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Volumn 11, Issue 5, 2013, Pages 491-498

Pyroglutamate-modified amyloid beta peptides: Emerging targets for alzheimer's disease immunotherapy

Author keywords

Alzheimer's disease; Amyloid beta; Glutaminyl cyclase; Immunotherapy; N terminal truncated amyloid beta; Pyroglutamate modified amyloid beta

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN N11; AMYLOID BETA PROTEIN N3; BAPINEUZUMAB; ENZYME INHIBITOR; GLUTAMINYL CYCLASE INHIBITOR; PRESENILIN 1; PYROGLUTAMIC ACID; SOLANEZUMAB; UNCLASSIFIED DRUG;

EID: 84884266807     PISSN: 1570159X     EISSN: 18756190     Source Type: Journal    
DOI: 10.2174/1570159X11311050004     Document Type: Article
Times cited : (56)

References (96)
  • 2
    • 5344277556 scopus 로고    scopus 로고
    • Deciphering the molecular basis of memory failure in Alzheimer's diseas
    • Walsh, D. M.; Selkoe, D. J. Deciphering the molecular basis of memory failure in Alzheimer's diseas. Neuron, 2004, 44(1), 181-193.
    • (2004) Neuron , vol.44 , Issue.1 , pp. 181-193
    • Walsh, D.M.1    Selkoe, D.J.2
  • 3
    • 33847662852 scopus 로고    scopus 로고
    • Soluble protein oligomers in neurodegeneration: Lessons from the Alzheimer's amyloid beta-peptide
    • Haass, C; Selkoe, D. J. Soluble protein oligomers in neurodegeneration: lessons from the Alzheimer's amyloid beta-peptide. Nat. Rev. Mol. Cell. Biol., 2007, 8(2), 101-112.
    • (2007) Nat. Rev. Mol. Cell. Biol , vol.8 , Issue.2 , pp. 101-112
    • Haass, C.1    Selkoe, D.J.2
  • 4
    • 34250819839 scopus 로고    scopus 로고
    • Intracellular amyloid-p in Alzheimer's disease
    • LaFerla, F.; Green, K. N.; Oddo, S. Intracellular amyloid-p in Alzheimer's disease. Nat. Rev. Neurosci., 2007, 8, 499-509.
    • (2007) Nat. Rev. Neurosci , vol.8 , pp. 499-509
    • Laferla, F.1    Green, K.N.2    Oddo, S.3
  • 5
    • 77953019895 scopus 로고    scopus 로고
    • Intraneuronal beta-amyloid accumulation and synapse pathology in Alzheimer's disease
    • Gouras, G. K.; Tampellini, D.; Takahashi, R. H.; Capetillo-Zarate, E. Intraneuronal beta-amyloid accumulation and synapse pathology in Alzheimer's disease. Acta Neuropathol, 2010, 119(5), 523-541.
    • (2010) Acta Neuropathol , vol.119 , Issue.5 , pp. 523-541
    • Gouras, G.K.1    Tampellini, D.2    Takahashi, R.H.3    Capetillo-Zarate, E.4
  • 7
    • 82355192272 scopus 로고    scopus 로고
    • The Ap oligomer hypothesis for synapse failure and memory loss in Alzheimer's disease
    • Ferreira, S. T.; Klein, W. L. The Ap oligomer hypothesis for synapse failure and memory loss in Alzheimer's disease. Neurobiol. Learn. Mem., 2011, 96(4), 529-543.
    • (2011) Neurobiol. Learn. Mem , vol.96 , Issue.4 , pp. 529-543
    • Ferreira, S.T.1    Klein, W.L.2
  • 9
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins and therapy
    • Selkoe, D. J. Alzheimer's disease: genes, proteins and therapy. Physiol. Rev., 2001, 81(2), 741-766.
    • (2001) Physiol. Rev , vol.81 , Issue.2 , pp. 741-766
    • Selkoe, D.J.1
  • 10
    • 0242330363 scopus 로고    scopus 로고
    • Cysteine proteases are the major beta-secretase in the regulated secretory pathway that provides most of the beta-amyloid in Alzheimer's disease: Role of BACE1 in the constitutive secretory pathway
    • Hook, V. Y.; Reisine, T. D. Cysteine proteases are the major beta-secretase in the regulated secretory pathway that provides most of the beta-amyloid in Alzheimer's disease: role of BACE1 in the constitutive secretory pathway. J. Neurosci. Res., 2003, 74(3), 393-405.
    • (2003) J. Neurosci. Res , vol.74 , Issue.3 , pp. 393-405
    • Hook, V.Y.1    Reisine, T.D.2
  • 11
    • 0026794746 scopus 로고
    • Mass spectrometry of purified amyloid beta protein in Alzheimer's disease
    • Mori, H.; Takio, K.; Ogawara, M.; Selkoe, D. J. Mass spectrometry of purified amyloid beta protein in Alzheimer's disease. J. Biol. Chem., 1992, 267(24), 17082-17086.
    • (1992) J. Biol. Chem , vol.267 , Issue.24 , pp. 17082-17086
    • Mori, H.1    Takio, K.2    Ogawara, M.3    Selkoe, D.J.4
  • 13
  • 14
    • 0028855851 scopus 로고
    • Dominant and differential deposition of distinct pi-amyloid peptide species, ApN3(pE), in senile plaques
    • Saido, T. C; Iwatsubo, T.; Mann, D. M. A.; Shimada, H.; Ihara, Y.; Kawashima, S. Dominant and differential deposition of distinct pi-amyloid peptide species, ApN3(pE), in senile plaques. Neuron, 1995, 14, 457-466.
    • (1995) Neuron , vol.14 , pp. 457-466
    • Saido, T.C.1    Iwatsubo, T.2    Mann, D.M.A.3    Shimada, H.4    Ihara, Y.5    Kawashima, S.6
  • 15
    • 0030582387 scopus 로고    scopus 로고
    • Amino- and carboxyl-terminal heterogeneity of p-amyloid peptides deposited in human brain
    • Saido, T. C; Yamao-Harigaya, W.; Iwatsubo, T.; Kawashima, S. Amino- and carboxyl-terminal heterogeneity of p-amyloid peptides deposited in human brain. Neurosci. Lett., 1996, 215, 173-176.
    • (1996) Neurosci. Lett , vol.215 , pp. 173-176
    • Saido, T.C.1    Yamao-Harigaya, W.2    Iwatsubo, T.3    Kawashima, S.4
  • 16
    • 0029889248 scopus 로고    scopus 로고
    • High-resolution separation of amyloid beta-peptides: Structural variants present in Alzheimer's disease amyloid
    • Naslund, J.; Karlstrom, A. R.; Tjernberg, L. O.; Schierhorn, A.; Terenius, L.; Nordstedt, C. High-resolution separation of amyloid beta-peptides: structural variants present in Alzheimer's disease amyloid. J. Neurochem., 1996, 67(1), 294-301.
    • (1996) J. Neurochem , vol.67 , Issue.1 , pp. 294-301
    • Naslund, J.1    Karlstrom, A.R.2    Tjernberg, L.O.3    Schierhorn, A.4    Terenius, L.5    Nordstedt, C.6
  • 17
    • 0030742712 scopus 로고    scopus 로고
    • Heterogeneity of water-soluble amyloid beta-peptide in Alzheimer's disease and Dowńs syndrome brains
    • Russo, C; Saido, T. C; DeBusk, L. M.; Tabaton, M.; Gambetti, P.; Teller, J. K. Heterogeneity of water-soluble amyloid beta-peptide in Alzheimer's disease and Dowńs syndrome brains. FEBS Lett., 1997, 409(3), 411-416.
    • (1997) FEBS Lett , vol.409 , Issue.3 , pp. 411-416
    • Russo, C.1    Saido, T.C.2    Debusk, L.M.3    Tabaton, M.4    Gambetti, P.5    Teller, J.K.6
  • 19
    • 0032815498 scopus 로고    scopus 로고
    • Hypothesis: Amyloid p-peptides truncated at the N-terminus contribute to the pathogenesis of Alzheimer's disease
    • Larner, A. J. Hypothesis: amyloid p-peptides truncated at the N-terminus contribute to the pathogenesis of Alzheimer's disease. Neurobiol. Aging, 1999, 20, 65-69.
    • (1999) Neurobiol. Aging , vol.20 , pp. 65-69
    • Larner, A.J.1
  • 21
    • 23844551164 scopus 로고    scopus 로고
    • Amino-terminally truncated Ap peptide species are the main component of cotton wool plaques
    • Miravalle, L.; Calero, M.; Takao, M.; Roher, A. E.; Ghetti, B.; Vidal, R. Amino-terminally truncated Ap peptide species are the main component of cotton wool plaques. Biochemistry, 2005, 44, 10810-10821.
    • (2005) Biochemistry , vol.44 , pp. 10810-10821
    • Miravalle, L.1    Calero, M.2    Takao, M.3    Roher, A.E.4    Ghetti, B.5    Vidal, R.6
  • 22
  • 23
    • 0037013209 scopus 로고    scopus 로고
    • p-Secretase processing in the trans-Golgi network preferentially generates truncated amyloid species that accumulate in Alzheimer's disease brain
    • Huse, J. T.; Liu, K.; Pijak, D. S.; Carlin, D.; Lee, V. M. -Y.; Doms, R. W. p-Secretase processing in the trans-Golgi network preferentially generates truncated amyloid species that accumulate in Alzheimer's disease brain. J. Biol. Chem., 2002, 277(18), 16278-16284.
    • (2002) J. Biol. Chem , vol.277 , Issue.18 , pp. 16278-16284
    • Huse, J.T.1    Liu, K.2    Pijak, D.S.3    Carlin, D.4    Lee, V.M.-Y.5    Doms, R.W.6
  • 24
    • 0038751845 scopus 로고    scopus 로고
    • Secretion and intracellular generation of truncated Ap in p-site amyloid-p precursor protein-cleaving enzyme expressing human neurons
    • Lee, E. B.; Skovronsky, D. M.; Abtahian, F.; Doms, R. W.; Lee, V. M. Y. Secretion and intracellular generation of truncated Ap in p-site amyloid-p precursor protein-cleaving enzyme expressing human neurons. J. Biol. Chem., 2003, 278(7), 4458-4466.
    • (2003) J. Biol. Chem , vol.278 , Issue.7 , pp. 4458-4466
    • Lee, E.B.1    Skovronsky, D.M.2    Abtahian, F.3    Doms, R.W.4    Lee, V.M.Y.5
  • 25
    • 33947305482 scopus 로고    scopus 로고
    • Characterization of Ap11-40/42 peptide deposition in Alzheimer's disease and young Down's syndrome brains: Implication of N-terminally truncated Ap species in the pathogenesis of Alzheimer's disease
    • Liu, K.; Solano, I.; Mann, D.; Lemere, C; Mercken, M.; Trojanowski, J. Q.; Lee, V. M. Y. Characterization of Ap11-40/42 peptide deposition in Alzheimer's disease and young Down's syndrome brains: implication of N-terminally truncated Ap species in the pathogenesis of Alzheimer's disease. Acta Neuropathol., 2006, 112(2), 163-174.
    • (2006) Acta Neuropathol , vol.112 , Issue.2 , pp. 163-174
    • Liu, K.1    Solano, I.2    Mann, D.3    Lemere, C.4    Mercken, M.5    Trojanowski, J.Q.6    Lee, V.M.Y.7
  • 27
    • 33750825049 scopus 로고    scopus 로고
    • High sensitivity analysis of amyloid-beta peptide composition in amyloid deposits from human and PS2APP mouse brain
    • Guntert, A.; Dobeli, H.; Bohrmann, B. High sensitivity analysis of amyloid-beta peptide composition in amyloid deposits from human and PS2APP mouse brain. Neuroscience, 2006, 143, 461-475.
    • (2006) Neuroscience , vol.143 , pp. 461-475
    • Guntert, A.1    Dobeli, H.2    Bohrmann, B.3
  • 29
    • 78149281327 scopus 로고    scopus 로고
    • Pyroglutamate-Ap: Role in the natural history of Alzheimer's disease
    • Gunn, A. P.; Masters, C. L.; Cherny, R. A. Pyroglutamate-Ap: role in the natural history of Alzheimer's disease. Int. J. Biochem. Cell Biol, 2010, 42(12), 1915-1918.
    • (2010) Int. J. Biochem. Cell Biol , vol.42 , Issue.12 , pp. 1915-1918
    • Gunn, A.P.1    Masters, C.L.2    Cherny, R.A.3
  • 30
    • 80655144756 scopus 로고    scopus 로고
    • Pyroglutamate amyloid p (Ap): A hatchet man in Alzheimer Disease
    • Jawhar, S.; Wirths, O.; Bayer, T. A. Pyroglutamate amyloid p (Ap): a hatchet man in Alzheimer Disease. J. Biol. Chem., 2011, 286(45), 38825-38832.
    • (2011) J. Biol. Chem , vol.286 , Issue.45 , pp. 38825-38832
    • Jawhar, S.1    Wirths, O.2    Bayer, T.A.3
  • 31
    • 81055155827 scopus 로고    scopus 로고
    • Pyroglutamate-Ap 3 and 11 colocalize in amyloid plaques in Alzheimer's disease cerebral cortex with pyroglutamate-Ap 11 forming central core
    • Sullivan, C. P.; Berg, E. A.; Elliot-Bryant, R.; Fishman, J. B.; McKee, A. C; Morin, P. J.; Shia, M. A.; Fine, R. E. Pyroglutamate-Ap 3 and 11 colocalize in amyloid plaques in Alzheimer's disease cerebral cortex with pyroglutamate-Ap 11 forming central core. Neurosci. Lett., 2011, 505(2), 109-112.
    • (2011) Neurosci. Lett , vol.505 , Issue.2 , pp. 109-112
    • Sullivan, C.P.1    Berg, E.A.2    Elliot-Bryant, R.3    Fishman, J.B.4    McKee, A.C.5    Morin, P.J.6    Shia, M.A.7    Fine, R.E.8
  • 32
    • 0034710784 scopus 로고    scopus 로고
    • Amyloid p protein starting pyroglutamate at position 3 is a major component of the amyloid deposits in the Alzheimers disease brain
    • Harigaya, Y.; Saido, T. C; Eckman, C. B.; Prada, C. M.; Shoji, M.; Younkin, S. G. Amyloid p protein starting pyroglutamate at position 3 is a major component of the amyloid deposits in the Alzheimers disease brain. Biochem. Biophys. Res. Comm., 2000, 276(2), 422-427.
    • (2000) Biochem. Biophys. Res. Comm , vol.276 , Issue.2 , pp. 422-427
    • Harigaya, Y.1    Saido, T.C.2    Eckman, C.B.3    Prada, C.M.4    Shoji, M.5    Younkin, S.G.6
  • 34
    • 76949102099 scopus 로고    scopus 로고
    • Pyroglutamate Abeta pathology in APP/PS1KI mice, sporadic and familial Alzheimer's disease cases
    • Wirths, O.; Bethge, T.; Marcello, A.; Harmeier, A.; Jawhar, S.; Lucassen, P. J.; Milthaup, G. Pyroglutamate Abeta pathology in APP/PS1KI mice, sporadic and familial Alzheimer's disease cases. J. Neural. Transm., 2010, 117(1), 85-96.
    • (2010) J. Neural. Transm , vol.117 , Issue.1 , pp. 85-96
    • Wirths, O.1    Bethge, T.2    Marcello, A.3    Harmeier, A.4    Jawhar, S.5    Lucassen, P.J.6    Milthaup, G.7
  • 37
    • 0028885682 scopus 로고
    • Amino-terminal Deletions Enhance Aggregation of beta-Amyloid Peptides in vitro
    • Pike, C. J.; Overman, M. J.; Cotman, C. W. Amino-terminal Deletions Enhance Aggregation of beta-Amyloid Peptides in vitro. J. Biol. Chem., 1995, 270(41), 23895-23898.
    • (1995) J. Biol. Chem , vol.270 , Issue.41 , pp. 23895-23898
    • Pike, C.J.1    Overman, M.J.2    Cotman, C.W.3
  • 38
    • 0033578402 scopus 로고    scopus 로고
    • The A beta 3-pyroglutamyl and 11-pyroglutamyl peptides found in senile plaque have greater beta-sheet forming and aggregation propensities in vitro than full-length A beta
    • He, W.; Barrow, C. J. The A beta 3-pyroglutamyl and 11-pyroglutamyl peptides found in senile plaque have greater beta-sheet forming and aggregation propensities in vitro than full-length A beta. Biochemistry, 1999, 38, 10871-10877.
    • (1999) Biochemistry , vol.38 , pp. 10871-10877
    • He, W.1    Barrow, C.J.2
  • 42
    • 70349787118 scopus 로고    scopus 로고
    • N-terminal truncated pyroglutamyl p amyloid peptide Appy3-42 shows a faster aggregation kinetics than the full-length Ap1-42
    • D'Arrigo, C; Tabaton, M.; Perico, A. N-terminal truncated pyroglutamyl p amyloid peptide Appy3-42 shows a faster aggregation kinetics than the full-length Ap1-42. Biopolymers, 2009, 91(10), 861-873.
    • (2009) Biopolymers , vol.91 , Issue.10 , pp. 861-873
    • D'Arrigo, C.1    Tabaton, M.2    Perico, A.3
  • 45
    • 0022654027 scopus 로고
    • Isolation of low-molecular-weight proteins from amyloid plaque fibers in Alzheimer's disease
    • Selkoe, D. J.; Abraham, C. R.; Podlisny, M. B.; Duffy, L. K. Isolation of low-molecular-weight proteins from amyloid plaque fibers in Alzheimer's disease. J. Neurochem., 1986, 46(6), 1820-1834.
    • (1986) J. Neurochem , vol.46 , Issue.6 , pp. 1820-1834
    • Selkoe, D.J.1    Abraham, C.R.2    Podlisny, M.B.3    Duffy, L.K.4
  • 46
    • 0024370108 scopus 로고
    • Relationships among the cerebral amyloid peptides and their precursors
    • Miller, D. L.; Currie, J. R.; Iqbal, K.; Potempska, A.; Styles, J. Relationships among the cerebral amyloid peptides and their precursors. Ann. Med., 1989, 21(2), 83-87.
    • (1989) Ann. Med , vol.21 , Issue.2 , pp. 83-87
    • Miller, D.L.1    Currie, J.R.2    Iqbal, K.3    Potempska, A.4    Styles, J.5
  • 48
    • 77952551031 scopus 로고    scopus 로고
    • Concomitant detection of p-amyloid peptides with N-terminal truncation and diffeent C-terminal endings in cortical plaques from cases with Alzheimer's disease, senile monkeys and triple transgenic mice
    • Hartig, W.; Goldhammer, S.; Bauer, U.; Wegner, F.; Wirths, O.; Bayer, T. A.; Grosche, J. Concomitant detection of p-amyloid peptides with N-terminal truncation and diffeent C-terminal endings in cortical plaques from cases with Alzheimer's disease, senile monkeys and triple transgenic mice. J. Chem. Neuroanatomy, 2010, 40, 82-92.
    • (2010) J. Chem. Neuroanatomy , vol.40 , pp. 82-92
    • Hartig, W.1    Goldhammer, S.2    Bauer, U.3    Wegner, F.4    Wirths, O.5    Bayer, T.A.6    Grosche, J.7
  • 49
    • 0029849644 scopus 로고    scopus 로고
    • Full-length amyloid beta (1-42(43)) and amino-terminally modified and truncated amyloid-beta 42(43) deposit in diffuse plaques
    • Iwatsubo, T.; Saido, T. C; Mann, D. M.; Lee, V. M.; Trojanowski, J. Q. Full-length amyloid beta (1-42(43)) and amino-terminally modified and truncated amyloid-beta 42(43) deposit in diffuse plaques. Am. J. Pathol, 1996, 149(6), 1823-1830.
    • (1996) Am. J. Pathol , vol.149 , Issue.6 , pp. 1823-1830
    • Iwatsubo, T.1    Saido, T.C.2    Mann, D.M.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 50
    • 0031559602 scopus 로고    scopus 로고
    • Isolation, Chemicalm characterization and quantitation of Ap 3-pyroglutamyl peptide from neuritic plaques and vascular amyloid deposits
    • Kuo, Y. M.; Emmerling, M. R.; Woods, A. S.; Cotter, R. J.; Roher, A. E. Isolation, Chemicalm characterization and quantitation of Ap 3-pyroglutamyl peptide from neuritic plaques and vascular amyloid deposits. Biochem. Biophys. Res. Commun., 1997, 237, 188-191.
    • (1997) Biochem. Biophys. Res. Commun , vol.237 , pp. 188-191
    • Kuo, Y.M.1    Emmerling, M.R.2    Woods, A.S.3    Cotter, R.J.4    Roher, A.E.5
  • 51
    • 84858051817 scopus 로고    scopus 로고
    • Detection of peri-synaptic amyloid-b pyroglutamate aggregates in early stages of Alzheimer's disease and in AbPP transgenic mice using a novel monoclonal antibody
    • Mandler, M.; Rockenstein, E.; Ubhi, K.; Hansen, L.; Adame, A.; Michael, S.; Galasko, D.; Santic, R.; Mattner, F.; Masliah, E. Detection of peri-synaptic amyloid-b pyroglutamate aggregates in early stages of Alzheimer's disease and in AbPP transgenic mice using a novel monoclonal antibody. J. Alzheimers Dis., 2012, 28(4), 783-794.
    • (2012) J. Alzheimers Dis , vol.28 , Issue.4 , pp. 783-794
    • Mandler, M.1    Rockenstein, E.2    Ubhi, K.3    Hansen, L.4    Adame, A.5    Michael, S.6    Galasko, D.7    Santic, R.8    Mattner, F.9    Masliah, E.10
  • 52
    • 79960882442 scopus 로고    scopus 로고
    • Intraneuronal Ap is a trigger for neuronal loss: Can this be translated into human pathology?
    • Bayer, T. A.; Wirths, O. Intraneuronal Ap is a trigger for neuronal loss: can this be translated into human pathology? Biochem. Soc. Trans., 2011, 39(4), 857-861.
    • (2011) Biochem. Soc. Trans , vol.39 , Issue.4 , pp. 857-861
    • Bayer, T.A.1    Wirths, O.2
  • 54
    • 84860519322 scopus 로고    scopus 로고
    • N-terminal pyroglutamate formation of Ap38 and Ap40 enforces oligomer formation and potency to disrupt hippocampal long-term potentiation
    • Schlenzig, D.; Ronicke, R.; Cynis, H.; Ludwig, H. H.; Scheel, E.; Reymann, K.; Saido, T.; Hause, G.; Schilling, S.; Demuth, H. U. N-terminal pyroglutamate formation of Ap38 and Ap40 enforces oligomer formation and potency to disrupt hippocampal long-term potentiation. J. Neurochem., 2012, 121(5), 774-784.
    • (2012) J. Neurochem , vol.121 , Issue.5 , pp. 774-784
    • Schlenzig, D.1    Ronicke, R.2    Cynis, H.3    Ludwig, H.H.4    Scheel, E.5    Reymann, K.6    Saido, T.7    Hause, G.8    Schilling, S.9    Demuth, H.U.10
  • 55
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed, R.; Head, E.; Thompson, J. L.; McIntire, T. M.; Milton, S. C; Cotman, C. W.; Glabe, C. G. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science, 2003, 300(5618), 486-489.
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5    Cotman, C.W.6    Glabe, C.G.7
  • 57
    • 0035863055 scopus 로고    scopus 로고
    • Age-dependent changes in brain, CSF, and plasma amyloid(beta) protein in the Tg2576 transgenic mouse model of Alzheimer's disease
    • Kawarabashi, T.; Younkin, L. H.; Saido, T. C; Shoji, M.; Ashe, K. H.; Younkin, S. G. Age-dependent changes in brain, CSF, and plasma amyloid(beta) protein in the Tg2576 transgenic mouse model of Alzheimer's disease. J. Neurosci., 2001, 21(2), 372-381.
    • (2001) J. Neurosci , vol.21 , Issue.2 , pp. 372-381
    • Kawarabashi, T.1    Younkin, L.H.2    Saido, T.C.3    Shoji, M.4    Ashe, K.H.5    Younkin, S.G.6
  • 61
    • 40449115788 scopus 로고    scopus 로고
    • Intraneuronal p-amyloid is a major risk factor - novel evidence from the APP/PS1KI mouse model
    • Bayer, T. A.; Breyhan, H.; Duan, K.; Rettig, J.; Wirths, O. Intraneuronal p-amyloid is a major risk factor - novel evidence from the APP/PS1KI mouse model. Neurodegener. Dis., 2008, 5(3-4), 140-142.
    • (2008) Neurodegener. Dis , vol.5 , Issue.3-4 , pp. 140-142
    • Bayer, T.A.1    Breyhan, H.2    Duan, K.3    Rettig, J.4    Wirths, O.5
  • 62
    • 67349160489 scopus 로고    scopus 로고
    • APP/PS1KI bigenic mice develop early synaptic deficits and hippocampus atrophy
    • Breyhan, H.; Wirths, O.; Duan, K.; Marcello, A.; Rettig, J.; Bayer, T. A. APP/PS1KI bigenic mice develop early synaptic deficits and hippocampus atrophy. Acta Neuropathol., 2009, 117(6), 677-685.
    • (2009) Acta Neuropathol , vol.117 , Issue.6 , pp. 677-685
    • Breyhan, H.1    Wirths, O.2    Duan, K.3    Marcello, A.4    Rettig, J.5    Bayer, T.A.6
  • 63
    • 34548553576 scopus 로고    scopus 로고
    • Age-dependent axonal degeneration in an Alzheimer mouse model
    • Wirths, O.; Weis, J.; Kayed, R.; Saido, T. C; Bayer, T. A. Age-dependent axonal degeneration in an Alzheimer mouse model. Neurobiol. Aging, 2007, 28, 1689-1699.
    • (2007) Neurobiol. Aging , vol.28 , pp. 1689-1699
    • Wirths, O.1    Weis, J.2    Kayed, R.3    Saido, T.C.4    Bayer, T.A.5
  • 64
    • 69949135716 scopus 로고    scopus 로고
    • Intraneuronal pyroglutamate-Abeta 3-42 triggers neurodegeneration and lethal neurological deficits in a transgenic mouse model
    • Wirths, O.; Breyhan, H.; Cynis, H.; Schilling, S.; Demuth, H. U.; Bayer, T. A. Intraneuronal pyroglutamate-Abeta 3-42 triggers neurodegeneration and lethal neurological deficits in a transgenic mouse model. Acta Neuropathol., 2009, 118(4), 487-496.
    • (2009) Acta Neuropathol , vol.118 , Issue.4 , pp. 487-496
    • Wirths, O.1    Breyhan, H.2    Cynis, H.3    Schilling, S.4    Demuth, H.U.5    Bayer, T.A.6
  • 66
    • 79953002787 scopus 로고    scopus 로고
    • Overexpression of glutaminyl cyclase, the enzyme responsible for pyroglutamate Ab formation, induces behavioral deficits, and glutaminyl cyclase knock-out rescues the behavioral phenotype in 5XFAD mice
    • Jawhar, S.; Wirths, O.; Schilling, S.; Graubner, S.; Demuth, H. U.; Bayer, T. A. Overexpression of glutaminyl cyclase, the enzyme responsible for pyroglutamate Ab formation, induces behavioral deficits, and glutaminyl cyclase knock-out rescues the behavioral phenotype in 5XFAD mice. J. Biol. Chem., 2011, 286(6), 4454-4460.
    • (2011) J. Biol. Chem , vol.286 , Issue.6 , pp. 4454-4460
    • Jawhar, S.1    Wirths, O.2    Schilling, S.3    Graubner, S.4    Demuth, H.U.5    Bayer, T.A.6
  • 68
    • 1842636794 scopus 로고    scopus 로고
    • Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions
    • Schilling, S.; Hoffmann, T.; Manhart, S.; Hoffmann, M.; Demuth, H. U. Glutaminyl cyclases unfold glutamyl cyclase activity under mild acid conditions. FEBS Lett, 2004, 563, 191-196.
    • (2004) FEBS Lett , vol.563 , pp. 191-196
    • Schilling, S.1    Hoffmann, T.2    Manhart, S.3    Hoffmann, M.4    Demuth, H.U.5
  • 69
    • 0000495632 scopus 로고
    • Identification of a mammalian glutaminyl cyclase converting glutaminyl into pyroglutamyl peptides
    • Fischer, W. H.; Spiess, J. Identification of a mammalian glutaminyl cyclase converting glutaminyl into pyroglutamyl peptides. Proc. Natl. Acad. Sci. USA, 1987, 84(11), 3628-3632.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , Issue.11 , pp. 3628-3632
    • Fischer, W.H.1    Spiess, J.2
  • 70
    • 47249117092 scopus 로고    scopus 로고
    • Amyloidogenic processing of amyloid precursor protein: Evidence of a pivotal role of glutaminyl cyclase in generation of pyroglutamate-modified amyloid-p
    • Cynis, H.; Scheel, E.; Saido, T. C; Schilling, S.; Demuth, H. U. Amyloidogenic processing of amyloid precursor protein: evidence of a pivotal role of glutaminyl cyclase in generation of pyroglutamate-modified amyloid-p. Biochemistry, 2008, 47, 7405-7413.
    • (2008) Biochemistry , vol.47 , pp. 7405-7413
    • Cynis, H.1    Scheel, E.2    Saido, T.C.3    Schilling, S.4    Demuth, H.U.5
  • 72
    • 84866107329 scopus 로고    scopus 로고
    • Disturbed Ca2+ homeostasis increases glutaminyl cyclase expression; connecting two early pathogenic events in Alzheimer's disease in vitro
    • De Kimpe, L.; Bennis, A.; Zwart, R.; van Haastert, E. S.; Hoozemans, J. J. Disturbed Ca2+ homeostasis increases glutaminyl cyclase expression; connecting two early pathogenic events in Alzheimer's disease in vitro. PLoS ONE 2012, 7(9), e44674.
    • (2012) PLoS ONE , vol.7 , Issue.9
    • de Kimpe, L.1    Bennis, A.2    Zwart, R.3    van Haastert, E.S.4    Hoozemans, J.J.5
  • 80
    • 47949132196 scopus 로고    scopus 로고
    • Active and passive immunotherapy for neurodegenerative disorders
    • Brody, D. L.; Holtzman, D. M. Active and passive immunotherapy for neurodegenerative disorders. Annu. Rev. Neurosci., 2008, 31, 175-193.
    • (2008) Annu. Rev. Neurosci , vol.31 , pp. 175-193
    • Brody, D.L.1    Holtzman, D.M.2
  • 82
    • 70449669057 scopus 로고    scopus 로고
    • Ap immunotherapy protects morphology and survival of adult-born neurons in doubly transgenic APP/PS1 mice
    • Biscaro, B.; Lindvall, O.; Hock, C; Ekdahl, C. T.; Nitsch, R. M. Ap immunotherapy protects morphology and survival of adult-born neurons in doubly transgenic APP/PS1 mice. J. Neurosci., 2009, 29(45), 14108-14119.
    • (2009) J. Neurosci , vol.29 , Issue.45 , pp. 14108-14119
    • Biscaro, B.1    Lindvall, O.2    Hock, C.3    Ekdahl, C.T.4    Nitsch, R.M.5
  • 83
    • 78650210590 scopus 로고    scopus 로고
    • Immunotherapy for Alzheimer's disease
    • Morgan, D. Immunotherapy for Alzheimer's disease. J. Intern. Med., 2011, 269(1), 54-63.
    • (2011) J. Intern. Med , vol.269 , Issue.1 , pp. 54-63
    • Morgan, D.1
  • 84
    • 76849091134 scopus 로고    scopus 로고
    • Can Alzheimer disease be prevented by amyloid-p immunotherapy?
    • Lemere, C. A.; Masliah, E. Can Alzheimer disease be prevented by amyloid-p immunotherapy? Nat. Rev. Neurol, 2010, 6(2), 108-119.
    • (2010) Nat. Rev. Neurol , vol.6 , Issue.2 , pp. 108-119
    • Lemere, C.A.1    Masliah, E.2
  • 86
    • 0037107177 scopus 로고    scopus 로고
    • Non-Fc-mediated mechanisms are involved in clearance of amyloid-beta in vivo by immunotherapy
    • Bacskai, B. J.; Kajdasz, S. T.; McLellan, M. E.; Games, D.; Seubert, P.; Schenk, D.; Hyman, B. T. Non-Fc-mediated mechanisms are involved in clearance of amyloid-beta in vivo by immunotherapy. J. Neurosci., 2002, 22, 7873-7878.
    • (2002) J. Neurosci , vol.22 , pp. 7873-7878
    • Bacskai, B.J.1    Kajdasz, S.T.2    McLellan, M.E.3    Games, D.4    Seubert, P.5    Schenk, D.6    Hyman, B.T.7
  • 89
    • 84859408039 scopus 로고    scopus 로고
    • Antibody 9D5 recognizes oligomeric pyroglutamate amyloid-b in a fraction of amyloid-b deposits in Alzheimer's disease without cross-reactivity with other protein aggregates
    • Venkataramani, V.; Wirths, O.; Budka, H.; Hartig, W.; Kovacs, G. G.; Bayer, T. A. Antibody 9D5 recognizes oligomeric pyroglutamate amyloid-b in a fraction of amyloid-b deposits in Alzheimer's disease without cross-reactivity with other protein aggregates. J. Alzheimers Dis., 2012, 29(2), 361-371.
    • (2012) J. Alzheimers Dis , vol.29 , Issue.2 , pp. 361-371
    • Venkataramani, V.1    Wirths, O.2    Budka, H.3    Hartig, W.4    Kovacs, G.G.5    Bayer, T.A.6
  • 90
    • 84862816040 scopus 로고    scopus 로고
    • Passive immunization against pyroglutamate-3 amyloid-b reduces plaque burden in Alzheimer-like transgenic mice: A pilot study
    • Frost, J. L.; Liu, B.; Kleinschmidt, M.; Schilling, S.; Demuth, H. U.; Lemere, C. A. Passive immunization against pyroglutamate-3 amyloid-b reduces plaque burden in Alzheimer-like transgenic mice: a pilot study. Neurodegenerative Dis., 2012, 10, 265-270.
    • (2012) Neurodegenerative Dis , vol.10 , pp. 265-270
    • Frost, J.L.1    Liu, B.2    Kleinschmidt, M.3    Schilling, S.4    Demuth, H.U.5    Lemere, C.A.6
  • 92
    • 79957951065 scopus 로고    scopus 로고
    • Aluminum vaccine adjuvants: Are they safe?
    • Tomljenovic, L.; Shaw, C. A. Aluminum vaccine adjuvants: are they safe? Curr. Med. Chem., 2011, 18, 2630-2637.
    • (2011) Curr. Med. Chem , vol.18 , pp. 2630-2637
    • Tomljenovic, L.1    Shaw, C.A.2
  • 93
    • 77951086901 scopus 로고    scopus 로고
    • Safety and changes in plasma and cerebrospinal fluid amyloid beta after a single administration of an amyloid beta monoclonal antibody in subjects with Alzheimer disease
    • Siemers, E. R.; Friedrich, S.; Dean, R A.; Gonzalez, C. R.; Farlow, M. R.; Paul, S. M.; DeMattos, R. B. Safety and changes in plasma and cerebrospinal fluid amyloid beta after a single administration of an amyloid beta monoclonal antibody in subjects with Alzheimer disease. Clin. Neuropharmacol, 2010, 33(2), 67-73.
    • (2010) Clin. Neuropharmacol , vol.33 , Issue.2 , pp. 67-73
    • Siemers, E.R.1    Friedrich, S.2    Dean, R.A.3    Gonzalez, C.R.4    Farlow, M.R.5    Paul, S.M.6    Demattos, R.B.7
  • 94
    • 79955803502 scopus 로고    scopus 로고
    • Solanezumab for Alzheimer's disease
    • Samadi, H.; Sultzer, D. Solanezumab for Alzheimer's disease. Expert Opin. Biol. Ther., 2011, 11(6), 787-798.
    • (2011) Expert Opin. Biol. Ther , vol.11 , Issue.6 , pp. 787-798
    • Samadi, H.1    Sultzer, D.2


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