메뉴 건너뛰기




Volumn 217, Issue 3-4, 2012, Pages 389-395

Structural aspects and physiological consequences of APP/APLP trans-dimerization

Author keywords

Alzheimer disease; APLP 1; APLP 2; Cell adhesion; Dimerization; Synaptogenesis

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; CELL ADHESION MOLECULE; OLIGOMER; PROTEIN APLP1; PROTEIN APLP2; UNCLASSIFIED DRUG;

EID: 84862867237     PISSN: 00144819     EISSN: 14321106     Source Type: Journal    
DOI: 10.1007/s00221-011-2878-6     Document Type: Review
Times cited : (38)

References (56)
  • 1
    • 33750151420 scopus 로고    scopus 로고
    • The functions of mammalian amyloid precursor protein and related amyloid precursor-like proteins
    • DOI 10.1159/000095262
    • Anliker B, Muller U (2006) The functions of mammalian amyloid precursor protein and related amyloid precursor-like proteins. Neurodegener Dis 3(4-5):239-246 (Pubitemid 44600310)
    • (2006) Neurodegenerative Diseases , vol.3 , Issue.4-5 , pp. 239-246
    • Anliker, B.1    Muller, U.2
  • 2
    • 79952903577 scopus 로고    scopus 로고
    • A single tyrosine residue in the amyloid precursor protein intracellular domain is essential for developmental function
    • doi:10.1074/jbc.C111.219873
    • Barbagallo AP, Wang Z, Zheng H, D'Adamio L (2011) A single tyrosine residue in the amyloid precursor protein intracellular domain is essential for developmental function. J Biol Chem 286(11):8717-8721. doi:10.1074/jbc.C111. 219873
    • (2011) J Biol Chem , vol.286 , Issue.11 , pp. 8717-8721
    • Barbagallo, A.P.1    Wang, Z.2    Zheng, H.3    D'Adamio, L.4
  • 3
    • 0034704089 scopus 로고    scopus 로고
    • Mints as adaptors. Direct binding to neurexins and recruitment of Munc18
    • DOI 10.1074/jbc.C000656200
    • Biederer T, Sudhof TC (2000) Mints as adaptors. Direct binding to neurexins and recruitment of munc18. J Biol Chem 275(51): 39803-39806. doi:10.1074/jbc.C000656200 (Pubitemid 32064595)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.51 , pp. 39803-39806
    • Biederer, T.1    Sudhof, T.C.2
  • 4
    • 0032510834 scopus 로고    scopus 로고
    • The X11α protein slows cellular amyloid precursor protein processing and reduces aβ40 and aβ42 secretion
    • DOI 10.1074/jbc.273.24.14761
    • Borg JP, Yang Y, De Taddeo-Borg M, Margolis B, Turner RS (1998) The X11alpha protein slows cellular amyloid precursor protein processing and reduces Abeta40 and Abeta42 secretion. J Biol Chem 273(24):14761-14766 (Pubitemid 28272761)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.24 , pp. 14761-14766
    • Borg, J.-P.1    Yang, Y.2    De Taddeo-Borg, M.3    Margolis, B.4    Turner, R.S.5
  • 5
    • 33747623018 scopus 로고    scopus 로고
    • Notch signalling: A simple pathway becomes complex
    • DOI 10.1038/nrm2009, PII NRM2009
    • Bray SJ (2006) Notch signalling: a simple pathway becomes complex. Nat Rev Mol Cell Biol 7(9):678-689. doi:10.1038/nrm2009 (Pubitemid 44268213)
    • (2006) Nature Reviews Molecular Cell Biology , vol.7 , Issue.9 , pp. 678-689
    • Bray, S.J.1
  • 7
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptivety active complex of APP with Fe65 and histone acetyltransferase Tip60
    • DOI 10.1126/science.1058783
    • Cao X, Sudhof TC (2001) A transcriptionally [correction of transcriptively] active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293(5527):115-120 (Pubitemid 32625507)
    • (2001) Science , vol.293 , Issue.5527 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 9
    • 77950385325 scopus 로고    scopus 로고
    • Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein
    • doi:10.1073/pnas.09113 26107
    • Dahms SO, Hoefgen S, Roeser D, Schlott B, Guhrs KH, Than ME (2010) Structure and biochemical analysis of the heparin-induced E1 dimer of the amyloid precursor protein. Proc Natl Acad Sci USA 107(12):5381-5386. doi:10.1073/pnas.09113 26107
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.12 , pp. 5381-5386
    • Dahms, S.O.1    Hoefgen, S.2    Roeser, D.3    Schlott, B.4    Guhrs, K.H.5    Than, M.E.6
  • 10
    • 33847119026 scopus 로고    scopus 로고
    • Cell adhesion molecules: Signalling functions at the synapse
    • DOI 10.1038/nrn2075, PII NRN2075
    • Dalva MB, McClelland AC, Kayser MS (2007) Cell adhesion molecules: signalling functions at the synapse. Nat Rev Neurosci 8(3):206-220. doi:10.1038/nrn2075 (Pubitemid 46294663)
    • (2007) Nature Reviews Neuroscience , vol.8 , Issue.3 , pp. 206-220
    • Dalva, M.B.1    McClelland, A.C.2    Kayser, M.S.3
  • 11
    • 30344454380 scopus 로고    scopus 로고
    • Neuroligins and neurexins: Linking cell adhesion, synapse formation and cognitive function
    • DOI 10.1016/j.tins.2005.11.003, PII S0166223605003000
    • Dean C, Dresbach T (2006) Neuroligins and neurexins: linking cell adhesion, synapse formation and cognitive function. Trends Neurosci 29(1):21-29. doi:10.1016/j.tins.2005.11.003 (Pubitemid 43063127)
    • (2006) Trends in Neurosciences , vol.29 , Issue.1 , pp. 21-29
    • Dean, C.1    Dresbach, T.2
  • 12
    • 2442592973 scopus 로고    scopus 로고
    • The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves α-, β-, γ-, and ε-Like cleavages: Modulation of APLP-1 processing by N-glycosylation
    • DOI 10.1074/jbc.M311601200
    • Eggert S, Paliga K, Soba P, Evin G, Masters CL, Weidemann A, Beyreuther K (2004) The proteolytic processing of the amyloid precursor protein gene family members APLP-1 and APLP-2 involves alpha-, beta-, gamma-, and epsilon-like cleavages: modulation of APLP-1 processing by n-glycosylation. J Biol Chem 279(18):18146-18156 (Pubitemid 38623227)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.18 , pp. 18146-18156
    • Eggert, S.1    Paliga, K.2    Soba, P.3    Evin, G.4    Masters, C.L.5    Weidemann, A.6    Beyreuther, K.7
  • 13
    • 70350350069 scopus 로고    scopus 로고
    • Induced dimerization of the amyloid precursor protein leads to decreased amyloid-beta protein production
    • Eggert S, Midthune B, Cottrell B, Koo EH (2009) Induced dimerization of the amyloid precursor protein leads to decreased amyloid-beta protein production. J Biol Chem 284(42):28943-28952
    • (2009) J Biol Chem , vol.284 , Issue.42 , pp. 28943-28952
    • Eggert, S.1    Midthune, B.2    Cottrell, B.3    Koo, E.H.4
  • 14
    • 34248172449 scopus 로고    scopus 로고
    • Structure and functions of the human amyloid precursor protein: The whole is more than the sum of its parts
    • DOI 10.1016/j.pneurobio.2007.02.001, PII S0301008207000160
    • Gralle M, Ferreira ST (2007) Structure and functions of the human amyloid precursor protein: the whole is more than the sum of its parts. Prog Neurobiol 82(1):11-32 (Pubitemid 46719589)
    • (2007) Progress in Neurobiology , vol.82 , Issue.1 , pp. 11-32
    • Gralle, M.1    Ferreira, S.T.2
  • 16
    • 84855483701 scopus 로고    scopus 로고
    • APP physiological and pathophysiological functions: Insights from animal models
    • doi:10.1038/cr.2011.116
    • Guo Q, Wang Z, Li H, Wiese M, Zheng H (2011) APP physiological and pathophysiological functions: insights from animal models. Cell Res. doi:10.1038/cr.2011.116
    • (2011) Cell Res.
    • Guo, Q.1    Wang, Z.2    Li, H.3    Wiese, M.4    Zheng, H.5
  • 17
    • 77955328980 scopus 로고    scopus 로고
    • Fyn-tau-amyloid: A toxic triad
    • doi:10.1016/j.cell.2010.07.032
    • Haass C, Mandelkow E (2010) Fyn-tau-amyloid: a toxic triad. Cell 142(3):356-358. doi:10.1016/j.cell.2010.07.032
    • (2010) Cell , vol.142 , Issue.3 , pp. 356-358
    • Haass, C.1    Mandelkow, E.2
  • 18
    • 1442306058 scopus 로고    scopus 로고
    • Binding of F-spondin to amyloid-β precursor protein: A candidate amyloid-β precursor protein ligand that modulates amyloid-β precursor protein cleavage
    • DOI 10.1073/pnas.0308655100
    • Ho A, Sudhof TC (2004) 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(8):2548-2553 (Pubitemid 38269348)
    • (2004) Proceedings of the National Academy of Sciences of the United States of America , vol.101 , Issue.8 , pp. 2548-2553
    • Ho, A.1    Sudhof, T.C.2
  • 21
    • 67650383731 scopus 로고    scopus 로고
    • Amyloid precursor protein and its homologues: A family of proteolysis-dependent receptors
    • Jacobsen KT, Iverfeldt K (2009) Amyloid precursor protein and its homologues: a family of proteolysis-dependent receptors. Cell Mol Life Sci 66(14):2299-2318
    • (2009) Cell Mol Life Sci , vol.66 , Issue.14 , pp. 2299-2318
    • Jacobsen, K.T.1    Iverfeldt, K.2
  • 22
    • 43749112022 scopus 로고    scopus 로고
    • Homophilic interactions of the amyloid precursor protein (APP) ectodomain are regulated by the loop region and affect beta-secretase cleavage of APP
    • Kaden D, Munter LM, Joshi M, Treiber C, Weise C, Bethge T, Voigt P, Schaefer M, Beyermann M, Reif B, Multhaup G (2008) Homophilic interactions of the amyloid precursor protein (APP) ectodomain are regulated by the loop region and affect beta-secretase cleavage of APP. J Biol Chem 283(11):7271-7279
    • (2008) J Biol Chem , vol.283 , Issue.11 , pp. 7271-7279
    • Kaden, D.1    Munter, L.M.2    Joshi, M.3    Treiber, C.4    Weise, C.5    Bethge, T.6    Voigt, P.7    Schaefer, M.8    Beyermann, M.9    Reif, B.10    Multhaup, G.11
  • 23
    • 65249143369 scopus 로고    scopus 로고
    • Subcellular localization and dimerization of APLP1 are strikingly different from APP and APLP2
    • Kaden D, Voigt P, Munter LM, Bobowski KD, Schaefer M, Multhaup G (2009) Subcellular localization and dimerization of APLP1 are strikingly different from APP and APLP2. J Cell Sci 122(Pt 3):368-377
    • (2009) J Cell Sci , vol.122 , Issue.PART 3 , pp. 368-377
    • Kaden, D.1    Voigt, P.2    Munter, L.M.3    Bobowski, K.D.4    Schaefer, M.5    Multhaup, G.6
  • 24
    • 0029015855 scopus 로고
    • Selective localization of amyloid precursor-like protein 1 in the cerebral cortex postsynaptic density
    • Kim TW, Wu K, Xu JL, McAuliffe G, Tanzi RE, Wasco W, Black IB (1995) Selective localization of amyloid precursor-like protein 1 in the cerebral cortex postsynaptic density. Brain Res Mol Brain Res 32(1):36-44
    • (1995) Brain Res Mol Brain Res , vol.32 , Issue.1 , pp. 36-44
    • Kim, T.W.1    Wu, K.2    Xu, J.L.3    McAuliffe, G.4    Tanzi, R.E.5    Wasco, W.6    Black, I.B.7
  • 25
    • 79955528442 scopus 로고    scopus 로고
    • Extracellular matrix and cell signalling: The dynamic cooperation of integrin, proteoglycan and growth factor receptor
    • doi: 10.1530/JOE-10-0377
    • Kim SH, Turnbull J, Guimond S (2011) Extracellular matrix and cell signalling: the dynamic cooperation of integrin, proteoglycan and growth factor receptor. J Endocrinol 209(2):139-151. doi: 10.1530/JOE-10-0377
    • (2011) J Endocrinol , vol.209 , Issue.2 , pp. 139-151
    • Kim, S.H.1    Turnbull, J.2    Guimond, S.3
  • 26
    • 84655176840 scopus 로고    scopus 로고
    • AICD nuclear signaling and its possible contribution to alzheimer's disease
    • [Epub ahead of print]
    • Konietzko U (2011) AICD nuclear signaling and its possible contribution to Alzheimer's disease. Curr Alzheimer Res [Epub ahead of print]
    • (2011) Curr Alzheimer Res
    • Konietzko, U.1
  • 27
    • 0027484116 scopus 로고
    • The Alzheimer β-amyloid protein precursor/protease nexin-II is cleaved by secretase in a trans-Golgi secretory compartment in human neuroglioma cells
    • Kuentzel SL, Ali SM, Altman RA, Greenberg BD, Raub TJ (1993) The Alzheimer beta-amyloid protein precursor/protease nexin-II is cleaved by secretase in a trans-Golgi secretory compartment in human neuroglioma cells. Biochem J 295(Pt 2):367-378 (Pubitemid 23315173)
    • (1993) Biochemical Journal , vol.295 , Issue.2 , pp. 367-378
    • Kuentzel, S.L.1    Ali, S.M.2    Altman, R.A.3    Greenberg, B.D.4    Raub, T.J.5
  • 29
    • 79959284264 scopus 로고    scopus 로고
    • The E2 domains of APP and APLP1 share a conserved mode of dimerization
    • doi:10.1021/bi101846x
    • Lee S, Xue Y, Hu J, Wang Y, Liu X, Demeler B, Ha Y (2011) The E2 domains of APP and APLP1 share a conserved mode of dimerization. Biochemistry 50(24):5453. doi:10.1021/bi101846x
    • (2011) Biochemistry , vol.50 , Issue.24 , pp. 5453
    • Lee, S.1    Xue, Y.2    Hu, J.3    Wang, Y.4    Liu, X.5    Demeler, B.6    Ha, Y.7
  • 30
    • 78049267204 scopus 로고    scopus 로고
    • Soluble amyloid precursor protein (APP) regulates transthyretin and klotho gene expression without rescuing the essential function of APP
    • doi:10.1073/pnas.1012568107
    • Li H, Wang B, Wang Z, Guo Q, Tabuchi K, Hammer RE, Sudhof TC, Zheng H (2010) Soluble amyloid precursor protein (APP) regulates transthyretin and Klotho gene expression without rescuing the essential function of APP. Proc Natl Acad Sci USA 107(40):17362-17367. doi:10.1073/pnas.1012568107
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.40 , pp. 17362-17367
    • Li, H.1    Wang, B.2    Wang, Z.3    Guo, Q.4    Tabuchi, K.5    Hammer, R.E.6    Sudhof, T.C.7    Zheng, H.8
  • 31
    • 0028914672 scopus 로고
    • Expression in mouse embryos and in adult mouse brain of three members of the amyloid precursor protein family, of the alpha-2-macroglobulin receptor/low density lipoprotein receptor-related protein and of its ligands apolipoprotein E, lipoprotein lipase, alpha-2-macroglobulin and the 40,000 molecular weight receptor-associated protein
    • Lorent K, Overbergh L, Moechars D, De Strooper B, Van Leuven F, Van den Berghe H (1995) Expression in mouse embryos and in adult mouse brain of three members of the amyloid precursor protein family, of the alpha-2-macroglobulin receptor/low density lipoprotein receptor-related protein and of its ligands apolipoprotein E, lipoprotein lipase, alpha-2-macroglobulin and the 40,000 molecular weight receptor-associated protein. Neuroscience 65(4):1009-1025
    • (1995) Neuroscience , vol.65 , Issue.4 , pp. 1009-1025
    • Lorent, K.1    Overbergh, L.2    Moechars, D.3    De Strooper, B.4    Van Leuven, F.5    Van Den Berghe, H.6
  • 32
    • 0032079899 scopus 로고    scopus 로고
    • Post-translational processing and turnover kinetics of presynaptically targeted amyloid precursor superfamily proteins in the central nervous system
    • DOI 10.1074/jbc.273.18.11100
    • Lyckman AW, Confaloni AM, Thinakaran G, Sisodia SS, Moya KL (1998) Post-translational processing and turnover kinetics of presynaptically targeted amyloid precursor superfamily proteins in the central nervous system. J Biol Chem 273(18):11100-11106 (Pubitemid 28204956)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.18 , pp. 11100-11106
    • Lyckman, A.W.1    Confaloni, A.M.2    Thinakaran, G.3    Sisodia, S.S.4    Moya, K.L.5
  • 34
    • 3042534412 scopus 로고    scopus 로고
    • Basal lamina and the organization of neuromuscular synapses
    • DOI 10.1023/B:NEUR.0000020630.74955.19
    • Patton BL (2003) Basal lamina and the organization of neuromuscular synapses. J Neurocytol 32(5-8):883-903. doi:10.1023/B:NEUR. 0000020630.74955.19 (Pubitemid 39011267)
    • (2003) Journal of Neurocytology , vol.32 , Issue.5-8 , pp. 883-903
    • Patton, B.L.1
  • 35
    • 55549113149 scopus 로고    scopus 로고
    • Structure of the intracellular domain of the amyloid precursor in complex with fe65-PTB2
    • Radzimanowski J, Simon B, Sattler M, Beyreuther K, Sinning I, Wild K (2008) Structure of the intracellular domain of the amyloid precursor in complex with Fe65-PTB2. EMBO Rep 9(11):1134-1140
    • (2008) EMBO Rep , vol.9 , Issue.11 , pp. 1134-1140
    • Radzimanowski, J.1    Simon, B.2    Sattler, M.3    Beyreuther, K.4    Sinning, I.5    Wild, K.6
  • 36
    • 0035970301 scopus 로고    scopus 로고
    • Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR
    • DOI 10.1006/jmbi.2001.4535
    • Ramelot TA, Nicholson LK (2001) Phosphorylation-induced structural changes in the amyloid precursor protein cytoplasmic tail detected by NMR. J Mol Biol 307(3):871-884. doi:10.1006/jmbi.2001.4535 (Pubitemid 33027665)
    • (2001) Journal of Molecular Biology , vol.307 , Issue.3 , pp. 871-884
    • Ramelot, T.A.1    Nicholson, L.K.2
  • 37
    • 28644437291 scopus 로고    scopus 로고
    • The amyloid-β precursor protein: Integrating structure with biological function
    • DOI 10.1038/sj.emboj.7600860
    • Reinhard C, Hebert SS, De Strooper B (2005) The amyloid-beta precursor protein: integrating structure with biological function. EMBO J 24(23):3996-4006 (Pubitemid 41752869)
    • (2005) EMBO Journal , vol.24 , Issue.23 , pp. 3996-4006
    • Reinhard, C.1    Hebert, S.S.2    De Strooper, B.3
  • 40
    • 0035954426 scopus 로고    scopus 로고
    • The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement
    • DOI 10.1083/jcb.153.7.1403
    • Sabo SL, Ikin AF, Buxbaum JD, Greengard P (2001) The Alzheimer amyloid precursor protein (APP) and FE65, an APP-binding protein, regulate cell movement. J Cell Biol 153(7):1403-1414 (Pubitemid 34286125)
    • (2001) Journal of Cell Biology , vol.153 , Issue.7 , pp. 1403-1414
    • Sabo, S.L.1    Ikin, A.F.2    Buxbaum, J.D.3    Greengard, P.4
  • 41
    • 0029970325 scopus 로고    scopus 로고
    • APP gene family. Alternative splicing generates functionally related isoforms
    • Sandbrink R, Masters CL, Beyreuther K (1996) APP gene family. Alternative splicing generates functionally related isoforms. Ann N Y Acad Sci 777:281-287
    • (1996) Ann N y Acad Sci , vol.777 , pp. 281-287
    • Sandbrink, R.1    Masters, C.L.2    Beyreuther, K.3
  • 42
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • DOI 10.1126/science.1074069
    • Selkoe DJ (2002) Alzheimer's disease is a synaptic failure. Science 298(5594):789-791 (Pubitemid 35231524)
    • (2002) Science , vol.298 , Issue.5594 , pp. 789-791
    • Selkoe, D.J.1
  • 43
    • 0028059841 scopus 로고
    • Expression of a ubiquitous, cross-reactive homologue of the mouse beta-amyloid precursor protein (APP)
    • Slunt HH, Thinakaran G, Von Koch C, Lo AC, Tanzi RE, Sisodia SS (1994) Expression of a ubiquitous, cross-reactive homologue of the mouse beta-amyloid precursor protein (APP). J Biol Chem 269(4):2637-2644
    • (1994) J Biol Chem , vol.269 , Issue.4 , pp. 2637-2644
    • Slunt, H.H.1    Thinakaran, G.2    Von Koch, C.3    Lo, A.C.4    Tanzi, R.E.5    Sisodia, S.S.6
  • 45
    • 57649221135 scopus 로고    scopus 로고
    • Amyloid precursor protein trafficking, processing, and function
    • Thinakaran G, Koo EH (2008) Amyloid precursor protein trafficking, processing, and function. J Biol Chem 283(44):29615-29619
    • (2008) J Biol Chem , vol.283 , Issue.44 , pp. 29615-29619
    • Thinakaran, G.1    Koo, E.H.2
  • 46
    • 0042634362 scopus 로고    scopus 로고
    • Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory
    • DOI 10.1016/S0301-0082(03)00089-3
    • Turner PR, O'Connor K, Tate WP, Abraham WC (2003) Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory. Prog Neurobiol 70(1):1-32 (Pubitemid 36966639)
    • (2003) Progress in Neurobiology , vol.70 , Issue.1 , pp. 1-32
    • Turner, P.R.1    O'Connor, K.2    Tate, W.P.3    Abraham, W.C.4
  • 50
    • 4143105782 scopus 로고    scopus 로고
    • The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain
    • DOI 10.1016/j.molcel.2004.06.037, PII S109727650400379X
    • Wang Y, Ha Y (2004) The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain. Mol Cell 15(3):343-353 (Pubitemid 39092751)
    • (2004) Molecular Cell , vol.15 , Issue.3 , pp. 343-353
    • Wang, Y.1    Ha, Y.2
  • 51
    • 69749090759 scopus 로고    scopus 로고
    • The APP-interacting protein FE65 is required for hippocampus-dependent learning and long-term potentiation
    • doi:10.1101/lm.1499309
    • Wang Y, Zhang M, Moon C, Hu Q, Wang B, Martin G, Sun Z, Wang H (2009a) The APP-interacting protein FE65 is required for hippocampus-dependent learning and long-term potentiation. Learn Mem 16(9):537-544. doi:10.1101/lm.1499309
    • (2009) Learn Mem , vol.16 , Issue.9 , pp. 537-544
    • Wang, Y.1    Zhang, M.2    Moon, C.3    Hu, Q.4    Wang, B.5    Martin, G.6    Sun, Z.7    Wang, H.8
  • 52
    • 69749115919 scopus 로고    scopus 로고
    • Presynaptic and postsynaptic interaction of the amyloid precursor protein promotes peripheral and central synaptogenesis
    • Wang Z, Wang B, Yang L, Guo Q, Aithmitti N, Songyang Z, Zheng H (2009b) Presynaptic and postsynaptic interaction of the amyloid precursor protein promotes peripheral and central synaptogenesis. J Neurosci 29(35):10788-10801
    • (2009) J Neurosci , vol.29 , Issue.35 , pp. 10788-10801
    • Wang, Z.1    Wang, B.2    Yang, L.3    Guo, Q.4    Aithmitti, N.5    Songyang, Z.6    Zheng, H.7
  • 54
    • 65649118535 scopus 로고    scopus 로고
    • AbetaPP/APLP2 family of kunitz serine proteinase inhibitors regulate cerebral thrombosis
    • doi:10.1523/JNEUROSCI.0095-09.2009
    • Xu F, Previti ML, Nieman MT, Davis J, Schmaier AH, Van Nostrand WE (2009) AbetaPP/APLP2 family of Kunitz serine proteinase inhibitors regulate cerebral thrombosis. J Neurosci 29(17):5666-5670. doi:10.1523/JNEUROSCI.0095-09.2009
    • (2009) J Neurosci , vol.29 , Issue.17 , pp. 5666-5670
    • Xu, F.1    Previti, M.L.2    Nieman, M.T.3    Davis, J.4    Schmaier, A.H.5    Van Nostrand, W.E.6
  • 55
    • 46149126877 scopus 로고    scopus 로고
    • Secreted APP regulates the function of full-length APP in neurite outgrowth through interaction with integrin beta1
    • Young-Pearse TL, Chen AC, Chang R, Marquez C, Selkoe DJ (2008) Secreted APP regulates the function of full-length APP in neurite outgrowth through interaction with integrin beta1. Neural Dev 3:15
    • (2008) Neural Dev , vol.3 , pp. 15
    • Young-Pearse, T.L.1    Chen, A.C.2    Chang, R.3    Marquez, C.4    Selkoe, D.J.5
  • 56
    • 79955128215 scopus 로고    scopus 로고
    • Biology and pathophysiology of the amyloid precursor protein
    • doi: 10.1186/1750-1326-6-27
    • Zheng H, Koo EH (2011) Biology and pathophysiology of the amyloid precursor protein. Mol Neurodegener 6(1):27. doi: 10.1186/1750-1326-6-27
    • (2011) Mol Neurodegener , vol.6 , Issue.1 , pp. 27
    • Zheng, H.1    Koo, E.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.