson and G. Von Heijne, N-Tail translocation in a eurkaryotic polytopic membrane protein, Eur J Biochem 263 (1999), 264-269.
    • (1999) Eur J Biochem , vol.263 , pp. 264-269
    • Monne, M.1    Gafvelin, G.2    Nilsson, R.3    Von Heijne, G.4
  • 81
    • 0034053280 scopus 로고    scopus 로고
    • Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane
    • I. Nilsson, S. Witt, H. Kiefer, I. Mingarro and G. Von Heijne, Distant downstream sequence determinants can control N-tail translocation during protein insertion into the endoplasmic reticulum membrane, J Biol Chem 275 (2000), 10716.
    • (2000) J Biol Chem , vol.275 , pp. 10716
    • Nilsson, I.1    Witt, S.2    Kiefer, H.3    Mingarro, I.4    Von Heijne, G.5
  • 82
    • 0342351613 scopus 로고
    • Predicting the orientation of eukaryotic membrane-spanning proteins
    • E. Hartmann, T.A. Rapoport and H.F. Lodish, Predicting the orientation of eukaryotic membrane-spanning proteins, Proc Natl Acad Sci USA 86 (1989), 5786-5790.
    • (1989) Proc Natl Acad Sci USA , vol.86 , pp. 5786-5790
    • Hartmann, E.1    Rapoport, T.A.2    Lodish, H.F.3
  • 83
    • 0025224551 scopus 로고
    • The structure and insertion of integral proteins in membranes
    • S.J. Singer, The structure and insertion of integral proteins in membranes, Annu Rev Cell Biol 6 (1990), 247-296.
    • (1990) Annu Rev Cell Biol , vol.6 , pp. 247-296
    • Singer, S.J.1
  • 85
    • 20944440679 scopus 로고    scopus 로고
    • The structure and functions of the presenilins
    • N.N. Dewji, The structure and functions of the presenilins, Cell Mol Life Sci 62 (2005), 1109-1119.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 1109-1119
    • Dewji, N.N.1
  • 88
    • 31944449213 scopus 로고    scopus 로고
    • An Early Specific Cell-Cell Interaction Occurs in the Production of Aβ Amyloid in Cell Cultures
    • N.N. Dewji, D. Mukhopadhyay and S.J. Singer, An Early Specific Cell-Cell Interaction Occurs in the Production of Aβ Amyloid in Cell Cultures, Proc Natl Acad Sci USA 103 1540-1545.
    • Proc Natl Acad Sci USA , vol.103 , pp. 1540-1545
    • Dewji, N.N.1    Mukhopadhyay, D.2    Singer, S.J.3
  • 89
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity
    • M.S. Wolfe, W. Xia, B. Ostaszewski, T. Diehl, W.T. Kimberly and D.J. Selkoe, Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity, Nature 398 (1999), 513-517.
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1    Xia, W.2    Ostaszewski, B.3    Diehl, T.4    Kimberly, W.T.5    Selkoe, D.J.6
  • 91
    • 0034621823 scopus 로고    scopus 로고
    • Alzheimer's disease: Closing in on gamma-secretase
    • B. De Strooper, Alzheimer's disease: Closing in on gamma-secretase, Nature 405 (2000), 627-628.
    • (2000) Nature , vol.405 , pp. 627-628
    • De Strooper, B.1
  • 98
    • 0023918551 scopus 로고
    • Mastoparan, a peptide toxin from wasp venom, mimics receptors by activating GTP-binding regulatory proteins (G proteins)
    • T. Higashijima, S. Uzu, T. Nakajima and E.M. Ross, Mastoparan, a peptide toxin from wasp venom, mimics receptors by activating GTP-binding regulatory proteins (G proteins), J Biol Chem 263 (1988), 6491-6494.
    • (1988) J Biol Chem , vol.263 , pp. 6491-6494
    • Higashijima, T.1    Uzu, S.2    Nakajima, T.3    Ross, E.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.