메뉴 건너뛰기




Volumn 20, Issue 2, 2006, Pages 105-119

Neuroproteases in peptide neurotransmission and neurodegenerative diseases: Applications to drug discovery research

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; BRAIN PEPTIDE; CA 074; CATHEPSIN B; CATHEPSIN B INHIBTOR; CATHEPSIN L; CHOLINESTERASE INHIBITOR; CORTICOTROPIN; CORTICOTROPIN RELEASING FACTOR; CYSTEINE PROTEINASE; CYSTEINE PROTEINASE INHIBITOR; DYNORPHIN; ENDORPHIN; ENKEPHALIN; FURIN; GALANIN; HUNTINGTIN; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE INHIBITOR; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; NEUROPEPTIDE; NEUROPEPTIDE Y; NEUROTRANSMITTER; NONSTEROID ANTIINFLAMMATORY AGENT; PARKIN; PROTEINASE; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SOMATOSTATIN; SUBTILISIN; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 33646261849     PISSN: 11738804     EISSN: 11738804     Source Type: Journal    
DOI: 10.2165/00063030-200620020-00005     Document Type: Review
Times cited : (12)

References (127)
  • 1
    • 0028569521 scopus 로고
    • Proteases and the emerging role of protease inhibitors in prohormone processing
    • Hook VY, Azaryan AV, Hwang SR, et al. Proteases and the emerging role of protease inhibitors in prohormone processing. FASEB J 1994; 8: 1269-78
    • (1994) FASEB J , vol.8 , pp. 1269-1278
    • Hook, V.Y.1    Azaryan, A.V.2    Hwang, S.R.3
  • 2
    • 0033597852 scopus 로고    scopus 로고
    • Proteolytic processing in the secretory pathway
    • Zhou A, Webb G, Zhu X, et al. Proteolytic processing in the secretory pathway. J Biol Chem 1999; 274: 20745-8
    • (1999) J Biol Chem , vol.274 , pp. 20745-20748
    • Zhou, A.1    Webb, G.2    Zhu, X.3
  • 3
    • 0038394566 scopus 로고    scopus 로고
    • Precursor convertases in the secretory pathway, cytosol and extracellular milieu
    • Seidah NG, Prat A. Precursor convertases in the secretory pathway, cytosol and extracellular milieu. Essays Biochem 2002; 38: 79-94
    • (2002) Essays Biochem , vol.38 , pp. 79-94
    • Seidah, N.G.1    Prat, A.2
  • 5
    • 0032698746 scopus 로고    scopus 로고
    • Alzheimer's disease: Perspectives for the new millennium
    • Sisodia SS. Alzheimer's disease: perspectives for the new millennium. J Clin Invest 1999; 104: 1169-70
    • (1999) J Clin Invest , vol.104 , pp. 1169-1170
    • Sisodia, S.S.1
  • 6
    • 0035066332 scopus 로고    scopus 로고
    • Alzheimer's disease: Genes, proteins, therapy
    • Selkoe DJ. Alzheimer's disease: genes, proteins, therapy. Physiol Rev 2001; 81: 741-61
    • (2001) Physiol Rev , vol.81 , pp. 741-761
    • Selkoe, D.J.1
  • 7
    • 0242330363 scopus 로고    scopus 로고
    • Cysteine proteases are the major β-secretase in the regulated secretory pathway that provides most of the β-amyloid in Alzheimer's disease: Role of BACE 1 in the constitutive secretory pathway
    • Hook VYH, Reisine TD. Cysteine proteases are the major β-secretase in the regulated secretory pathway that provides most of the β-amyloid in Alzheimer's disease: role of BACE 1 in the constitutive secretory pathway. J Neurosci Res 2003; 74: 393-405
    • (2003) J Neurosci Res , vol.74 , pp. 393-405
    • Hook, V.Y.H.1    Reisine, T.D.2
  • 8
    • 0035869544 scopus 로고    scopus 로고
    • Tissue-specific proteolysis of huntingtin (htt) in human brain: Evidence of enhanced levels of N- and C-terminal htt fragments in Huntington's disease striatum
    • Mende-Mueller LM, Toneff T, Hwang S-R, et al. Tissue-specific proteolysis of huntingtin (htt) in human brain: evidence of enhanced levels of N- and C-terminal htt fragments in Huntington's disease striatum. J Neurosci 2001; 21: 1830-7
    • (2001) J Neurosci , vol.21 , pp. 1830-1837
    • Mende-Mueller, L.M.1    Toneff, T.2    Hwang, S.-R.3
  • 9
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • DiFiglia M, Sapp E, Chase KO, et al. Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 1997; 277: 1990-3
    • (1997) Science , vol.277 , pp. 1990-1993
    • DiFiglia, M.1    Sapp, E.2    Chase, K.O.3
  • 11
    • 8844220536 scopus 로고    scopus 로고
    • Huntingtin and the molecular pathogenesis of Huntington's disease. Fourth in molecular medicine review series
    • Landles C, Bates GP. Huntingtin and the molecular pathogenesis of Huntington's disease. Fourth in molecular medicine review series. EMBO Rep 2004; 5: 958-63
    • (2004) EMBO Rep , vol.5 , pp. 958-963
    • Landles, C.1    Bates, G.P.2
  • 12
    • 1642342857 scopus 로고    scopus 로고
    • Recent advances in research on Parkinson disease: Synuclein and parkin
    • Burke RE. Recent advances in research on Parkinson disease: synuclein and parkin. Neurologist 2004; 10: 75-81
    • (2004) Neurologist , vol.10 , pp. 75-81
    • Burke, R.E.1
  • 13
    • 0242363670 scopus 로고    scopus 로고
    • Molecular pathways of neurodegeneration in Parkinson's disease
    • Dawson TM, Dawson VL. Molecular pathways of neurodegeneration in Parkinson's disease. Science 2003; 302: 819-22
    • (2003) Science , vol.302 , pp. 819-822
    • Dawson, T.M.1    Dawson, V.L.2
  • 14
    • 0035959931 scopus 로고    scopus 로고
    • Parkin and the molecular pathways of Parkinson's disease
    • Giasson BI, Lee VM. Parkin and the molecular pathways of Parkinson's disease. Neuron 2001; 31: 885-8
    • (2001) Neuron , vol.31 , pp. 885-888
    • Giasson, B.I.1    Lee, V.M.2
  • 15
    • 0025035291 scopus 로고
    • Central stimulation-induced analgesia in humans: Modulation by endogenous opioid peptides
    • Richardson DE. Central stimulation-induced analgesia in humans: modulation by endogenous opioid peptides. Crit Rev Neurobiol 1990; 6: 33-7
    • (1990) Crit Rev Neurobiol , vol.6 , pp. 33-37
    • Richardson, D.E.1
  • 16
    • 0032901479 scopus 로고    scopus 로고
    • Regulation of opioid receptor activities
    • Law PY, Loh HH. Regulation of opioid receptor activities. J Pharmacol Exp Ther 1999; 289: 607-24
    • (1999) J Pharmacol Exp Ther , vol.289 , pp. 607-624
    • Law, P.Y.1    Loh, H.H.2
  • 18
    • 27944466758 scopus 로고    scopus 로고
    • Endogenous opiates and behavior: 2004
    • Dec
    • Bodnar RJ, Klein GE. Endogenous opiates and behavior: 2004. Peptides 2005 Dec; 26 (12): 2629-711
    • (2005) Peptides , vol.26 , Issue.12 , pp. 2629-2711
    • Bodnar, R.J.1    Klein, G.E.2
  • 19
    • 0031657350 scopus 로고    scopus 로고
    • Central control of feeding behavior by neuropeptide Y
    • Zimanyi IA, Fathi Z, Poindexter GS. Central control of feeding behavior by neuropeptide Y. Curr Pharm Des 1998; 4: 349-66
    • (1998) Curr Pharm Des , vol.4 , pp. 349-366
    • Zimanyi, I.A.1    Fathi, Z.2    Poindexter, G.S.3
  • 20
    • 0034117088 scopus 로고    scopus 로고
    • The role of NPY in metabolic homeostasis: Implications for obesity therapy
    • Wieland HA, Hamilton BS, Krist B, et al. The role of NPY in metabolic homeostasis: implications for obesity therapy. Expert Opin Investig Drugs 2000; 9: 1327-46
    • (2000) Expert Opin Investig Drugs , vol.9 , pp. 1327-1346
    • Wieland, H.A.1    Hamilton, B.S.2    Krist, B.3
  • 21
    • 0033782054 scopus 로고    scopus 로고
    • Neuropeptides and obesity
    • Beck B. Neuropeptides and obesity. Nutrition 2000; 16: 916-23
    • (2000) Nutrition , vol.16 , pp. 916-923
    • Beck, B.1
  • 22
    • 0025972454 scopus 로고
    • The role of neuropeptide Y in cardiovascular regulation
    • Walker P, Grouzmann E, Burnier M, et al. The role of neuropeptide Y in cardiovascular regulation. Trends Pharmacol Sci 1991; 12: 111-5
    • (1991) Trends Pharmacol Sci , vol.12 , pp. 111-115
    • Walker, P.1    Grouzmann, E.2    Burnier, M.3
  • 23
    • 0029833456 scopus 로고    scopus 로고
    • The therapeutic potential of neuropeptide Y: Analgesic, anxiolytic and antihypertensive
    • Munglani R, Hudspith MJ, Hunt SP. The therapeutic potential of neuropeptide Y: analgesic, anxiolytic and antihypertensive. Drugs 1996; 52: 371-89
    • (1996) Drugs , vol.52 , pp. 371-389
    • Munglani, R.1    Hudspith, M.J.2    Hunt, S.P.3
  • 24
    • 0035957386 scopus 로고    scopus 로고
    • Galanin transgenic mice display cognitive and neurochemical deficits characteristic of Alzheimer's disease
    • U S A
    • Steiner RA, Hohmann JG, Holmes A, et al. Galanin transgenic mice display cognitive and neurochemical deficits characteristic of Alzheimer's disease. Proc Natl Acad Sci U S A 2001; 98: 4184-9
    • (2001) Proc Natl Acad Sci , vol.98 , pp. 4184-4189
    • Steiner, R.A.1    Hohmann, J.G.2    Holmes, A.3
  • 25
    • 0342859334 scopus 로고    scopus 로고
    • Galanin and spatial learning in the rat: Evidence for a differential role for galanin in subregions of the hippocampal formation
    • Schott PA, Hokfelt T, Ogren SO. Galanin and spatial learning in the rat: evidence for a differential role for galanin in subregions of the hippocampal formation. Neuropharmacology 2000; 39: 1386-403
    • (2000) Neuropharmacology , vol.39 , pp. 1386-1403
    • Schott, P.A.1    Hokfelt, T.2    Ogren, S.O.3
  • 26
    • 0037284475 scopus 로고    scopus 로고
    • Corticotropin-releasing hormone modulators and depression
    • Holsboer F. Corticotropin-releasing hormone modulators and depression. Curr Opin Investig Drugs 2003; 4: 46-50
    • (2003) Curr Opin Investig Drugs , vol.4 , pp. 46-50
    • Holsboer, F.1
  • 27
    • 0242352560 scopus 로고    scopus 로고
    • Neuropeptide systems as novel therapeutic targets for depression and anxiety disorders
    • Holmes A, Heilig M, Rupniak NM, et al. Neuropeptide systems as novel therapeutic targets for depression and anxiety disorders. Trends Pharmacol Sci 2003; 24: 580-8
    • (2003) Trends Pharmacol Sci , vol.24 , pp. 580-588
    • Holmes, A.1    Heilig, M.2    Rupniak, N.M.3
  • 28
    • 0036000176 scopus 로고    scopus 로고
    • Role of pituitary POMC-peptides and insulin-like growth factor II in the developmental biology of the adrenal gland
    • Coulter CL, Ross JT, Owens JA, et al. Role of pituitary POMC-peptides and insulin-like growth factor II in the developmental biology of the adrenal gland. Arch Physiol Biochem 2002; 110: 99-105
    • (2002) Arch Physiol Biochem , vol.110 , pp. 99-105
    • Coulter, C.L.1    Ross, J.T.2    Owens, J.A.3
  • 29
    • 21644461218 scopus 로고    scopus 로고
    • The adrenal
    • Lin L, Achermann JC. The adrenal. Horm Res 2004; 62 Suppl. 3: 22-9
    • (2004) Horm Res , vol.62 , Issue.3 SUPPL. , pp. 22-29
    • Lin, L.1    Achermann, J.C.2
  • 30
    • 18044363076 scopus 로고    scopus 로고
    • Hypothalamic-pituitary-adrenocortical axis regulation
    • Jacobson L. Hypothalamic-pituitary-adrenocortical axis regulation. Endocrinol Metab Clin North Am 2005; 34: 271-92
    • (2005) Endocrinol Metab Clin North Am , vol.34 , pp. 271-292
    • Jacobson, L.1
  • 31
    • 0029020160 scopus 로고
    • "Prohormone thiol protease" (PTP) processing of recombinant proenkephalin
    • Schiller MR, Mende-Mueller L, Moran K, et al. "Prohormone thiol protease" (PTP) processing of recombinant proenkephalin. Biochemistry 1995, 95
    • (1995) Biochemistry , pp. 95
    • Schiller, M.R.1    Mende-Mueller, L.2    Moran, K.3
  • 32
    • 0033535927 scopus 로고    scopus 로고
    • Evidence for the proenkephalin processing enzyme prohormone thiol protease (PTP) as a multicatalytic cysteine protease complex: Activation by glutathione localized to secretory vesicles
    • Yasothornsrikul S, Aaron W, Toneff T, et al. Evidence for the proenkephalin processing enzyme prohormone thiol protease (PTP) as a multicatalytic cysteine protease complex: activation by glutathione localized to secretory vesicles. Biochemistry 1999; 38: 7421-30
    • (1999) Biochemistry , vol.38 , pp. 7421-7430
    • Yasothornsrikul, S.1    Aaron, W.2    Toneff, T.3
  • 33
    • 0042924384 scopus 로고    scopus 로고
    • Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter
    • U S A
    • Yasothornsrikul S, Greenbaum D, Medzihradszky KF, et al. Cathepsin L in secretory vesicles functions as a prohormone-processing enzyme for production of the enkephalin peptide neurotransmitter. Proc Natl Acad Sci U S A 2003; 100: 9590-5
    • (2003) Proc Natl Acad Sci , vol.100 , pp. 9590-9595
    • Yasothornsrikul, S.1    Greenbaum, D.2    Medzihradszky, K.F.3
  • 34
    • 0034615570 scopus 로고    scopus 로고
    • Lysosomal cysteine proteases: More than scavengers
    • Turk B, Turk D, Turk V. Lysosomal cysteine proteases: more than scavengers. Biochim Biophys Acta 2000; 1477: 98-111
    • (2000) Biochim Biophys Acta , vol.1477 , pp. 98-111
    • Turk, B.1    Turk, D.2    Turk, V.3
  • 35
    • 0036929283 scopus 로고    scopus 로고
    • Processing and activation of lysosomal proteinases
    • Ishidoh K, Kominami E. Processing and activation of lysosomal proteinases. Biol Chem 2002; 383: 1827-31
    • (2002) Biol Chem , vol.383 , pp. 1827-1831
    • Ishidoh, K.1    Kominami, E.2
  • 36
    • 0031995477 scopus 로고    scopus 로고
    • The proprotein convertases
    • Steiner DF. The proprotein convertases. Curr Opin Chem Biol 1998; 2: 31-9
    • (1998) Curr Opin Chem Biol , vol.2 , pp. 31-39
    • Steiner, D.F.1
  • 37
    • 12644253798 scopus 로고    scopus 로고
    • Defective prohormone processing and altered pancreatic islet morphology in mice lacking active SPC2
    • U S A
    • Furuta M, Yano H, Zhou A, et al. Defective prohormone processing and altered pancreatic islet morphology in mice lacking active SPC2. Proc Natl Acad Sci U S A 1997; 94: 6646-51
    • (1997) Proc Natl Acad Sci , vol.94 , pp. 6646-6651
    • Furuta, M.1    Yano, H.2    Zhou, A.3
  • 38
    • 0032488981 scopus 로고    scopus 로고
    • Incomplete processing of proinsulin to insulin accompanied by elevation of Des-31,32 proinsulin intermediates in islets of mice lacking active PC2
    • Furuta M, Carroll R, Martin S, et al. Incomplete processing of proinsulin to insulin accompanied by elevation of Des-31,32 proinsulin intermediates in islets of mice lacking active PC2. J Biol Chem 1998; 273: 3431-7
    • (1998) J Biol Chem , vol.273 , pp. 3431-3437
    • Furuta, M.1    Carroll, R.2    Martin, S.3
  • 39
    • 0033817874 scopus 로고    scopus 로고
    • Defective prodynorphin processing in mice lacking prohormone convertase PC2
    • Berman Y, Mzhavia N, Polonskaia A, et al. Defective prodynorphin processing in mice lacking prohormone convertase PC2. J Neurochem 2000; 75: 1763-70
    • (2000) J Neurochem , vol.75 , pp. 1763-1770
    • Berman, Y.1    Mzhavia, N.2    Polonskaia, A.3
  • 40
    • 0035882519 scopus 로고    scopus 로고
    • Altered processing of pro-orphanin FQ/nociceptin and pro-opiomelanocortin-derived peptides in the brains of mice expressing defective prohormone convertase 2
    • Allen RG, Peng B, Pellegrino MJ, et al. Altered processing of pro-orphanin FQ/nociceptin and pro-opiomelanocortin-derived peptides in the brains of mice expressing defective prohormone convertase 2. J Neurosci 2001; 21: 5864-70
    • (2001) J Neurosci , vol.21 , pp. 5864-5870
    • Allen, R.G.1    Peng, B.2    Pellegrino, M.J.3
  • 41
    • 0036678560 scopus 로고    scopus 로고
    • Altered processing of the neurotensin/neuromedin N precursor in PC2 knock down mice: A biochemical and immunohistochemical study
    • Villeneuve P, Feliciangeli S, Croissandeau G, et al. Altered processing of the neurotensin/neuromedin N precursor in PC2 knock down mice: a biochemical and immunohistochemical study. J Neurochem 2002; 82: 783-93
    • (2002) J Neurochem , vol.82 , pp. 783-793
    • Villeneuve, P.1    Feliciangeli, S.2    Croissandeau, G.3
  • 42
    • 0042532282 scopus 로고    scopus 로고
    • Selective roles for the PC2 processing enzyme in the regulation of peptide neurotransmitter levels in brain and peripheral neuroendocrine tissues of PC2 deficient mice
    • Miller R, Toneff T, Vishnuvardhan D, et al. Selective roles for the PC2 processing enzyme in the regulation of peptide neurotransmitter levels in brain and peripheral neuroendocrine tissues of PC2 deficient mice. Neuropeptides 2003; 37: 140-8
    • (2003) Neuropeptides , vol.37 , pp. 140-148
    • Miller, R.1    Toneff, T.2    Vishnuvardhan, D.3
  • 43
    • 0041302361 scopus 로고    scopus 로고
    • Obliteration of α-melanocyte-stimulating hormone derived from POMC in pituitary and brains of PC2-deficient mice
    • Miller R, Aaron W, Toneff T, et al. Obliteration of α-melanocyte-stimulating hormone derived from POMC in pituitary and brains of PC2-deficient mice. J Neurochem 2003; 86: 556-63
    • (2003) J Neurochem , vol.86 , pp. 556-563
    • Miller, R.1    Aaron, W.2    Toneff, T.3
  • 44
    • 0036679173 scopus 로고    scopus 로고
    • Disruption of PC1/3 expression in mice causes dwarfism and multiple neuroendocrine peptide processing defects
    • U S A
    • Zhu X, Zhou A, Dey A, et al. Disruption of PC1/3 expression in mice causes dwarfism and multiple neuroendocrine peptide processing defects. Proc Natl Acad Sci U S A 2002; 99: 10293-8
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 10293-10298
    • Zhu, X.1    Zhou, A.2    Dey, A.3
  • 45
    • 0036678101 scopus 로고    scopus 로고
    • Severe block in processing of proinsulin to insulin accompanied by elevation of des-64,65 proinsulin intermediates in islets of mice lacking prohormone convertase 1/3
    • U S A
    • Zhu X, Orci L, Carroll R, et al. Severe block in processing of proinsulin to insulin accompanied by elevation of des-64,65 proinsulin intermediates in islets of mice lacking prohormone convertase 1/3. Proc Natl Acad Sci U S A 2002; 99: 10299-304
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 10299-10304
    • Zhu, X.1    Orci, L.2    Carroll, R.3
  • 46
    • 1442274636 scopus 로고    scopus 로고
    • Impaired intestinal proglucagon processing in mice lacking prohormone convertase 1
    • Ugleholdt R, Zhu X, Deacon CF, et al. Impaired intestinal proglucagon processing in mice lacking prohormone convertase 1. Endocrinology 2004; 145: 1349-55
    • (2004) Endocrinology , vol.145 , pp. 1349-1355
    • Ugleholdt, R.1    Zhu, X.2    Deacon, C.F.3
  • 47
    • 1942487781 scopus 로고    scopus 로고
    • Genetic inactivation of prohormone convertase (PC1) causes a reduction in cholecystokinin (CCK) levels in the hippocampus, amygdala, pons and medulla in mouse brain that correlates with the degree of colocalization of PC1 and CCK mRNA in these structures in rat brain
    • Cain BM, Connolly K, Blum AC, et al. Genetic inactivation of prohormone convertase (PC1) causes a reduction in cholecystokinin (CCK) levels in the hippocampus, amygdala, pons and medulla in mouse brain that correlates with the degree of colocalization of PC1 and CCK mRNA in these structures in rat brain. J Neurochem 2004; 89: 307-13
    • (2004) J Neurochem , vol.89 , pp. 307-313
    • Cain, B.M.1    Connolly, K.2    Blum, A.C.3
  • 48
    • 15444366205 scopus 로고    scopus 로고
    • Neuropeptide processing profile in mice lacking prohormone convertase-1
    • Pan H, Nanno D, Che FY, et al. Neuropeptide processing profile in mice lacking prohormone convertase-1. Biochemistry 2005; 44: 4939-48
    • (2005) Biochemistry , vol.44 , pp. 4939-4948
    • Pan, H.1    Nanno, D.2    Che, F.Y.3
  • 49
    • 0036882395 scopus 로고    scopus 로고
    • Serpin structure, mechanism, and function
    • Gettins PG. Serpin structure, mechanism, and function. Chem Rev 2002; 102: 4751-804
    • (2002) Chem Rev , vol.102 , pp. 4751-4804
    • Gettins, P.G.1
  • 50
    • 0035823595 scopus 로고    scopus 로고
    • The serpins are an expanding superfamily of structurally similar but functionally diverse proteins: Evolution, mechanism of inhibition, novel functions, and a revised nomenclature
    • Silverman GA, Bird PI, Carrell RW, et al. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins: evolution, mechanism of inhibition, novel functions, and a revised nomenclature. J Biol Chem 2001; 276: 33293-6
    • (2001) J Biol Chem , vol.276 , pp. 33293-33296
    • Silverman, G.A.1    Bird, P.I.2    Carrell, R.W.3
  • 51
    • 0036789017 scopus 로고    scopus 로고
    • Serpinopathies and the conformational dementias
    • Lomas DA, Carrell RW. Serpinopathies and the conformational dementias. Nat Rev Genet 2002; 3: 759-68
    • (2002) Nat Rev Genet , vol.3 , pp. 759-768
    • Lomas, D.A.1    Carrell, R.W.2
  • 52
    • 0026728952 scopus 로고
    • Viral inhibition of inflammation: Cowpox virus encodes an inhibitor of the interleukin-1 β-converting enzyme
    • Ray CA, Black RA, Kronheim SR, et al. Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1 β-converting enzyme. Cell 1992; 69: 597-604
    • (1992) Cell , vol.69 , pp. 597-604
    • Ray, C.A.1    Black, R.A.2    Kronheim, S.R.3
  • 53
    • 12644256886 scopus 로고    scopus 로고
    • CrmA/SPI-2 inhibition of an endogenous ICE-related protease responsible for lamin A cleavage and apoptotic nuclear fragmentation
    • Takahashi A, Musy PY, Martins LM, et al. CrmA/SPI-2 inhibition of an endogenous ICE-related protease responsible for lamin A cleavage and apoptotic nuclear fragmentation. J Biol Chem 1996; 271: 32487-90
    • (1996) J Biol Chem , vol.271 , pp. 32487-32490
    • Takahashi, A.1    Musy, P.Y.2    Martins, L.M.3
  • 54
    • 0032515939 scopus 로고    scopus 로고
    • Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: A kinetic analysis
    • Schick C, Pemberton PA, Shi GP, et al. Cross-class inhibition of the cysteine proteinases cathepsins K, L, and S by the serpin squamous cell carcinoma antigen 1: a kinetic analysis. Biochemistry 1998; 37: 5258-66
    • (1998) Biochemistry , vol.37 , pp. 5258-5266
    • Schick, C.1    Pemberton, P.A.2    Shi, G.P.3
  • 55
    • 0037143531 scopus 로고    scopus 로고
    • The novel serpin endopin 2 demonstrates cross-class inhibition of papain and elastase: Localization of endopin 2 to regulated secretory vesicles of neuroendocrine chromaffin cells
    • Hwang S-R, Steineckert B, Toneff T, et al. The novel serpin endopin 2 demonstrates cross-class inhibition of papain and elastase: localization of endopin 2 to regulated secretory vesicles of neuroendocrine chromaffin cells. Biochemistry 2002; 41: 10397-405
    • (2002) Biochemistry , vol.41 , pp. 10397-10405
    • Hwang, S.-R.1    Steineckert, B.2    Toneff, T.3
  • 56
    • 19644394871 scopus 로고    scopus 로고
    • The novel bovine serpin endopin 2C demonstrates selective inhibition of the cysteine protease cathepsin L compared to the serine protease elastase, in cross-class inhibition
    • Hwang S-R, Stoka V, Turk V, et al. The novel bovine serpin endopin 2C demonstrates selective inhibition of the cysteine protease cathepsin L compared to the serine protease elastase, in cross-class inhibition. Biochemistry 2005; 44: 7757-67
    • (2005) Biochemistry , vol.44 , pp. 7757-7767
    • Hwang, S.-R.1    Stoka, V.2    Turk, V.3
  • 57
    • 11844263401 scopus 로고    scopus 로고
    • Demonstration of GTG as an alternative initiation codon for the serpin endopin 2B-2
    • Hwang S-R, Garza CZ, Wegrzyn JL, et al. Demonstration of GTG as an alternative initiation codon for the serpin endopin 2B-2. Biochem Biophys Res Commun 2005; 327: 837-44
    • (2005) Biochem Biophys Res Commun , vol.327 , pp. 837-844
    • Hwang, S.-R.1    Garza, C.Z.2    Wegrzyn, J.L.3
  • 58
    • 0036660933 scopus 로고    scopus 로고
    • Novel secretory vesicle serpins, endopin 1 and endopin 2: Endogenous protease inhibitors with distinct target protease specificities
    • Jul-Aug
    • Hook VY, Hwang SR. Novel secretory vesicle serpins, endopin 1 and endopin 2: endogenous protease inhibitors with distinct target protease specificities. Biol Chem 2002 Jul-Aug; 383 (7-8): 1067-74
    • (2002) Biol Chem , vol.383 , Issue.7-8 , pp. 1067-1074
    • Hook, V.Y.1    Hwang, S.R.2
  • 59
    • 0033607674 scopus 로고    scopus 로고
    • Molecular cloning of endopin 1, a novel serpin localized to neurosecretory vesicles of chromaffin cells: Inhibition of basic residue-cleaving proteases by endopin 1
    • Hwang S-R, Steineckert B, Yasothornsrikul S, et al. Molecular cloning of endopin 1, a novel serpin localized to neurosecretory vesicles of chromaffin cells: inhibition of basic residue-cleaving proteases by endopin 1. J Biol Chem 1999; 274: 34164-73
    • (1999) J Biol Chem , vol.274 , pp. 34164-34173
    • Hwang, S.-R.1    Steineckert, B.2    Yasothornsrikul, S.3
  • 60
    • 0029022254 scopus 로고
    • Enzymatic characterization of immunopurified prohormone convertase 2: Potent inhibition by a 7B2 peptide fragment
    • Lindberg I, van den Hurk WH, Bui C, et al. Enzymatic characterization of immunopurified prohormone convertase 2: potent inhibition by a 7B2 peptide fragment. Biochemistry 1995; 34: 5486-93
    • (1995) Biochemistry , vol.34 , pp. 5486-5493
    • Lindberg, I.1    Van Den Hurk, W.H.2    Bui, C.3
  • 61
    • 0032819395 scopus 로고    scopus 로고
    • The role of the 7B2 CT peptide in the inhibition of prohormone convertase 2 in endocrine cell lines
    • Fortenberry Y, Liu J, Lindberg I. The role of the 7B2 CT peptide in the inhibition of prohormone convertase 2 in endocrine cell lines. J Neurochem 1999; 73: 994-1003
    • (1999) J Neurochem , vol.73 , pp. 994-1003
    • Fortenberry, Y.1    Liu, J.2    Lindberg, I.3
  • 62
    • 0034640505 scopus 로고    scopus 로고
    • The SAAS granin exhibits structural and functional homology to 7B2 and contains a highly potent hexapeptide inhibitor of PC1
    • Cameron A, Fortenberry Y, Lindberg I. The SAAS granin exhibits structural and functional homology to 7B2 and contains a highly potent hexapeptide inhibitor of PC1. FEBS Lett 2000; 473: 135-8
    • (2000) FEBS Lett , vol.473 , pp. 135-138
    • Cameron, A.1    Fortenberry, Y.2    Lindberg, I.3
  • 63
    • 0035980127 scopus 로고    scopus 로고
    • Inhibitory specificity and potency of proSAAS-derived peptides toward proprotein convertase 1
    • Basak A, Koch P, Dupelle M, et al. Inhibitory specificity and potency of proSAAS-derived peptides toward proprotein convertase 1. J Biol Chem 2001; 276: 32720-8
    • (2001) J Biol Chem , vol.276 , pp. 32720-32728
    • Basak, A.1    Koch, P.2    Dupelle, M.3
  • 64
    • 0025916877 scopus 로고
    • Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway
    • Hosaka M, Nagahama M, Kim WS, et al. Arg-X-Lys/Arg-Arg motif as a signal for precursor cleavage catalyzed by furin within the constitutive secretory pathway. J Biol Chem 1991; 266: 12127-30
    • (1991) J Biol Chem , vol.266 , pp. 12127-12130
    • Hosaka, M.1    Nagahama, M.2    Kim, W.S.3
  • 65
    • 0031994695 scopus 로고    scopus 로고
    • Subtilisin-related serine proteases in the mammalian constitutive secretory pathway
    • Gensberg K, Jan S, Matthews GM. Subtilisin-related serine proteases in the mammalian constitutive secretory pathway. Semin Cell Dev Biol 1998; 9: 11-7
    • (1998) Semin Cell Dev Biol , vol.9 , pp. 11-17
    • Gensberg, K.1    Jan, S.2    Matthews, G.M.3
  • 66
    • 0036312990 scopus 로고    scopus 로고
    • β-amyloid peptide in regulated secretory vesicles of chromaffin cells: Evidence for multiple cysteine proteolytic activities in distinct pathways for β-secretase activity in chromaffin vesicles
    • Hook VYH, Toneff T, Aaron W, et al. β-amyloid peptide in regulated secretory vesicles of chromaffin cells: evidence for multiple cysteine proteolytic activities in distinct pathways for β-secretase activity in chromaffin vesicles. J Neurochem 2002; 81: 237-56
    • (2002) J Neurochem , vol.81 , pp. 237-256
    • Hook, V.Y.H.1    Toneff, T.2    Aaron, W.3
  • 67
    • 26844559355 scopus 로고    scopus 로고
    • Inhibition of cathepsin B reduces β-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: Evidence for cathepsin B as a candidate β-secretase of Alzheimer's disease
    • Hook V, Toneff T, Bogyo M, et al. Inhibition of cathepsin B reduces β-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: evidence for cathepsin B as a candidate β-secretase of Alzheimer's disease. Biol Chem 2005; 386: 931-40
    • (2005) Biol Chem , vol.386 , pp. 931-940
    • Hook, V.1    Toneff, T.2    Bogyo, M.3
  • 68
    • 0033037118 scopus 로고    scopus 로고
    • Structural basis of inhibition of cysteine proteases by E-64 and its derivatives
    • Matsumoto K, Mizoue K, Kitamura K, et al. Structural basis of inhibition of cysteine proteases by E-64 and its derivatives. Biopolymers 1999; 51: 99-107
    • (1999) Biopolymers , vol.51 , pp. 99-107
    • Matsumoto, K.1    Mizoue, K.2    Kitamura, K.3
  • 69
    • 0030961306 scopus 로고    scopus 로고
    • Binding mode of CA074, a specific irreversible inhibitor, to bovine cathepsin B as determined by X-ray crystal analysis of the complex
    • Yamamoto A, Hara T, Tomoo K, et al. Binding mode of CA074, a specific irreversible inhibitor, to bovine cathepsin B as determined by X-ray crystal analysis of the complex. J Biochem 1997; 121: 974-7
    • (1997) J Biochem , vol.121 , pp. 974-977
    • Yamamoto, A.1    Hara, T.2    Tomoo, K.3
  • 70
    • 0027053210 scopus 로고
    • CA074 methyl ester: A proinhibitor for intracellular cathepsin B
    • Buttle DJ, Murata M, Knight CG, et al. CA074 methyl ester: a proinhibitor for intracellular cathepsin B. Arch Biochem Biophys 1992; 299: 377-80
    • (1992) Arch Biochem Biophys , vol.299 , pp. 377-380
    • Buttle, D.J.1    Murata, M.2    Knight, C.G.3
  • 71
    • 0033382226 scopus 로고    scopus 로고
    • Identification of a novel aspartic protease (Asp 2) as β-Secretase
    • Hussain I, Powell D, Howlett DR, et al. Identification of a novel aspartic protease (Asp 2) as β-Secretase. Mol Cell Neurosci 1999; 14: 419-27
    • (1999) Mol Cell Neurosci , vol.14 , pp. 419-427
    • Hussain, I.1    Powell, D.2    Howlett, D.R.3
  • 72
    • 0033518251 scopus 로고    scopus 로고
    • Purification and cloning of amyloid precursor protein β-secretase from human brain
    • Sinha S, Anderson JP, Barbour R, et al. Purification and cloning of amyloid precursor protein β-secretase from human brain. Nature 1999; 402: 537-40
    • (1999) Nature , vol.402 , pp. 537-540
    • Sinha, S.1    Anderson, J.P.2    Barbour, R.3
  • 73
    • 0033595706 scopus 로고    scopus 로고
    • β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar R, Bennet BD, Babu-Khan S, et al. β-secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 1999; 286: 735-41
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1    Bennet, B.D.2    Babu-Khan, S.3
  • 74
    • 0033518264 scopus 로고    scopus 로고
    • Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity
    • Yan R, Bienkowski MJ, Shuck ME, et al. Membrane-anchored aspartyl protease with Alzheimer's disease β-secretase activity. Nature 1999; 402: 533-7
    • (1999) Nature , vol.402 , pp. 533-537
    • Yan, R.1    Bienkowski, M.J.2    Shuck, M.E.3
  • 75
    • 0034652309 scopus 로고    scopus 로고
    • Human aspartic protease memapsin 2 cleaves the β-secretase site of β-amyloid precursor protein
    • U S A
    • Lin X, Koelsch G, Wu S, et al. Human aspartic protease memapsin 2 cleaves the β-secretase site of β-amyloid precursor protein. Proc Natl Acad Sci U S A 2000; 97: 1456-60
    • (2000) Proc Natl Acad Sci , vol.97 , pp. 1456-1460
    • Lin, X.1    Koelsch, G.2    Wu, S.3
  • 76
    • 0032516003 scopus 로고    scopus 로고
    • Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation
    • U S A
    • Deussing J, Roth W, Saftig P, et al. Cathepsins B and D are dispensable for major histocompatibility complex class II-mediated antigen presentation. Proc Natl Acad Sci U S A 1998; 95: 4516-21
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 4516-4521
    • Deussing, J.1    Roth, W.2    Saftig, P.3
  • 77
    • 0042744006 scopus 로고    scopus 로고
    • Cathepsin B inactivation attenuates hepatic injury and fibrosis during cholestasis
    • Canbay A, Guicciardi ME, Higuchi H, et al. Cathepsin B inactivation attenuates hepatic injury and fibrosis during cholestasis. J Clin Invest 2003; 112: 152-9
    • (2003) J Clin Invest , vol.112 , pp. 152-159
    • Canbay, A.1    Guicciardi, M.E.2    Higuchi, H.3
  • 78
    • 0035180207 scopus 로고    scopus 로고
    • Cathepsin B knockout mice are resistant to tumor necrosis factor-α-mediated hepatocyte apoptosis and liver injury
    • Guicciardi ME, Miyoshi H, Bronk SF, et al. Cathepsin B knockout mice are resistant to tumor necrosis factor-α-mediated hepatocyte apoptosis and liver injury. Am J Pathol 2001; 159: 2045-54
    • (2001) Am J Pathol , vol.159 , pp. 2045-2054
    • Guicciardi, M.E.1    Miyoshi, H.2    Bronk, S.F.3
  • 79
    • 0033795691 scopus 로고    scopus 로고
    • Role of cathepsin B in intracellular trypsinogen activation and the onset of acute pancreatitis
    • Halangk W, Lerch MM, Brandt-Nedelev B, et al. Role of cathepsin B in intracellular trypsinogen activation and the onset of acute pancreatitis. J Clin Invest 2000; 106: 773-81
    • (2000) J Clin Invest , vol.106 , pp. 773-781
    • Halangk, W.1    Lerch, M.M.2    Brandt-Nedelev, B.3
  • 80
    • 0036813533 scopus 로고    scopus 로고
    • Regulation of amyloid β-peptide levels by enzymatic degradation
    • Mukerjee A, Hersh LB. Regulation of amyloid β-peptide levels by enzymatic degradation. J Alzheimers Dis 2002; 4: 341-8
    • (2002) J Alzheimers Dis , vol.4 , pp. 341-348
    • Mukerjee, A.1    Hersh, L.B.2
  • 81
    • 0348010388 scopus 로고    scopus 로고
    • Substrate activation of insulin-degrading enzyme (insulysin): A potential target for drug development
    • Song E-S, Juliano MA, Juliano L, et al. Substrate activation of insulin-degrading enzyme (insulysin): a potential target for drug development. J Biol Chem 2003; 278: 49789-94
    • (2003) J Biol Chem , vol.278 , pp. 49789-49794
    • Song, E.-S.1    Juliano, M.A.2    Juliano, L.3
  • 82
    • 28544451677 scopus 로고    scopus 로고
    • Design, synthesis, and biological evaluation of dual binding site acetylcholinesterase inhibitors: New disease-modifying agents for Alzheimer's disease
    • Muñoz-Ruiz P, Rubio L, García-Palomero E, et al. Design, synthesis, and biological evaluation of dual binding site acetylcholinesterase inhibitors: new disease-modifying agents for Alzheimer's disease. J Med Chem 2005; 48: 7223-33
    • (2005) J Med Chem , vol.48 , pp. 7223-7233
    • Muñoz-Ruiz, P.1    Rubio, L.2    García-Palomero, E.3
  • 83
    • 19944363180 scopus 로고    scopus 로고
    • The role of COX-1 and COX-2 in Alzheimer's disease pathology and the therapeutic potentials of non-steroidal anti-inflammatory drugs
    • Hoozemans JJM, O'Banion MK. The role of COX-1 and COX-2 in Alzheimer's disease pathology and the therapeutic potentials of non-steroidal anti-inflammatory drugs. Curr Drug Targets CNS Neurol Disord 2005; 4: 307-15
    • (2005) Curr Drug Targets CNS Neurol Disord , vol.4 , pp. 307-315
    • Hoozemans, J.J.M.1    O'Banion, M.K.2
  • 84
    • 0038458980 scopus 로고    scopus 로고
    • Statins as potential therapeutic agents in neuroinflammatory disorders
    • Stuve O, Youssef S, Steinman L, et al. Statins as potential therapeutic agents in neuroinflammatory disorders. Curr Opin Neurol 2003; 16: 393-401
    • (2003) Curr Opin Neurol , vol.16 , pp. 393-401
    • Stuve, O.1    Youssef, S.2    Steinman, L.3
  • 86
    • 0642309508 scopus 로고    scopus 로고
    • Potential use of estrogen-like drugs for the prevention of Alzheimer's disease
    • Smith JD, Levin-Allerhand JA. Potential use of estrogen-like drugs for the prevention of Alzheimer's disease. J Mol Neurosci 2003; 20: 277-82
    • (2003) J Mol Neurosci , vol.20 , pp. 277-282
    • Smith, J.D.1    Levin-Allerhand, J.A.2
  • 87
    • 20844460621 scopus 로고    scopus 로고
    • The molecular basis of memantine action in Alzheimer's disease and other neurologic disorders: Low-affinity, uncompetitive antagonism
    • Lipton SA. The molecular basis of memantine action in Alzheimer's disease and other neurologic disorders: low-affinity, uncompetitive antagonism. Curr Alzheimer Res 2005; 2: 155-65
    • (2005) Curr Alzheimer Res , vol.2 , pp. 155-165
    • Lipton, S.A.1
  • 88
    • 0027480960 scopus 로고
    • A novel gene containing a trinucleotide repeat that is expanded on Huntington's disease chromosomes
    • MacDonald ME, Ambrose CM, Duyao MP, et al. A novel gene containing a trinucleotide repeat that is expanded on Huntington's disease chromosomes. Cell 1993; 72: 971-83
    • (1993) Cell , vol.72 , pp. 971-983
    • MacDonald, M.E.1    Ambrose, C.M.2    Duyao, M.P.3
  • 89
    • 0030826134 scopus 로고    scopus 로고
    • Homozygotes and heterozygotes for ciliary neurotrophic factor null alleles do not show earlier onset of Huntington's disease
    • Rubinsztein DC, Leggo J, Chiano M, et al. Homozygotes and heterozygotes for ciliary neurotrophic factor null alleles do not show earlier onset of Huntington's disease. Neurology 1997; 49: 890-2
    • (1997) Neurology , vol.49 , pp. 890-892
    • Rubinsztein, D.C.1    Leggo, J.2    Chiano, M.3
  • 90
    • 0030866538 scopus 로고    scopus 로고
    • Transgenic models of Huntington's disease
    • Bates GP, Mangiarini L, Mahal A, et al. Transgenic models of Huntington's disease. Hum Mol Genet 1997; 6: 1633-7
    • (1997) Hum Mol Genet , vol.6 , pp. 1633-1637
    • Bates, G.P.1    Mangiarini, L.2    Mahal, A.3
  • 91
    • 18544410106 scopus 로고    scopus 로고
    • Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic of the HD mutation
    • Davies SW, Turmaine M, Cozens BA, et al. Formation of neuronal intranuclear inclusions underlies the neurological dysfunction in mice transgenic of the HD mutation. Cell 1997; 90: 537-48
    • (1997) Cell , vol.90 , pp. 537-548
    • Davies, S.W.1    Turmaine, M.2    Cozens, B.A.3
  • 92
    • 0033560924 scopus 로고    scopus 로고
    • Characterization of progressive motor deficits in mice transgenic for the human Huntington's disease mutation
    • Carter RJ, Lione LA, Humby T, et al. Characterization of progressive motor deficits in mice transgenic for the human Huntington's disease mutation. J Neurosci 1999; 19: 3248-57
    • (1999) J Neurosci , vol.19 , pp. 3248-3257
    • Carter, R.J.1    Lione, L.A.2    Humby, T.3
  • 93
    • 0033136692 scopus 로고    scopus 로고
    • A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration
    • Hodgson JG, Agopyan N, Gutekunst CA, et al. A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration. Neuron 1999; 23: 181-92
    • (1999) Neuron , vol.23 , pp. 181-192
    • Hodgson, J.G.1    Agopyan, N.2    Gutekunst, C.A.3
  • 94
    • 0037333666 scopus 로고    scopus 로고
    • Staging of brain pathology related to sporadic Parkinson's disease
    • Braak H, Del Tredici K, Rüb U, et al. Staging of brain pathology related to sporadic Parkinson's disease. Neurobiol Aging 2003; 24: 197-211
    • (2003) Neurobiol Aging , vol.24 , pp. 197-211
    • Braak, H.1    Del Tredici, K.2    Rüb, U.3
  • 95
  • 96
    • 0031668101 scopus 로고    scopus 로고
    • Genetic dissection of familial Parkinson's disease
    • Riess O, Jakes R, Kruger R. Genetic dissection of familial Parkinson's disease. Mol Med Today 1998; 4310: 438-44
    • (1998) Mol Med Today , vol.4310 , pp. 438-444
    • Riess, O.1    Jakes, R.2    Kruger, R.3
  • 97
    • 0032568534 scopus 로고    scopus 로고
    • α-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies
    • U S A
    • Spillantini MG, Crowther RA, Jakes R, et al. α-synuclein in filamentous inclusions of Lewy bodies from Parkinson's disease and dementia with Lewy bodies. Proc Natl Acad Sci U S A 1998; 95: 6469-73
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 6469-6473
    • Spillantini, M.G.1    Crowther, R.A.2    Jakes, R.3
  • 98
    • 0032545154 scopus 로고    scopus 로고
    • Degenerative terminals of the perforant pathway are human α-synuclein-immunoreactive in the hippocampus of patients with diffuse Lewy body disease
    • Iseki E, Marui W, Kosaka K, et al. Degenerative terminals of the perforant pathway are human α-synuclein-immunoreactive in the hippocampus of patients with diffuse Lewy body disease. Neurosci Lett 1998; 258: 81-4
    • (1998) Neurosci Lett , vol.258 , pp. 81-84
    • Iseki, E.1    Marui, W.2    Kosaka, K.3
  • 99
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the α-synuclein gene identified in families with Parkinson's disease
    • Polymeropoulos MH, Lavedan C, Leroy E, et al. Mutation in the α-synuclein gene identified in families with Parkinson's disease. Science 1997; 276: 2045-7
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3
  • 100
    • 0031990490 scopus 로고    scopus 로고
    • Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease
    • Kruger R, Kuhn W, Muller T, et al. Ala30Pro mutation in the gene encoding α-synuclein in Parkinson's disease. Nat Genet 1998; 18: 106-8
    • (1998) Nat Genet , vol.18 , pp. 106-108
    • Kruger, R.1    Kuhn, W.2    Muller, T.3
  • 101
    • 0027489773 scopus 로고
    • Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease
    • U S A
    • Ueda K, Fukushima HJ, Masliah E, et al. Molecular cloning of cDNA encoding an unrecognized component of amyloid in Alzheimer disease. Proc Natl Acad Sci U S A 1993; 90: 11282-6
    • (1993) Proc Natl Acad Sci , vol.90 , pp. 11282-11286
    • Ueda, K.1    Fukushima, H.J.2    Masliah, E.3
  • 102
    • 0028984925 scopus 로고
    • Non-Aβ component of Alzheimer's disease amyloid (NAC) is amyloidogenic
    • Iwai A, Yoshimoto M, Masliah E, et al. Non-Aβ component of Alzheimer's disease amyloid (NAC) is amyloidogenic. Biochemistry 1995; 34: 10139-45
    • (1995) Biochemistry , vol.34 , pp. 10139-10145
    • Iwai, A.1    Yoshimoto, M.2    Masliah, E.3
  • 103
    • 0029056115 scopus 로고
    • NACP, the precursor protein of the non-amyloid β/A4 protein (Aβ) component of Alzheimer disease amyloid, binds Aβ and stimulates Aβ aggregation
    • U S A
    • Yoshimoto M, Iwai A, Kang D, et al. NACP, the precursor protein of the non-amyloid β/A4 protein (Aβ) component of Alzheimer disease amyloid, binds Aβ and stimulates Aβ aggregation. Proc Natl Acad Sci U S A 1995; 92: 9141-5
    • (1995) Proc Natl Acad Sci , vol.92 , pp. 9141-9145
    • Yoshimoto, M.1    Iwai, A.2    Kang, D.3
  • 104
    • 0030025635 scopus 로고    scopus 로고
    • Altered presynaptic protein NACP is associated with plaque formation and neurodegeneration in Alzheimer's disease
    • Masliah E, Iwai A, Mallory M, et al. Altered presynaptic protein NACP is associated with plaque formation and neurodegeneration in Alzheimer's disease. Am J Pathol 1996; 148: 201-10
    • (1996) Am J Pathol , vol.148 , pp. 201-210
    • Masliah, E.1    Iwai, A.2    Mallory, M.3
  • 105
    • 0032102455 scopus 로고    scopus 로고
    • The synucleins: A family of proteins involved in synaptic function, plasticity, neurodegeneration and disease
    • Clayton DF, George JM. The synucleins: a family of proteins involved in synaptic function, plasticity, neurodegeneration and disease. Trends Neurosci 1998; 21: 249-54
    • (1998) Trends Neurosci , vol.21 , pp. 249-254
    • Clayton, D.F.1    George, J.M.2
  • 106
    • 0031705984 scopus 로고    scopus 로고
    • Identification, localization, and characterization of the human γ-synuclein gene
    • Lavedan C, Leroy E, Dehejia A, et al. Identification, localization, and characterization of the human γ-synuclein gene. Hum Genet 1998; 103: 106-12
    • (1998) Hum Genet , vol.103 , pp. 106-112
    • Lavedan, C.1    Leroy, E.2    Dehejia, A.3
  • 107
    • 0037137702 scopus 로고    scopus 로고
    • Parkin protects against the toxicity associated with mutant α-synuclein: Proteasome dysfunction selectively affects catecholaminergic neurons
    • Petrucelli L, O'Farrell C, Lockhart PJ, et al. Parkin protects against the toxicity associated with mutant α-synuclein: proteasome dysfunction selectively affects catecholaminergic neurons. Neuron 2002; 36: 1007-19
    • (2002) Neuron , vol.36 , pp. 1007-1019
    • Petrucelli, L.1    O'Farrell, C.2    Lockhart, P.J.3
  • 108
    • 0035894855 scopus 로고    scopus 로고
    • Expression of A53T mutant but not wild-type α-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death
    • Stefanis L, Larsen KE, Rideout HJ, et al. Expression of A53T mutant but not wild-type α-synuclein in PC12 cells induces alterations of the ubiquitin-dependent degradation system, loss of dopamine release, and autophagic cell death. J Neurosci 2001; 21: 9549-60
    • (2001) J Neurosci , vol.21 , pp. 9549-9560
    • Stefanis, L.1    Larsen, K.E.2    Rideout, H.J.3
  • 109
    • 5444249974 scopus 로고    scopus 로고
    • Overexpression of α-synuclein in rat substantia nigra results in loss of dopaminergic neurons, phosphorylation of α-synuclein, and activation of caspase-9: Resemblance to pathogenic changes in Parkinson's disease
    • Yamada M, Iwatsubo T, Mizuno Y, et al. Overexpression of α-synuclein in rat substantia nigra results in loss of dopaminergic neurons, phosphorylation of α-synuclein, and activation of caspase-9: resemblance to pathogenic changes in Parkinson's disease. J Neurochem 2004; 91: 451-61
    • (2004) J Neurochem , vol.91 , pp. 451-461
    • Yamada, M.1    Iwatsubo, T.2    Mizuno, Y.3
  • 110
    • 20744442130 scopus 로고    scopus 로고
    • A precipitating role for truncated α-synuclein and the proteasome in α-synuclein aggregation: Implications for pathogenesis of Parkinson disease
    • Liu CW, Giasson BI, Lewis KA, et al. A precipitating role for truncated α-synuclein and the proteasome in α-synuclein aggregation: implications for pathogenesis of Parkinson disease. J Biol Chem 2005; 280: 22670-8
    • (2005) J Biol Chem , vol.280 , pp. 22670-22678
    • Liu, C.W.1    Giasson, B.I.2    Lewis, K.A.3
  • 111
    • 19644371237 scopus 로고    scopus 로고
    • Cleavage of α-synuclein by calpain: Potential role in degradation of fibrillized and nitrated species of α-synuclein
    • Mishizen-Eberz AJ, Norris EH, Giasson BI, et al. Cleavage of α-synuclein by calpain: potential role in degradation of fibrillized and nitrated species of α-synuclein. Biochemistry 2005; 44: 7818-29
    • (2005) Biochemistry , vol.44 , pp. 7818-7829
    • Mishizen-Eberz, A.J.1    Norris, E.H.2    Giasson, B.I.3
  • 112
    • 21644446495 scopus 로고    scopus 로고
    • Proteolytic cleavage of extracellular secreted α-synuclein via matrix metalloproteinases
    • Sung JY, Park SM, Lee CH, et al. Proteolytic cleavage of extracellular secreted α-synuclein via matrix metalloproteinases. J Biol Chem 2005; 280: 25216-24
    • (2005) J Biol Chem , vol.280 , pp. 25216-25224
    • Sung, J.Y.1    Park, S.M.2    Lee, C.H.3
  • 113
    • 0142154275 scopus 로고    scopus 로고
    • Alpha-synuclein degradation by serine protease neurosin: Implication for pathogenesis of synucleinopathies
    • Iwata A, Maruyama M, Akagi T, et al. Alpha-synuclein degradation by serine protease neurosin: implication for pathogenesis of synucleinopathies. Hum Mol Genet 2003; 12: 2625-35
    • (2003) Hum Mol Genet , vol.12 , pp. 2625-2635
    • Iwata, A.1    Maruyama, M.2    Akagi, T.3
  • 114
    • 0043233011 scopus 로고    scopus 로고
    • Distinct cleavage patterns of normal and pathologic forms of α-synuclein by calpain I in vitro
    • Mishizen-Eberz AJ, Guttmann RP, Giasson BI, et al. Distinct cleavage patterns of normal and pathologic forms of α-synuclein by calpain I in vitro. J Neurochem 2003; 86: 836-47
    • (2003) J Neurochem , vol.86 , pp. 836-847
    • Mishizen-Eberz, A.J.1    Guttmann, R.P.2    Giasson, B.I.3
  • 115
    • 0142242238 scopus 로고    scopus 로고
    • Parkin cleaves intracellular α-synuclein inclusions via the activation of calpain
    • Kim SJ, Sung JY, Um JW, et al. Parkin cleaves intracellular α-synuclein inclusions via the activation of calpain. J Biol Chem 2003; 278: 41890-9
    • (2003) J Biol Chem , vol.278 , pp. 41890-41899
    • Kim, S.J.1    Sung, J.Y.2    Um, J.W.3
  • 116
    • 0028985267 scopus 로고
    • The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system
    • Iwai A, Masliah E, Yamamoto M, et al. The precursor protein of non-Aβ component of Alzheimer's disease amyloid is a presynaptic protein of the central nervous system. Neuron 1995; 14: 467-75
    • (1995) Neuron , vol.14 , pp. 467-475
    • Iwai, A.1    Masliah, E.2    Yamamoto, M.3
  • 117
    • 0031866281 scopus 로고    scopus 로고
    • Expression pattern of synucleins (non-Aβ component of Alzheimer's disease amyloid precursor protein/ α-synuclein) during murine brain development
    • Hsu L, Mallory M, Xia Y, et al. Expression pattern of synucleins (non-Aβ component of Alzheimer's disease amyloid precursor protein/ α-synuclein) during murine brain development. J Neurochem 1998; 71: 338-44
    • (1998) J Neurochem , vol.71 , pp. 338-344
    • Hsu, L.1    Mallory, M.2    Xia, Y.3
  • 118
    • 0032499264 scopus 로고    scopus 로고
    • Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism
    • Kitada T, Asakawa S, Hattori N, et al. Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Nature 1998; 392: 605-8
    • (1998) Nature , vol.392 , pp. 605-608
    • Kitada, T.1    Asakawa, S.2    Hattori, N.3
  • 119
    • 0345490853 scopus 로고    scopus 로고
    • A wide variety of mutations in the parkin gene are responsible for autosomal recessive parkinsonism in Europe
    • Abbas N, Lucking CB, Ricard S, et al. A wide variety of mutations in the parkin gene are responsible for autosomal recessive parkinsonism in Europe. Hum Mol Genet 1999; 8: 567-74
    • (1999) Hum Mol Genet , vol.8 , pp. 567-574
    • Abbas, N.1    Lucking, C.B.2    Ricard, S.3
  • 120
    • 4444327827 scopus 로고    scopus 로고
    • Parkin protects human dopaminergic neuroblastoma cells against dopamine-induced apoptosis
    • Jiang H, Ren Y, Zhao J, et al. Parkin protects human dopaminergic neuroblastoma cells against dopamine-induced apoptosis. Hum Mol Genet 2004; 13: 1745-54
    • (2004) Hum Mol Genet , vol.13 , pp. 1745-1754
    • Jiang, H.1    Ren, Y.2    Zhao, J.3
  • 121
    • 3042656791 scopus 로고    scopus 로고
    • Parkin attenuates manganese-induced dopaminergic cell death
    • Higashi Y, Asanuma M, Miyazaki I, et al. Parkin attenuates manganese-induced dopaminergic cell death. J Neurochem 2004; 89: 1490-7
    • (2004) J Neurochem , vol.89 , pp. 1490-1497
    • Higashi, Y.1    Asanuma, M.2    Miyazaki, I.3
  • 122
    • 24144447377 scopus 로고    scopus 로고
    • Updated clinical pharmacologic considerations for HIV-1 protease inhibitors
    • Anderson PL, Fletcher CV. Updated clinical pharmacologic considerations for HIV-1 protease inhibitors. Curr HIV/AIDS Rep 2004; 1: 33-9
    • (2004) Curr HIV/AIDS Rep , vol.1 , pp. 33-39
    • Anderson, P.L.1    Fletcher, C.V.2
  • 124
    • 3042554178 scopus 로고    scopus 로고
    • Peptidomimetic inhibitors of HIV protease
    • Randolph JT, Degoey DA. Peptidomimetic inhibitors of HIV protease. Curr Top Med Chem 2004; 4: 1079-95
    • (2004) Curr Top Med Chem , vol.4 , pp. 1079-1095
    • Randolph, J.T.1    Degoey, D.A.2
  • 125
    • 27644519247 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme inhibitors or angiotensin II receptor blockers for prevention and treatment of nephropathy associated with type 2 diabetes mellitus
    • Hughes DB, Britton ML. Angiotensin-converting enzyme inhibitors or angiotensin II receptor blockers for prevention and treatment of nephropathy associated with type 2 diabetes mellitus. Pharmacotherapy 2005; 25: 1602-20
    • (2005) Pharmacotherapy , vol.25 , pp. 1602-1620
    • Hughes, D.B.1    Britton, M.L.2
  • 126
    • 27744490529 scopus 로고    scopus 로고
    • Pharmacotherapy review: Angiotensin-converting enzyme inhibitors
    • Sica DA. Pharmacotherapy review: angiotensin-converting enzyme inhibitors. J Clin Hypertens 2005; 7: 485-8
    • (2005) J Clin Hypertens , vol.7 , pp. 485-488
    • Sica, D.A.1
  • 127
    • 21244451105 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme inhibitors and angiotensin II type I receptor blockers in the management of congestive heart failure patients
    • Mielniczuk L, Stevenson LW. Angiotensin-converting enzyme inhibitors and angiotensin II type I receptor blockers in the management of congestive heart failure patients. Curr Opin Cardiol 2005; 20: 250-5
    • (2005) Curr Opin Cardiol , vol.20 , pp. 250-255
    • Mielniczuk, L.1    Stevenson, L.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.