메뉴 건너뛰기




Volumn 494, Issue , 2008, Pages 71-86

Analysis of Aβ interactions using ProteinChip technology

Author keywords

Alzheimer's disease; Amyloid precursor protein; A ; ProteinChip technology; SELDI TOF MS

Indexed keywords


EID: 84934444430     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-59745-419-3_5     Document Type: Article
Times cited : (2)

References (28)
  • 1
    • 0023037536 scopus 로고
    • Isolation and partial characterization of neurofibrillary tangles and amyloid plaque core in Alzheimer's disease: Immunohistological studies
    • Gorevic, P.D., Goni, F., Pons-Estel, B., Alvarez, F., Peress, N.S. and Frangione, B. (1986) Isolation and partial characterization of neurofibrillary tangles and amyloid plaque core in Alzheimer's disease: immunohistological studies. J. Neuropathol. Exp. Neurol. 45, 647-664.
    • (1986) J. Neuropathol. Exp. Neurol , vol.45 , pp. 647-664
    • Gorevic, P.D.1    Goni, F.2    Pons-Estel, B.3    Alvarez, F.4    Peress, N.S.5    Frangione, B.6
  • 3
    • 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
  • 4
    • 0036548070 scopus 로고    scopus 로고
    • Gamma-Secretase, Notch, Abeta and Alzheimer's disease: Where do the presenilins fit in?
    • Sisodia, S.S. and St George-Hyslop, P.H. (2002) Gamma-Secretase, Notch, Abeta and Alzheimer's disease: where do the presenilins fit in? Nat. Rev. Neurosci. 3, 281-290.
    • (2002) Nat. Rev. Neurosci , vol.3 , pp. 281-290
    • Sisodia, S.S.1    St George-Hyslop, P.H.2
  • 5
    • 0025373508 scopus 로고
    • Evidence that beta-amyloid protein in Alzheimer's disease is not derived by normal processing
    • Sisodia, S.S., Koo, E.H., Beyreuther, K., Unterbeck, A. and Price, D.L. (1990) Evidence that beta-amyloid protein in Alzheimer's disease is not derived by normal processing. Science 248, 492-495.
    • (1990) Science , vol.248 , pp. 492-495
    • Sisodia, S.S.1    Koo, E.H.2    Beyreuther, K.3    Unterbeck, A.4    Price, D.L.5
  • 6
    • 0027535111 scopus 로고
    • beta-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms
    • Haass, C., Hung, A.Y., Schlossmacher, M.G., Teplow, D.B. and Selkoe, D.J. (1993) beta-Amyloid peptide and a 3-kDa fragment are derived by distinct cellular mechanisms. J. Biol. Chem. 268, 3021-3024.
    • (1993) J. Biol. Chem , vol.268 , pp. 3021-3024
    • Haass, C.1    Hung, A.Y.2    Schlossmacher, M.G.3    Teplow, D.B.4    Selkoe, D.J.5
  • 7
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett, J.T., Berger, E.P. and Lansbury, Jr. P.T. (1993) The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32, 4693-4697.
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury Jr., P.T.3
  • 8
    • 33645038471 scopus 로고    scopus 로고
    • A specific amyloid-beta protein assembly in the brain impairs memory
    • Lesne, S., Koh, M.T., Kotilinek, L., et al. (2006) A specific amyloid-beta protein assembly in the brain impairs memory. Nature 440, 352-357.
    • (2006) Nature , vol.440 , pp. 352-357
    • Lesne, S.1    Koh, M.T.2    Kotilinek, L.3
  • 9
    • 0030614627 scopus 로고    scopus 로고
    • Observation of metastable Abeta amyloid protofibrils by atomic force microscopy
    • Harper, J.D., Wong, S.S., Lieber, C.M. and Lansbury, P.T. (1997) Observation of metastable Abeta amyloid protofibrils by atomic force microscopy. Chem. Biol. 4, 119-125.
    • (1997) Chem. Biol , vol.4 , pp. 119-125
    • Harper, J.D.1    Wong, S.S.2    Lieber, C.M.3    Lansbury, P.T.4
  • 10
    • 11144353842 scopus 로고    scopus 로고
    • Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils
    • Relini, A., Torrassa, S., Rolandi, R., et al. (2004). Monitoring the process of HypF fibrillization and liposome permeabilization by protofibrils. J. Mol. Biol. 338, 943-957.
    • (2004) J. Mol. Biol , vol.338 , pp. 943-957
    • Relini, A.1    Torrassa, S.2    Rolandi, R.3
  • 11
    • 0033570337 scopus 로고    scopus 로고
    • Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons
    • Hartley, D.M., Walsh, D.M., Ye, C.P., et al. (1999) Protofibrillar intermediates of amyloid beta-protein induce acute electrophysiological changes and progressive neurotoxicity in cortical neurons. J. Neurosci. 19, 8876-8884.
    • (1999) J. Neurosci , vol.19 , pp. 8876-8884
    • Hartley, D.M.1    Walsh, D.M.2    Ye, C.P.3
  • 12
    • 0028233494 scopus 로고
    • Hydrogen peroxide mediates amyloid beta protein toxicity
    • Behl, C., Davis, J.B., Lesley, R. and Schubert, D. (1994) Hydrogen peroxide mediates amyloid beta protein toxicity. Cell 77, 817-827.
    • (1994) Cell , vol.77 , pp. 817-827
    • Behl, C.1    Davis, J.B.2    Lesley, R.3    Schubert, D.4
  • 13
    • 22144455300 scopus 로고    scopus 로고
    • Surface behavior and lipid interaction of Alzheimer beta-amyloid peptide 1-42: A membrane-disrupting peptide
    • Ambroggio, E.E., Kim, D.H., Separovic, F., et al. (2005) Surface behavior and lipid interaction of Alzheimer beta-amyloid peptide 1-42: a membrane-disrupting peptide. Biophys. J. 88, 2706-2713.
    • (2005) Biophys. J , vol.88 , pp. 2706-2713
    • Ambroggio, E.E.1    Kim, D.H.2    Separovic, F.3
  • 14
    • 0026570528 scopus 로고
    • beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson, M.P., Cheng, B., Davis, D., Bryant, K., Lieberburg, I. and Rydel, R.E. (1992) beta-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12, 376-389.
    • (1992) J. Neurosci , vol.12 , pp. 376-389
    • Mattson, M.P.1    Cheng, B.2    Davis, D.3    Bryant, K.4    Lieberburg, I.5    Rydel, R.E.6
  • 15
    • 0035827681 scopus 로고    scopus 로고
    • Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits
    • Curtain, C.C., Ali, F., Volitakis, I., et al. (2001) Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits. J. Biol. Chem. 276, 20466-20473.
    • (2001) J. Biol. Chem , vol.276 , pp. 20466-20473
    • Curtain, C.C.1    Ali, F.2    Volitakis, I.3
  • 16
    • 0346106076 scopus 로고    scopus 로고
    • Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence
    • Dong, J., Atwood, C.S., Anderson, V.E., et al. (2003) Metal binding and oxidation of amyloid-beta within isolated senile plaque cores: Raman microscopic evidence. Biochemistry 42, 2768-2773.
    • (2003) Biochemistry , vol.42 , pp. 2768-2773
    • Dong, J.1    Atwood, C.S.2    Anderson, V.E.3
  • 17
    • 0028981219 scopus 로고
    • Structure-activity analyses of beta-amyloid peptides: Contributions of the beta 25-35 region to aggregation and neurotoxicity
    • Pike, C.J., Walencewicz-Wasserman, A.J., Kosmoski, J., Cribbs, D.H., Glabe, C.G. and Cotman, C.W. (1995) Structure-activity analyses of beta-amyloid peptides: contributions of the beta 25-35 region to aggregation and neurotoxicity. J. Neurochem. 64, 253-265.
    • (1995) J. Neurochem , vol.64 , pp. 253-265
    • Pike, C.J.1    Walencewicz-Wasserman, A.J.2    Kosmoski, J.3    Cribbs, D.H.4    Glabe, C.G.5    Cotman, C.W.6
  • 18
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum
    • Arispe, N., Rojas, E. and Pollard, H.B. (1993) Alzheimer disease amyloid beta protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. Proc. Natl. Acad. Sci. USA 90, 567-571.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 19
    • 0031927628 scopus 로고    scopus 로고
    • Par-4 is a mediator of neuronal degeneration associated with the pathogenesis of Alzheimer disease
    • Guo, Q., Fu, W., Xie, J., et al. (1998) Par-4 is a mediator of neuronal degeneration associated with the pathogenesis of Alzheimer disease. Nat. Med. 4, 957-962.
    • (1998) Nat. Med , vol.4 , pp. 957-962
    • Guo, Q.1    Fu, W.2    Xie, J.3
  • 20
    • 1642524231 scopus 로고    scopus 로고
    • Detection of tumor markers with ProteinChip technology
    • Wiesner, A. (2004) Detection of tumor markers with ProteinChip technology. Curr. Pharm. Biotechnol. 5, 45-67.
    • (2004) Curr. Pharm. Biotechnol , vol.5 , pp. 45-67
    • Wiesner, A.1
  • 21
    • 0033626226 scopus 로고    scopus 로고
    • The use of seldi proteinchip arrays to monitor production of Alzheimer's betaamyloid in transfected cells
    • Austen, B.M., Frears, E.R. and Davies, H. (2000) The use of seldi proteinchip arrays to monitor production of Alzheimer's betaamyloid in transfected cells. J. Pept. Sci. 6, 459-469.
    • (2000) J. Pept. Sci , vol.6 , pp. 459-469
    • Austen, B.M.1    Frears, E.R.2    Davies, H.3
  • 23
    • 9244240337 scopus 로고    scopus 로고
    • Cerebrospinal fluid profile of amyloid beta peptides in patients with Alzheimer's disease determined by protein biochip technology
    • Maddalena, A.S., Papassotiropoulos, A., Gonzalez-Agosti, C., et al. (2004) Cerebrospinal fluid profile of amyloid beta peptides in patients with Alzheimer's disease determined by protein biochip technology. Neurodegener. Dis. 1, 231-235.
    • (2004) Neurodegener. Dis , vol.1 , pp. 231-235
    • Maddalena, A.S.1    Papassotiropoulos, A.2    Gonzalez-Agosti, C.3
  • 24
    • 0035860781 scopus 로고    scopus 로고
    • Amyloid beta-protein oligomerization: Prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins
    • Bitan, G., Lomakin, A. and Teplow, D. B. (2001) Amyloid beta-protein oligomerization: prenucleation interactions revealed by photo-induced cross-linking of unmodified proteins. J. Biol. Chem. 276, 35176-35184.
    • (2001) J. Biol. Chem , vol.276 , pp. 35176-35184
    • Bitan, G.1    Lomakin, A.2    Teplow, D.B.3
  • 25
    • 0028170719 scopus 로고
    • Soluble amyloid β-protein in the cerebrospinal fluid from patients with Alzheimer's disease, vascular dementia and controls
    • Pirttilä, T., Kim, K.S., Mehta, P.D., Frey, H. and Wisniewski, H.M. (1994) Soluble amyloid β-protein in the cerebrospinal fluid from patients with Alzheimer's disease, vascular dementia and controls. J. Neurol. Sci. 127, 90-95.
    • (1994) J. Neurol. Sci , vol.127 , pp. 90-95
    • Pirttilä, T.1    Kim, K.S.2    Mehta, P.D.3    Frey, H.4    Wisniewski, H.M.5
  • 26
    • 0029661424 scopus 로고    scopus 로고
    • Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay
    • Ida, N., Hartmann, T., Pantel, J., et al. (1996) Analysis of heterogeneous A4 peptides in human cerebrospinal fluid and blood by a newly developed sensitive Western blot assay. J. Biol. Chem. 271, 22908-22914.
    • (1996) J. Biol. Chem , vol.271 , pp. 22908-22914
    • Ida, N.1    Hartmann, T.2    Pantel, J.3
  • 27
    • 0034168240 scopus 로고    scopus 로고
    • Quantification of Alzheimer amyloid beta peptides ending at residues 40 and 42 by novel ELISA systems
    • Jensen, M., Hartmann, T., Engvall, B., et al. (2000) Quantification of Alzheimer amyloid beta peptides ending at residues 40 and 42 by novel ELISA systems. Mol. Med. 6, 291-302.
    • (2000) Mol. Med , vol.6 , pp. 291-302
    • Jensen, M.1    Hartmann, T.2    Engvall, B.3
  • 28
    • 14444267540 scopus 로고    scopus 로고
    • Characterization of new polyclonal antibodies specific for 40 and 42 amino acid-long amyloid beta peptides: Their use to examine the cell biology of presenilins and the immunohistochemistry of sporadic Alzheimer's disease and cerebral amyloid angiopathy cases
    • Barelli, H., Lebeau, A., Vizzavona, J., et al. (1997) Characterization of new polyclonal antibodies specific for 40 and 42 amino acid-long amyloid beta peptides: their use to examine the cell biology of presenilins and the immunohistochemistry of sporadic Alzheimer's disease and cerebral amyloid angiopathy cases. Mol. Med. 3, 695-707.
    • (1997) Mol. Med , vol.3 , pp. 695-707
    • Barelli, H.1    Lebeau, A.2    Vizzavona, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.