메뉴 건너뛰기




Volumn 357, Issue 2, 2006, Pages 493-508

Solution conformation and heparin-induced dimerization of the full-length extracellular domain of the human amyloid precursor protein

Author keywords

Analytical ultracentrifugation; Modeling; Signal transduction; Small angle X ray scattering; Structural domains

Indexed keywords

AMYLOID PRECURSOR PROTEIN; HEPARIN;

EID: 33344458873     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2005.12.053     Document Type: Article
Times cited : (59)

References (63)
  • 2
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid-A4 protein resembles a cell surface receptor
    • J. Kang, H.G. Lemaire, A. Unterbeck, J.M. Salbaum, C.L. Masters, and K.H. Grzeschik The precursor of Alzheimer's disease amyloid-A4 protein resembles a cell surface receptor Nature 325 1987 733 736
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.G.2    Unterbeck, A.3    Salbaum, J.M.4    Masters, C.L.5    Grzeschik, K.H.6
  • 3
    • 0026088977 scopus 로고
    • Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease
    • A. Goate, M.C. Chartier-Harlin, M. Mullan, J. Brown, F. Crawford, and L. Fidani Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's disease Nature 349 1991 704 706
    • (1991) Nature , vol.349 , pp. 704-706
    • Goate, A.1    Chartier-Harlin, M.C.2    Mullan, M.3    Brown, J.4    Crawford, F.5    Fidani, L.6
  • 4
  • 5
    • 85047690140 scopus 로고    scopus 로고
    • A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model
    • R. Postina, A. Schroeder, I. Dewachter, J. Bohl, U. Schmitt, and E. Kojro A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model J. Clin. Invest. 113 2004 1456 1464
    • (2004) J. Clin. Invest. , vol.113 , pp. 1456-1464
    • Postina, R.1    Schroeder, A.2    Dewachter, I.3    Bohl, J.4    Schmitt, U.5    Kojro, E.6
  • 6
    • 0037038816 scopus 로고    scopus 로고
    • Beta-secretase (BACE) as a drug target for Alzheimer's disease
    • R. Vassar Beta-secretase (BACE) as a drug target for Alzheimer's disease Advan. Drug Deliv. Rev. 54 2002 1589 1602
    • (2002) Advan. Drug Deliv. Rev. , vol.54 , pp. 1589-1602
    • Vassar, R.1
  • 7
    • 0034488295 scopus 로고    scopus 로고
    • Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor
    • B. Passer, L. Pellegrini, C. Russo, R.M. Siegel, M.J. Lenardo, and G. Schettini Generation of an apoptotic intracellular peptide by gamma-secretase cleavage of Alzheimer's amyloid beta protein precursor J. Alzheimers Dis. 2 2000 289 301
    • (2000) J. Alzheimers Dis. , vol.2 , pp. 289-301
    • Passer, B.1    Pellegrini, L.2    Russo, C.3    Siegel, R.M.4    Lenardo, M.J.5    Schettini, G.6
  • 9
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60
    • X. Cao, and T.C. Südhof A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60 Science 293 2001 115 120
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Südhof, T.C.2
  • 10
    • 0042634362 scopus 로고    scopus 로고
    • Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory
    • P.R. Turner, K. O'Connor, W.P. Tate, and W.C. Abraham Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory Prog. Neurobiol. 70 2003 1 32
    • (2003) Prog. Neurobiol. , vol.70 , pp. 1-32
    • Turner, P.R.1    O'Connor, K.2    Tate, W.P.3    Abraham, W.C.4
  • 12
    • 0038722283 scopus 로고    scopus 로고
    • The amyloid precursor protein and its regulatory protein, FE65, in growth cones and synapses in vitro and in vivo
    • S.L. Sabo, A.F. Ikin, J.D. Buxbaum, and P. Greengard The amyloid precursor protein and its regulatory protein, FE65, in growth cones and synapses in vitro and in vivo J. Neurosci. 23 2003 5407 5415
    • (2003) J. Neurosci. , vol.23 , pp. 5407-5415
    • Sabo, S.L.1    Ikin, A.F.2    Buxbaum, J.D.3    Greengard, P.4
  • 13
    • 0030574061 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid precursor protein on the surface of cortical neurons in primary culture co-localizes with adhesion patch components
    • E. Storey, K. Beyreuther, and C.L. Masters Alzheimer's disease amyloid precursor protein on the surface of cortical neurons in primary culture co-localizes with adhesion patch components Brain Res. 735 1996 217 231
    • (1996) Brain Res. , vol.735 , pp. 217-231
    • Storey, E.1    Beyreuther, K.2    Masters, C.L.3
  • 14
    • 0035829720 scopus 로고    scopus 로고
    • Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila
    • S. Gunawardena, and L.S. Goldstein Disruption of axonal transport and neuronal viability by amyloid precursor protein mutations in Drosophila Neuron 32 2001 389 401
    • (2001) Neuron , vol.32 , pp. 389-401
    • Gunawardena, S.1    Goldstein, L.S.2
  • 15
    • 0029935396 scopus 로고    scopus 로고
    • The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I)
    • G. Multhaup, A. Schlicksupp, L. Hesse, D. Beher, T. Ruppert, C.L. Masters, and K. Beyreuther The amyloid precursor protein of Alzheimer's disease in the reduction of copper(II) to copper(I) Science 271 1996 1406 1409
    • (1996) Science , vol.271 , pp. 1406-1409
    • Multhaup, G.1    Schlicksupp, A.2    Hesse, L.3    Beher, D.4    Ruppert, T.5    Masters, C.L.6    Beyreuther, K.7
  • 16
    • 0027478347 scopus 로고
    • Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the beta-amyloid precursor protein
    • M.P. Mattson, B. Cheng, A.R. Culwell, F.S. Esch, I. Lieberburg, and R.E. Rydel Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the beta-amyloid precursor protein Neuron 10 1993 243 254
    • (1993) Neuron , vol.10 , pp. 243-254
    • Mattson, M.P.1    Cheng, B.2    Culwell, A.R.3    Esch, F.S.4    Lieberburg, I.5    Rydel, R.E.6
  • 17
  • 18
    • 2542519087 scopus 로고    scopus 로고
    • Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone
    • I. Caille, B. Allinquant, E. Dupont, C. Bouillot, A. Langer, U. Muller, and A. Prochiantz Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone Development 131 2004 2173 2181
    • (2004) Development , vol.131 , pp. 2173-2181
    • Caille, I.1    Allinquant, B.2    Dupont, E.3    Bouillot, C.4    Langer, A.5    Muller, U.6    Prochiantz, A.7
  • 19
    • 0032539666 scopus 로고    scopus 로고
    • From differentiation to proliferation: The secretory amyloid precursor protein as a local mediator of growth in thyroid epithelial cells
    • C.U. Pietrzik, J. Hoffmann, K. Stober, C.Y. Chen, C. Bauer, and D.A.C. Otero From differentiation to proliferation: the secretory amyloid precursor protein as a local mediator of growth in thyroid epithelial cells Proc. Natl Acad. Sci. USA 95 1998 1770 1775
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1770-1775
    • Pietrzik, C.U.1    Hoffmann, J.2    Stober, K.3    Chen, C.Y.4    Bauer, C.5    Otero, D.A.C.6
  • 20
    • 0025008384 scopus 로고
    • X-ray crystal structure of the protease inhibitor domain of Alzheimer's amyloid beta-protein precursor
    • T.R. Hynes, M. Randal, L.A. Kennedy, C. Eigenbrot, and A.A. Kossiakoff X-ray crystal structure of the protease inhibitor domain of Alzheimer's amyloid beta-protein precursor Biochemistry 29 1990 10018 10022
    • (1990) Biochemistry , vol.29 , pp. 10018-10022
    • Hynes, T.R.1    Randal, M.2    Kennedy, L.A.3    Eigenbrot, C.4    Kossiakoff, A.A.5
  • 21
    • 0030740213 scopus 로고    scopus 로고
    • Solution conformations of a peptide containing the cytoplasmic domain sequence of the beta amyloid precursor protein
    • C.D. Kroenke, D. Ziemnicka-Kotula, J. Xu, L. Kotula, and A.G. Palmer 3rd Solution conformations of a peptide containing the cytoplasmic domain sequence of the beta amyloid precursor protein Biochemistry 36 1997 8145 8152
    • (1997) Biochemistry , vol.36 , pp. 8145-8152
    • Kroenke, C.D.1    Ziemnicka-Kotula, D.2    Xu, J.3    Kotula, L.4    Palmer III, A.G.5
  • 22
    • 0032945805 scopus 로고    scopus 로고
    • Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein
    • J. Rossjohn, R. Cappai, S.C. Feil, A. Henry, W.J. McKinstry, and D. Galatis Crystal structure of the N-terminal, growth factor-like domain of Alzheimer amyloid precursor protein Nature Struct. Biol. 6 1999 327 331
    • (1999) Nature Struct. Biol. , vol.6 , pp. 327-331
    • Rossjohn, J.1    Cappai, R.2    Feil, S.C.3    Henry, A.4    McKinstry, W.J.5    Galatis, D.6
  • 23
    • 0037931743 scopus 로고    scopus 로고
    • Structure of the Alzheimer's disease amyloid precursor protein copper binding domain - A regulator of neuronal copper homeostasis
    • K.J. Barnham, W.J. McKinstry, G. Multhaup, D. Galatis, C.J. Morton, and C.C. Curtain Structure of the Alzheimer's disease amyloid precursor protein copper binding domain - a regulator of neuronal copper homeostasis J. Biol. Chem. 278 2003 17401 17407
    • (2003) J. Biol. Chem. , vol.278 , pp. 17401-17407
    • Barnham, K.J.1    McKinstry, W.J.2    Multhaup, G.3    Galatis, D.4    Morton, C.J.5    Curtain, C.C.6
  • 24
    • 3342915630 scopus 로고    scopus 로고
    • Three-dimensional structure of an independently folded extracellular domain of human amyloid-beta precursor protein
    • I. Dulubova, A. Ho, I. Huryeva, T.C. Südhof, and J. Rizo Three-dimensional structure of an independently folded extracellular domain of human amyloid-beta precursor protein Biochemistry 43 2004 9583 9588
    • (2004) Biochemistry , vol.43 , pp. 9583-9588
    • Dulubova, I.1    Ho, A.2    Huryeva, I.3    Südhof, T.C.4    Rizo, J.5
  • 25
    • 4143105782 scopus 로고    scopus 로고
    • The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain
    • Y. Wang, and Y. Ha The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain Mol. Cell. 15 2004 343 353
    • (2004) Mol. Cell. , vol.15 , pp. 343-353
    • Wang, Y.1    Ha, Y.2
  • 26
    • 0036932412 scopus 로고    scopus 로고
    • Solution studies and structural model of the extracellular domain of the human amyloid precursor protein
    • M. Gralle, M.M. Botelho, C.L.P. de Oliveira, I. Torriani, and S.T. Ferreira Solution studies and structural model of the extracellular domain of the human amyloid precursor protein Biophys. J. 83 2002 3513 3524
    • (2002) Biophys. J. , vol.83 , pp. 3513-3524
    • Gralle, M.1    Botelho, M.M.2    De Oliveira, C.L.P.3    Torriani, I.4    Ferreira, S.T.5
  • 27
    • 0141668941 scopus 로고    scopus 로고
    • Folding and stability of the extracellular domain of the human amyloid precursor protein
    • M.G. Botelho, M. Gralle, C.L.P. Oliveira, I. Torriani, and S.T. Ferreira Folding and stability of the extracellular domain of the human amyloid precursor protein J. Biol. Chem. 278 2003 34259 34267
    • (2003) J. Biol. Chem. , vol.278 , pp. 34259-34267
    • Botelho, M.G.1    Gralle, M.2    Oliveira, C.L.P.3    Torriani, I.4    Ferreira, S.T.5
  • 28
    • 0030671397 scopus 로고    scopus 로고
    • The mechanism by which heparin promotes the inhibition of coagulation factor XIa by protease nexin-2
    • Y. Zhang, J.M. Scandura, W.E. Van Nostrand, and P.N. Walsh The mechanism by which heparin promotes the inhibition of coagulation factor XIa by protease nexin-2 J. Biol. Chem. 272 1997 26139 26144
    • (1997) J. Biol. Chem. , vol.272 , pp. 26139-26144
    • Zhang, Y.1    Scandura, J.M.2    Van Nostrand, W.E.3    Walsh, P.N.4
  • 29
    • 0034496657 scopus 로고    scopus 로고
    • Advanced solution scattering data analysis methods and their applications
    • D.I. Svergun Advanced solution scattering data analysis methods and their applications J. Appl. Crystallog. 33 2000 530 534
    • (2000) J. Appl. Crystallog. , vol.33 , pp. 530-534
    • Svergun, D.I.1
  • 30
    • 0035010533 scopus 로고    scopus 로고
    • Determination of domain structure of proteins from X-ray solution scattering
    • D.I. Svergun, M.V. Petoukhov, and M.H.J. Koch Determination of domain structure of proteins from X-ray solution scattering Biophys. J. 80 2001 2946 2953
    • (2001) Biophys. J. , vol.80 , pp. 2946-2953
    • Svergun, D.I.1    Petoukhov, M.V.2    Koch, M.H.J.3
  • 31
    • 0037701771 scopus 로고    scopus 로고
    • New methods for domain structure determination of proteins from solution scattering data
    • M.V. Petoukhov, and D.I. Svergun New methods for domain structure determination of proteins from solution scattering data J. Appl. Crystallog. 36 2003 540 544
    • (2003) J. Appl. Crystallog. , vol.36 , pp. 540-544
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 32
    • 0037701585 scopus 로고    scopus 로고
    • Uniqueness of ab initio shape determination in small-angle scattering
    • V.V. Volkov, and D.I. Svergun Uniqueness of ab initio shape determination in small-angle scattering J. Appl. Crystallog. 36 2003 860 864
    • (2003) J. Appl. Crystallog. , vol.36 , pp. 860-864
    • Volkov, V.V.1    Svergun, D.I.2
  • 33
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • J.G. de la Torre, M.L. Huertas, and B. Carrasco Calculation of hydrodynamic properties of globular proteins from their atomic-level structure Biophys. J. 78 2000 719 730
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • De La Torre, J.G.1    Huertas, M.L.2    Carrasco, B.3
  • 34
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • R. Ehehalt, P. Keller, C. Haass, C. Thiele, and K. Simons Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts J. Cell Biol. 160 2003 113 123
    • (2003) J. Cell Biol. , vol.160 , pp. 113-123
    • Ehehalt, R.1    Keller, P.2    Haass, C.3    Thiele, C.4    Simons, K.5
  • 35
    • 0027333449 scopus 로고
    • Apl-1, a Caenorhabditis elegans gene encoding a protein related to the human beta-amyloid protein precursor
    • I. Daigle, and C. Li apl-1, a Caenorhabditis elegans gene encoding a protein related to the human beta-amyloid protein precursor Proc. Natl Acad. Sci. USA 90 1993 12045 12049
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 12045-12049
    • Daigle, I.1    Li, C.2
  • 36
    • 0035124442 scopus 로고    scopus 로고
    • Automated matching of high- and low-resolution structural models
    • M.B. Kozin, and D.I. Svergun Automated matching of high- and low-resolution structural models J. Appl. Crystallog. 34 2001 33 41
    • (2001) J. Appl. Crystallog. , vol.34 , pp. 33-41
    • Kozin, M.B.1    Svergun, D.I.2
  • 38
    • 0034849689 scopus 로고    scopus 로고
    • MASSHA - A graphics system for rigid-body modelling of macromolecular complexes against solution scattering data
    • P.V. Konarev, M.V. Petoukhov, and D.I. Svergun MASSHA - a graphics system for rigid-body modelling of macromolecular complexes against solution scattering data J. Appl. Crystallog. 34 2001 527 532
    • (2001) J. Appl. Crystallog. , vol.34 , pp. 527-532
    • Konarev, P.V.1    Petoukhov, M.V.2    Svergun, D.I.3
  • 39
    • 10544230644 scopus 로고    scopus 로고
    • Secreted glypican binds to the amyloid precursor protein of Alzheimer's disease (APP) and inhibits APP-induced neurite outgrowth
    • T.G. Williamson, S.S. Mok, A. Henry, R. Cappai, A.D. Lander, and V. Nurcombe Secreted glypican binds to the amyloid precursor protein of Alzheimer's disease (APP) and inhibits APP-induced neurite outgrowth J. Biol. Chem. 271 1996 31215 31221
    • (1996) J. Biol. Chem. , vol.271 , pp. 31215-31221
    • Williamson, T.G.1    Mok, S.S.2    Henry, A.3    Cappai, R.4    Lander, A.D.5    Nurcombe, V.6
  • 40
    • 0031026779 scopus 로고    scopus 로고
    • Identification of heparin-binding domains in the amyloid precursor protein of Alzheimer's disease by deletion mutagenesis and peptide mapping
    • H.J. Clarris, R. Cappai, D. Heffernan, K. Beyreuther, C.L. Masters, and D.H. Small Identification of heparin-binding domains in the amyloid precursor protein of Alzheimer's disease by deletion mutagenesis and peptide mapping J. Neurochem. 68 1997 1164 1172
    • (1997) J. Neurochem. , vol.68 , pp. 1164-1172
    • Clarris, H.J.1    Cappai, R.2    Heffernan, D.3    Beyreuther, K.4    Masters, C.L.5    Small, D.H.6
  • 41
    • 18844473445 scopus 로고    scopus 로고
    • Expression and analysis of heparin-binding regions of the amyloid precursor protein of Alzheimer's disease
    • S.S. Mok, G. Sberna, D. Heffernan, R. Cappai, D. Galatis, and H.J. Clarris Expression and analysis of heparin-binding regions of the amyloid precursor protein of Alzheimer's disease FEBS Letters 415 1997 303 307
    • (1997) FEBS Letters , vol.415 , pp. 303-307
    • Mok, S.S.1    Sberna, G.2    Heffernan, D.3    Cappai, R.4    Galatis, D.5    Clarris, H.J.6
  • 42
    • 0141483463 scopus 로고    scopus 로고
    • SAPP as a regulator of dendrite motility and melanin release in epidermal melanocytes and melanoma cells
    • T. Quast, S. Wehner, G. Kirfel, K. Jaeger, M. De Luca, and V. Herzog sAPP as a regulator of dendrite motility and melanin release in epidermal melanocytes and melanoma cells FASEB J. 17 2003 1739 1741
    • (2003) FASEB J. , vol.17 , pp. 1739-1741
    • Quast, T.1    Wehner, S.2    Kirfel, G.3    Jaeger, K.4    De Luca, M.5    Herzog, V.6
  • 43
    • 0032514633 scopus 로고    scopus 로고
    • Memory-enhancing effects of secreted forms of the beta-amyloid precursor protein in normal and amnestic mice
    • H. Meziane, J.C. Dodart, C. Mathis, S. Little, J. Clemens, S.M. Paul, and A. Ungerer Memory-enhancing effects of secreted forms of the beta-amyloid precursor protein in normal and amnestic mice Proc. Natl Acad. Sci. USA 95 1998 12683 12688
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12683-12688
    • Meziane, H.1    Dodart, J.C.2    Mathis, C.3    Little, S.4    Clemens, J.5    Paul, S.M.6    Ungerer, A.7
  • 44
    • 0028971033 scopus 로고
    • Regulated secretion of beta-amyloid precursor protein in rat brain
    • S.A. Farber, R.M. Nitsch, J.G. Schulz, and R.J. Wurtman Regulated secretion of beta-amyloid precursor protein in rat brain J. Neurosci. 15 1995 7442 7451
    • (1995) J. Neurosci. , vol.15 , pp. 7442-7451
    • Farber, S.A.1    Nitsch, R.M.2    Schulz, J.G.3    Wurtman, R.J.4
  • 45
    • 0036759157 scopus 로고    scopus 로고
    • Lack of neurodegeneration in transgenic mice overexpressing mutant amyloid precursor protein is associated with increased levels of transthyretin and the activation of cell survival pathways
    • T.D. Stein, and J.A. Johnson Lack of neurodegeneration in transgenic mice overexpressing mutant amyloid precursor protein is associated with increased levels of transthyretin and the activation of cell survival pathways J. Neurosci. 22 2002 7380 7388
    • (2002) J. Neurosci. , vol.22 , pp. 7380-7388
    • Stein, T.D.1    Johnson, J.A.2
  • 46
    • 0032992044 scopus 로고    scopus 로고
    • Binding and selective detection of the secretory N-terminal domain of the Alzheimer amyloid precursor protein on cell surfaces
    • J. Hoffmann, C.U. Pietrzik, M.P. Kummer, C. Twiesselmann, C. Bauer, and V. Herzog Binding and selective detection of the secretory N-terminal domain of the Alzheimer amyloid precursor protein on cell surfaces J. Histochem. Cytochem. 47 1999 373 382
    • (1999) J. Histochem. Cytochem. , vol.47 , pp. 373-382
    • Hoffmann, J.1    Pietrzik, C.U.2    Kummer, M.P.3    Twiesselmann, C.4    Bauer, C.5    Herzog, V.6
  • 48
    • 0035096910 scopus 로고    scopus 로고
    • Fibulin-1 binds the amino-terminal head of beta-amyloid precursor protein and modulates its physiological function
    • I. Ohsawa, C. Takamura, and S. Kohsaka Fibulin-1 binds the amino-terminal head of beta-amyloid precursor protein and modulates its physiological function J. Neurochem. 76 2001 1411 1420
    • (2001) J. Neurochem. , vol.76 , pp. 1411-1420
    • Ohsawa, I.1    Takamura, C.2    Kohsaka, S.3
  • 49
    • 1442306058 scopus 로고    scopus 로고
    • Binding of F-spondin to amyloid-beta precursor protein: A candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage
    • A. Ho, and T.C. Südhof Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage Proc. Natl Acad. Sci. USA 101 2004 2548 2553
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 2548-2553
    • Ho, A.1    Südhof, T.C.2
  • 50
    • 0035823495 scopus 로고    scopus 로고
    • Homodimerization of amyloid precursor protein and its implication in the amyloidogenic pathway of Alzheimer's disease
    • S. Scheuermann, B. Hambsch, L. Hesse, J. Stumm, C. Schmidt, and D. Beher Homodimerization of amyloid precursor protein and its implication in the amyloidogenic pathway of Alzheimer's disease J. Biol. Chem. 276 2001 33923 33929
    • (2001) J. Biol. Chem. , vol.276 , pp. 33923-33929
    • Scheuermann, S.1    Hambsch, B.2    Hesse, L.3    Stumm, J.4    Schmidt, C.5    Beher, D.6
  • 51
    • 0042887148 scopus 로고    scopus 로고
    • Demonstration by FRET of BACE interaction with the amyloid precursor protein at the cell surface and in early endosomes
    • A. Kinoshita, H. Fukumoto, T. Shah, C.M. Whelan, M.C. Irizarry, and B.T. Hyman Demonstration by FRET of BACE interaction with the amyloid precursor protein at the cell surface and in early endosomes J. Cell Sci. 116 2003 3339 3346
    • (2003) J. Cell Sci. , vol.116 , pp. 3339-3346
    • Kinoshita, A.1    Fukumoto, H.2    Shah, T.3    Whelan, C.M.4    Irizarry, M.C.5    Hyman, B.T.6
  • 52
    • 0035968192 scopus 로고    scopus 로고
    • Probing fibroblast growth factor dimerization and role of heparin-like glycosaminoglycans in modulating dimerization and signaling
    • C.P. Kwan, G. Venkatamaran, Z. Shriver, R. Raman, D. Liu, and Y. Qi Probing fibroblast growth factor dimerization and role of heparin-like glycosaminoglycans in modulating dimerization and signaling J. Biol. Chem. 276 2001 23421 23429
    • (2001) J. Biol. Chem. , vol.276 , pp. 23421-23429
    • Kwan, C.P.1    Venkatamaran, G.2    Shriver, Z.3    Raman, R.4    Liu, D.5    Qi, Y.6
  • 53
    • 0042934160 scopus 로고    scopus 로고
    • The cytoplasmic domain of Alzheimer's amyloid-beta protein precursor causes sustained apoptosis signal-regulating kinase 1/c-Jun NH2-terminal kinase-mediated neurotoxic signal via dimerization
    • Y. Hashimoto, T. Niikura, T. Chiba, E. Tsukamoto, H. Kadowaki, and H. Nishitoh The cytoplasmic domain of Alzheimer's amyloid-beta protein precursor causes sustained apoptosis signal-regulating kinase 1/c-Jun NH2-terminal kinase-mediated neurotoxic signal via dimerization J. Pharm. Expt. Ther. 306 2003 889 902
    • (2003) J. Pharm. Expt. Ther. , vol.306 , pp. 889-902
    • Hashimoto, Y.1    Niikura, T.2    Chiba, T.3    Tsukamoto, E.4    Kadowaki, H.5    Nishitoh, H.6
  • 54
    • 0141737107 scopus 로고    scopus 로고
    • Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering
    • J.A. Marquez, C.I.E. Smith, M.V. Petoukhov, P. Lo Surdo, P.T. Mattsson, and M. Knekt Conformation of full-length Bruton tyrosine kinase (Btk) from synchrotron X-ray solution scattering EMBO J. 22 2003 4616 4624
    • (2003) EMBO J. , vol.22 , pp. 4616-4624
    • Marquez, J.A.1    Smith, C.I.E.2    Petoukhov, M.V.3    Lo Surdo, P.4    Mattsson, P.T.5    Knekt, M.6
  • 57
    • 0026244044 scopus 로고
    • GNOM - A program package for small-angle scattering data processing
    • A.V. Semenyuk, and D.I. Svergun GNOM - a program package for small-angle scattering data processing J. Appl. Crystallog. 24 1991 537 540
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 537-540
    • Semenyuk, A.V.1    Svergun, D.I.2
  • 58
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • R. Koradi, M. Billeter, and K. Wuthrich MOLMOL: a program for display and analysis of macromolecular structures J. Mol. Graph. 14 1996 51 55
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wuthrich, K.3
  • 59
    • 0030900930 scopus 로고    scopus 로고
    • Native and multimeric vitronectin exhibit similar affinity for heparin - Differences in heparin binding properties induced upon denaturation are due to self-association into a multivalent form
    • P. Zhuang, A.I. Chen, and C.B. Peterson Native and multimeric vitronectin exhibit similar affinity for heparin - differences in heparin binding properties induced upon denaturation are due to self-association into a multivalent form J. Biol. Chem. 272 1997 6858 6867
    • (1997) J. Biol. Chem. , vol.272 , pp. 6858-6867
    • Zhuang, P.1    Chen, A.I.2    Peterson, C.B.3
  • 60
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • P. Schuck Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling Biophys. J. 78 2000 1606 1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 61
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • J. Lebowitz, M.S. Lewis, and P. Schuck Modern analytical ultracentrifugation in protein science: a tutorial review Protein Sci. 11 2002 2067 2079
    • (2002) Protein Sci. , vol.11 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 62
    • 23244455562 scopus 로고    scopus 로고
    • Global rigid body modelling of macromolecular complexes against small-angle scattering data
    • M.V. Petoukhov, and D.I. Svergun Global rigid body modelling of macromolecular complexes against small-angle scattering data Biophys. J. 89 2005 1237 1250
    • (2005) Biophys. J. , vol.89 , pp. 1237-1250
    • Petoukhov, M.V.1    Svergun, D.I.2
  • 63
    • 0029185933 scopus 로고
    • CRYSOL - A program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates
    • D. Svergun, C. Barberato, and M.H.J. Koch CRYSOL - a program to evaluate X-ray solution scattering of biological macromolecules from atomic coordinates J. Appl. Crystallog. 28 1995 768 773
    • (1995) J. Appl. Crystallog. , vol.28 , pp. 768-773
    • Svergun, D.1    Barberato, C.2    Koch, M.H.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.