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Volumn 3, Issue 7, 2007, Pages 374-382

Mechanisms of disease: New therapeutic strategies for Alzheimer's disease - Targeting APP processing in lipid rafts

Author keywords

[No Author keywords available]

Indexed keywords

3BETA (2 DIETHYLAMINOETHOXY)ANDROST 5 EN 17 ONE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; BETA SECRETASE 1; BETA SECRETASE INHIBITOR; CHOLESTEROL; GAMMA SECRETASE; GAMMA SECRETASE INHIBITOR; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; METHYL BETA CYCLODEXTRIN; MEVINOLIN; UNCLASSIFIED DRUG;

EID: 34447273123     PISSN: 1745834X     EISSN: 17458358     Source Type: Journal    
DOI: 10.1038/ncpneuro0549     Document Type: Review
Times cited : (89)

References (59)
  • 2
    • 4344630985 scopus 로고    scopus 로고
    • BACE1: The β-secretase enzyme in Alzheimer's disease
    • Vassar R (2004) BACE1: The β-secretase enzyme in Alzheimer's disease. J Mol Neurosci 23: 105-114
    • (2004) J Mol Neurosci , vol.23 , pp. 105-114
    • Vassar, R.1
  • 3
    • 0242330374 scopus 로고    scopus 로고
    • ADAMs family members as amyloid precursor protein alpha-secretases
    • Allinson TM et al. (2003) ADAMs family members as amyloid precursor protein alpha-secretases. J Neurosci Res 74: 342-352
    • (2003) J Neurosci Res , vol.74 , pp. 342-352
    • Allinson, T.M.1
  • 4
    • 2942604376 scopus 로고    scopus 로고
    • The γ-secretase complex: Machinery for intramembrane proteolysis
    • Iwatsubo T (2004) The γ-secretase complex: Machinery for intramembrane proteolysis. Curr Opin Neurobial 14: 379-383
    • (2004) Curr Opin Neurobial , vol.14 , pp. 379-383
    • Iwatsubo, T.1
  • 5
    • 0035923502 scopus 로고    scopus 로고
    • Alzheimer's β-secretase, β-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase
    • Kitazume S et al. (2001) Alzheimer's β-secretase, β-site amyloid precursor protein-cleaving enzyme, is responsible for cleavage secretion of a Golgi-resident sialyltransferase. Proc Natl Acad Sci USA 98: 13554-13559
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 13554-13559
    • Kitazume, S.1
  • 6
    • 1642345964 scopus 로고    scopus 로고
    • Cleavage of amyloid-β precursor protein and amyloid-β precursor-like protein by BACE 1
    • Li Q et al. (2004) Cleavage of amyloid-β precursor protein and amyloid-β precursor-like protein by BACE 1. J Biol Chem 279 10542-10550
    • (2004) J Biol Chem , vol.279 , pp. 10542-10550
    • Li, Q.1
  • 7
    • 0842325530 scopus 로고    scopus 로고
    • The cell adhesion protein P-selectin glycoprotein ligand-1 is a substrate for the aspartyl protease BACE1
    • Lichtenthaler SF et al. (2003) The cell adhesion protein P-selectin glycoprotein ligand-1 is a substrate for the aspartyl protease BACE1. J Biol Chem 278 48713-48719
    • (2003) J Biol Chem , vol.278 , pp. 48713-48719
    • Lichtenthaler, S.F.1
  • 8
    • 24044497252 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-rellated protein (LRP) is a novel β-secretase (BACE1) substrate
    • von Arnim CA et al. (2005) The low density lipoprotein receptor-rellated protein (LRP) is a novel β-secretase (BACE1) substrate. J Biol Chem 280: 17777-17785
    • (2005) J Biol Chem , vol.280 , pp. 17777-17785
    • von Arnim, C.A.1
  • 9
    • 20744454142 scopus 로고    scopus 로고
    • β Subunits of voltage-gated sodium channels are novel substrates of β-site amyloid precursor protein-cleaving enzyme (BACE1) and γ-secretase
    • Wong HK et al. (2005) β Subunits of voltage-gated sodium channels are novel substrates of β-site amyloid precursor protein-cleaving enzyme (BACE1) and γ-secretase. J Biol Chem 280: 23009-23017
    • (2005) J Biol Chem , vol.280 , pp. 23009-23017
    • Wong, H.K.1
  • 10
    • 33845236399 scopus 로고    scopus 로고
    • Bace1 modulates myelination in the central and peripheral nervous system
    • Hu X et al. (2006) Bace1 modulates myelination in the central and peripheral nervous system. Nat Neurosci 9: 1520-1525
    • (2006) Nat Neurosci , vol.9 , pp. 1520-1525
    • Hu, X.1
  • 11
    • 33750455150 scopus 로고    scopus 로고
    • Control of peripheral nerve myelination by the β-secretase BACE1
    • Willem M et al. (2006) Control of peripheral nerve myelination by the β-secretase BACE1. Science 314: 664-666
    • (2006) Science , vol.314 , pp. 664-666
    • Willem, M.1
  • 12
    • 0037111837 scopus 로고    scopus 로고
    • Evidence that synaptically released β-amyloid accumulates as extracellular deposits in the hippocampus of transgenic mice
    • Lazarov O et al. (2002) Evidence that synaptically released β-amyloid accumulates as extracellular deposits in the hippocampus of transgenic mice. J Neurosci 22: 9785-9793
    • (2002) J Neurosci , vol.22 , pp. 9785-9793
    • Lazarov, O.1
  • 13
    • 0025056563 scopus 로고
    • Precursor of amyloid protein in Alzheimer disease undergoes fast anterograde axonal transport
    • Koo EH et al. (1990) Precursor of amyloid protein in Alzheimer disease undergoes fast anterograde axonal transport. Proc Natl Acad Sci USA 87: 1561-1565
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 1561-1565
    • Koo, E.H.1
  • 14
    • 0026721943 scopus 로고
    • β-amyloid precursor protein cleavage by a membrane-bound protease
    • Sisodia SS (1992) β-amyloid precursor protein cleavage by a membrane-bound protease. Proc Natl Acad Sci USA 89: 6075-6079
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6075-6079
    • Sisodia, S.S.1
  • 15
    • 0034721842 scopus 로고    scopus 로고
    • Maturation and endosomal targeting of β-site amyloid precursor protein-cleaving enzyme: The Alzheimer's disease β-secretase
    • Huse JT et al. (2000) Maturation and endosomal targeting of β-site amyloid precursor protein-cleaving enzyme: The Alzheimer's disease β-secretase. J Biol Chem 275: 33729-33737
    • (2000) J Biol Chem , vol.275 , pp. 33729-33737
    • Huse, J.T.1
  • 16
    • 0028276801 scopus 로고
    • Evidence that production and release of amyloid β-protein involves the endocytic pathway
    • Koo EH et al. (1994) Evidence that production and release of amyloid β-protein involves the endocytic pathway. J Biol Chem 269: 17386-17389
    • (1994) J Biol Chem , vol.269 , pp. 17386-17389
    • Koo, E.H.1
  • 17
    • 0029942495 scopus 로고    scopus 로고
    • Metabolism of the "Swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "β-secretase" site occurs in the Golgi apparatus
    • Thinakaran G et al. (1996) Metabolism of the "Swedish" amyloid precursor protein variant in neuro2a (N2a) cells. Evidence that cleavage at the "β-secretase" site occurs in the Golgi apparatus. J Biol Chem 271: 9390-9397
    • (1996) J Biol Chem , vol.271 , pp. 9390-9397
    • Thinakaran, G.1
  • 18
    • 7244258941 scopus 로고    scopus 로고
    • Association of γ-secretase with lipid rafts in post-Golgi and endosome membranes
    • Vetrivel KS et al. (2004) Association of γ-secretase with lipid rafts in post-Golgi and endosome membranes. J Biol Chem 279: 44945-44954
    • (2004) J Biol Chem , vol.279 , pp. 44945-44954
    • Vetrivel, K.S.1
  • 19
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • Simons K et al. (2000) Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1: 31-39
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1
  • 20
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid raft in biological membranes
    • Brown DA et al. (1998) Functions of lipid raft in biological membranes. Annu Rev Cell Dev Biol 14: 111-136
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1
  • 21
    • 22744437388 scopus 로고    scopus 로고
    • Detergent-resistant membranes should not be identified with membrane rafts
    • Lichtenberg D et al. (2005) Detergent-resistant membranes should not be identified with membrane rafts. Trends Biochem Sci 30 430-436
    • (2005) Trends Biochem Sci , vol.30 , pp. 430-436
    • Lichtenberg, D.1
  • 22
    • 33746085241 scopus 로고    scopus 로고
    • Pike LJ (2006) Rafts defined: A report on the Keystone Symposium on Lipid Rafts and Cell Function. J Lipid Res 47: 1597-1598
    • Pike LJ (2006) Rafts defined: A report on the Keystone Symposium on Lipid Rafts and Cell Function. J Lipid Res 47: 1597-1598
  • 23
    • 33745801153 scopus 로고    scopus 로고
    • Lipid rafts: Contentious only from simplistic standpoints
    • Hancock JF (2006) Lipid rafts: Contentious only from simplistic standpoints. Nat Rev Mol Cell Biol 7: 456-462
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 456-462
    • Hancock, J.F.1
  • 24
    • 0035815635 scopus 로고    scopus 로고
    • Post-translational processing of beta-secretase (β-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-β production
    • Benjannet S et al. (2001) Post-translational processing of beta-secretase (β-amyloid-converting enzyme) and its ectodomain shedding. The pro- and transmembrane/cytosolic domains affect its cellular activity and amyloid-β production. J Biol Chem 276 10879-10887
    • (2001) J Biol Chem , vol.276 , pp. 10879-10887
    • Benjannet, S.1
  • 25
    • 0035928732 scopus 로고    scopus 로고
    • Compartmentalization of β-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts
    • Riddell DR et al. (2001) Compartmentalization of β-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts. Curr Biol 11: 1288-1293
    • (2001) Curr Biol , vol.11 , pp. 1288-1293
    • Riddell, D.R.1
  • 26
    • 0141482022 scopus 로고    scopus 로고
    • Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein
    • Cordy JM et al. (2003) Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein. Proc Natl Acad Sci USA 100: 11735-11740
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11735-11740
    • Cordy, J.M.1
  • 27
    • 33748546320 scopus 로고    scopus 로고
    • BACE1 interacts with lipid raft proteins
    • Hattori C et al. (2006) BACE1 interacts with lipid raft proteins. J Neurosci Res 84: 912-917
    • (2006) J Neurosci Res , vol.84 , pp. 912-917
    • Hattori, C.1
  • 28
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts
    • Ehehalt R et al. (2003) Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts. J Cell Biol 160: 113-123
    • (2003) J Cell Biol , vol.160 , pp. 113-123
    • Ehehalt, R.1
  • 29
    • 10344263931 scopus 로고    scopus 로고
    • Neuronal membrane cholesterol loss enhances amyloid peptide generation
    • Abad-Rodriguez J et al. (2004) Neuronal membrane cholesterol loss enhances amyloid peptide generation. J Cell Biol 167: 953-960
    • (2004) J Cell Biol , vol.167 , pp. 953-960
    • Abad-Rodriguez, J.1
  • 30
    • 21844448354 scopus 로고    scopus 로고
    • Spatial segregation of γ-secretase and substrates in distinct membrane domains
    • Vetrivel KS et al. (2005) Spatial segregation of γ-secretase and substrates in distinct membrane domains. J Biol Chem 280: 25892-25900
    • (2005) J Biol Chem , vol.280 , pp. 25892-25900
    • Vetrivel, K.S.1
  • 31
    • 30644466209 scopus 로고    scopus 로고
    • Membrane-lipid therapy: A new approach in molecular medicine
    • Escriba PV (2006) Membrane-lipid therapy: A new approach in molecular medicine. Trends Mol Med 12: 34-43
    • (2006) Trends Mol Med , vol.12 , pp. 34-43
    • Escriba, P.V.1
  • 32
    • 0032573572 scopus 로고    scopus 로고
    • Elevated low-density lipoprotein in Alzheimer's disease correlates with brain Aβ 1-42 levels
    • Kuo YM et al. (1998) Elevated low-density lipoprotein in Alzheimer's disease correlates with brain Aβ 1-42 levels. Biochem Biophys Res Commun 252: 711-715
    • (1998) Biochem Biophys Res Commun , vol.252 , pp. 711-715
    • Kuo, Y.M.1
  • 33
    • 0035897938 scopus 로고    scopus 로고
    • Midlife vascular risk factors and Alzheimer's disease in later life: Longitudinal, population based study
    • Kivipelto M et al. (2001) Midlife vascular risk factors and Alzheimer's disease in later life: Longitudinal, population based study. BMJ 322: 1447-1451
    • (2001) BMJ , vol.322 , pp. 1447-1451
    • Kivipelto, M.1
  • 34
    • 0034638746 scopus 로고    scopus 로고
    • Statins and the risk of dementia
    • Jick H et al. (2000) Statins and the risk of dementia. Lancet 356: 1627-1631
    • (2000) Lancet , vol.356 , pp. 1627-1631
    • Jick, H.1
  • 35
    • 0033772113 scopus 로고    scopus 로고
    • Decreased prevalence of Alzheimer disease associated with 3-hydroxy-3-methyglutaryl coenzyme A reductase inhibitors
    • Wolozin B et al. (2000) Decreased prevalence of Alzheimer disease associated with 3-hydroxy-3-methyglutaryl coenzyme A reductase inhibitors. Arch Neurol 57: 1439-1443
    • (2000) Arch Neurol , vol.57 , pp. 1439-1443
    • Wolozin, B.1
  • 36
    • 0028177562 scopus 로고
    • Induction of Alzheimer-like β-amyloid immunoreactivity in the brains of rabbits with dietary cholesterol
    • Sparks DL et al. (1994) Induction of Alzheimer-like β-amyloid immunoreactivity in the brains of rabbits with dietary cholesterol. Exp Neurol 126: 88-94
    • (1994) Exp Neurol , vol.126 , pp. 88-94
    • Sparks, D.L.1
  • 37
    • 0032568552 scopus 로고    scopus 로고
    • Cholesterol depletion inhibits the generation of β-amyloid in hippocampal neurons
    • Simons M et al. (1998) Cholesterol depletion inhibits the generation of β-amyloid in hippocampal neurons. Proc Natl Acad Sci USA 95: 6460-6464
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 6460-6464
    • Simons, M.1
  • 38
    • 0001504829 scopus 로고    scopus 로고
    • Simvastatin strongly reduces levels of Alzheimer's disease β-amyloid peptides Aβ42 and Aβ40 in vitro and in vivo
    • Fassbender K et al. (2001) Simvastatin strongly reduces levels of Alzheimer's disease β-amyloid peptides Aβ42 and Aβ40 in vitro and in vivo. Proc Natl Acad Sci USA 98: 5856-5861
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5856-5861
    • Fassbender, K.1
  • 39
    • 0033833354 scopus 로고    scopus 로고
    • Hypercholesterolemia accelerates the Alzheimer's amyloid pathology in a transgenic mouse model
    • Refolo LM et al. (2000) Hypercholesterolemia accelerates the Alzheimer's amyloid pathology in a transgenic mouse model. Neurobiol Dis 7: 321-331
    • (2000) Neurobiol Dis , vol.7 , pp. 321-331
    • Refolo, L.M.1
  • 40
    • 0035160066 scopus 로고    scopus 로고
    • A cholesterol-lowering drug reduces β-amyloid pathology in a transgenic mouse model of Alzheimer's disease
    • Refolo LM et al. (2001) A cholesterol-lowering drug reduces β-amyloid pathology in a transgenic mouse model of Alzheimer's disease. Neurobiol Dis 8: 890-899
    • (2001) Neurobiol Dis , vol.8 , pp. 890-899
    • Refolo, L.M.1
  • 41
    • 29444432498 scopus 로고    scopus 로고
    • Can statin therapy really reduce the risk of Alzheimer's disease and slow its progression?
    • Miida T et al. (2005) Can statin therapy really reduce the risk of Alzheimer's disease and slow its progression? Curr Opin Lipidol 16: 619-623
    • (2005) Curr Opin Lipidol , vol.16 , pp. 619-623
    • Miida, T.1
  • 42
    • 33947593576 scopus 로고    scopus 로고
    • Alzheimer disease - no target for statin treatment: A mini review
    • Hoyer S et al. (2007) Alzheimer disease - no target for statin treatment: A mini review. Neurochem Res 32: 695-706
    • (2007) Neurochem Res , vol.32 , pp. 695-706
    • Hoyer, S.1
  • 43
    • 33947589524 scopus 로고    scopus 로고
    • Alzheimer's disease and cholesterol: The fat connection
    • Canevari L et al. (2007) Alzheimer's disease and cholesterol: The fat connection. Neurochem Res 32: 739-750
    • (2007) Neurochem Res , vol.32 , pp. 739-750
    • Canevari, L.1
  • 44
    • 33745759330 scopus 로고    scopus 로고
    • Re-assessing the relationship between cholesterol, statins and Alzheimer's disease
    • Wolozin B et al. (2006) Re-assessing the relationship between cholesterol, statins and Alzheimer's disease. Acta Neurol Scand Suppl 185: 63-70
    • (2006) Acta Neurol Scand Suppl , vol.185 , pp. 63-70
    • Wolozin, B.1
  • 45
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10
    • Kojro E et al. (2001) Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the α-secretase ADAM 10. Proc Natl Acad Sci USA 98: 5815-5820
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 5815-5820
    • Kojro, E.1
  • 46
    • 0034681410 scopus 로고    scopus 로고
    • Cholesterol depletion of enterocytes: Effect on the Golgi complex and apical membrane trafficking
    • Hansen GH et al. (2000) Cholesterol depletion of enterocytes: effect on the Golgi complex and apical membrane trafficking. J Biol Chem 275: 5136-5142
    • (2000) J Biol Chem , vol.275 , pp. 5136-5142
    • Hansen, G.H.1
  • 47
    • 1842639444 scopus 로고    scopus 로고
    • Effects of cholesterol depletion and increased lipid unsaturation on the properties of endocytic membranes
    • Hao M et al. (2004) Effects of cholesterol depletion and increased lipid unsaturation on the properties of endocytic membranes. J Biol Chem 279: 14171-14178
    • (2004) J Biol Chem , vol.279 , pp. 14171-14178
    • Hao, M.1
  • 48
    • 0037333737 scopus 로고    scopus 로고
    • Statin effects on cholesterol micro-domains in brain plasma membranes
    • Kirsch C et al. (2003) Statin effects on cholesterol micro-domains in brain plasma membranes. Biochem Pharmacol 65: 843-856
    • (2003) Biochem Pharmacol , vol.65 , pp. 843-856
    • Kirsch, C.1
  • 49
    • 0036523031 scopus 로고    scopus 로고
    • Inhibition of intracellular cholesterol transport alters presenilin localization and amyloid precursor protein processing in neuronal cells
    • Runz H et al. (2002) Inhibition of intracellular cholesterol transport alters presenilin localization and amyloid precursor protein processing in neuronal cells. J Neurosci 22: 1679-1689
    • (2002) J Neurosci , vol.22 , pp. 1679-1689
    • Runz, H.1
  • 50
    • 0042346382 scopus 로고    scopus 로고
    • Expression of liver X receptor target genes decreases cellular amyloid β peptide secretion
    • Sun Y et al. (2003) Expression of liver X receptor target genes decreases cellular amyloid β peptide secretion. J Biol Chem 278: 27688-27694
    • (2003) J Biol Chem , vol.278 , pp. 27688-27694
    • Sun, Y.1
  • 51
    • 0034795651 scopus 로고    scopus 로고
    • Acyl-coenzyme A: Cholesterol acyltransferase modulates the generation of the amyloid β-peptide
    • Puglielli L et al. (2001) Acyl-coenzyme A: Cholesterol acyltransferase modulates the generation of the amyloid β-peptide. Nat Cell Biol 3: 905-912
    • (2001) Nat Cell Biol , vol.3 , pp. 905-912
    • Puglielli, L.1
  • 52
    • 21444445440 scopus 로고    scopus 로고
    • Statins cause intracellular accumulation of amylold precursor protein, β-secretase-cleaved fragments, and amyloid β-peptide via an isoprenoid-dependent mechanism
    • Cole SL et al. (2005) Statins cause intracellular accumulation of amylold precursor protein, β-secretase-cleaved fragments, and amyloid β-peptide via an isoprenoid-dependent mechanism. J Biol Chem 280: 18755-18770
    • (2005) J Biol Chem , vol.280 , pp. 18755-18770
    • Cole, S.L.1
  • 53
    • 1642482817 scopus 로고    scopus 로고
    • Modulation of amyloid precursor protein cleavage by cellular sphingolipids
    • Sawamura N et al. (2004) Modulation of amyloid precursor protein cleavage by cellular sphingolipids. J Biol Chem 279: 11984-11991
    • (2004) J Biol Chem , vol.279 , pp. 11984-11991
    • Sawamura, N.1
  • 54
    • 28644451007 scopus 로고    scopus 로고
    • Regulation of cholesterol and sphingomyelin metabolism by amyloid-β and presenilin
    • Grimm MO et al. (2005) Regulation of cholesterol and sphingomyelin metabolism by amyloid-β and presenilin. Nat Cell Biol 7: 1118-1123
    • (2005) Nat Cell Biol , vol.7 , pp. 1118-1123
    • Grimm, M.O.1
  • 55
    • 3543099503 scopus 로고    scopus 로고
    • Palmitoylation of intracellular signaling proteins: Regulation and function
    • Smotrys JE et al. (2004) Palmitoylation of intracellular signaling proteins: Regulation and function. Annu Rev Biochem 73: 559-587
    • (2004) Annu Rev Biochem , vol.73 , pp. 559-587
    • Smotrys, J.E.1
  • 56
    • 0030804183 scopus 로고    scopus 로고
    • Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain
    • Scheiffele P et al. (1997) Interaction of influenza virus haemagglutinin with sphingolipid-cholesterol membrane domains via its transmembrane domain. EMBO J 16: 5501-5508
    • (1997) EMBO J , vol.16 , pp. 5501-5508
    • Scheiffele, P.1
  • 57
    • 0033103887 scopus 로고    scopus 로고
    • EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains
    • Bruckner K et al. (1999) EphrinB ligands recruit GRIP family PDZ adaptor proteins into raft membrane microdomains. Neuron 22: 511-524
    • (1999) Neuron , vol.22 , pp. 511-524
    • Bruckner, K.1
  • 58
    • 17844362751 scopus 로고    scopus 로고
    • Post-translational processing of beta-secretase in Alzheimer's disease
    • Sidera C et al. (2005) Post-translational processing of beta-secretase in Alzheimer's disease. Proteomics 5: 1533-1543
    • (2005) Proteomics , vol.5 , pp. 1533-1543
    • Sidera, C.1
  • 59
    • 31444454174 scopus 로고    scopus 로고
    • The role of seladin-1/DHCR24 in cholesterol biosynthesis, APP processing and Aβ generation in vivo
    • Crameri A et al. (2006) The role of seladin-1/DHCR24 in cholesterol biosynthesis, APP processing and Aβ generation in vivo. EMBO J 25: 432-443
    • (2006) EMBO J , vol.25 , pp. 432-443
    • Crameri, A.1


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