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Volumn 48, Issue 3, 2013, Pages 516-532

Protein truncation as a common denominator of human neurodegenerative foldopathies

Author keywords

Alzheimer's disease; Foldopathies; Intrinsically disordered proteins; Parkinson's disease; Proteases; Truncation

Indexed keywords

ALPHA SECRETASE; ALPHA SYNUCLEIN; AMYLOID PRECURSOR PROTEIN; ATAXIN 3; ATAXIN 7; BETA SECRETASE; CALPAIN; CALPAIN 1; CALPAIN 2; CALPASTATIN; CALPEPTIN; CASPASE 10; CASPASE 11; CASPASE 2; CASPASE 3; CASPASE 5; CASPASE 6; CASPASE 7; CASPASE 8; CASPASE 9; CATHEPSIN; GAMMA SECRETASE; HUNTINGTIN; INTERLEUKIN 1BETA CONVERTING ENZYME; MICROTUBULE ASSOCIATED PROTEIN 1; MICROTUBULE ASSOCIATED PROTEIN 2; SPECTRIN; TAR DNA BINDING PROTEIN; TAU PROTEIN; UNINDEXED DRUG;

EID: 84888008556     PISSN: 08937648     EISSN: 15591182     Source Type: Journal    
DOI: 10.1007/s12035-013-8440-8     Document Type: Review
Times cited : (12)

References (189)
  • 1
    • 33751420301 scopus 로고    scopus 로고
    • Alzheimer's-disease-associated conformation of intrinsically disordered tau protein studied by intrinsically disordered protein liquid-phase competitive enzyme-linked immunosorbent assay
    • 1:CAS:528:DC%2BD28Xht1KrsbfK
    • Skrabana R, Skrabanova-Khuebachova M, Kontsek P, Novak M (2006) Alzheimer's-disease-associated conformation of intrinsically disordered tau protein studied by intrinsically disordered protein liquid-phase competitive enzyme-linked immunosorbent assay. Analytical biochem 359:230-237
    • (2006) Analytical Biochem , vol.359 , pp. 230-237
    • Skrabana, R.1    Skrabanova-Khuebachova, M.2    Kontsek, P.3    Novak, M.4
  • 2
    • 0028802212 scopus 로고
    • Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease
    • 7588758 1:CAS:528:DyaK2MXptVCgs70%3D
    • Sticht H, Bayer P, Willbold D, Dames S, Hilbich C et al (1995) Structure of amyloid A4-(1-40)-peptide of Alzheimer's disease. Eur J Biochem 233:293-298
    • (1995) Eur J Biochem , vol.233 , pp. 293-298
    • Sticht, H.1    Bayer, P.2    Willbold, D.3    Dames, S.4    Hilbich, C.5
  • 3
    • 14644435825 scopus 로고    scopus 로고
    • Intrisically unstructured proteins and their functions
    • 15738986 1:CAS:528:DC%2BD2MXhslSlsLo%3D
    • Dyson HJ, Wright PE (2005) Intrisically unstructured proteins and their functions. Nat Rev Mol Cell Biol 6:197-208
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 4
    • 0029904487 scopus 로고    scopus 로고
    • NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded
    • 8901511 1:CAS:528:DyaK28XmtVOls7s%3D
    • Weinreb PH, Zhen W, Poon AW, Conway KA, Lansbury PT Jr (1996) NACP, a protein implicated in Alzheimer's disease and learning, is natively unfolded. Biochemistry 35:13709-13715
    • (1996) Biochemistry , vol.35 , pp. 13709-13715
    • Weinreb, P.H.1    Zhen, W.2    Poon, A.W.3    Conway, K.A.4    Lansbury, Jr.P.T.5
  • 6
    • 0037375786 scopus 로고    scopus 로고
    • Local protein unfolding and pathogenesis of polyglutamine-expansion diseases
    • 1:CAS:528:DC%2BD3sXhvFyru7Y%3D
    • Chen YW (2003) Local protein unfolding and pathogenesis of polyglutamine-expansion diseases. PROTEINS: Struct Funct Genet 51:68-73
    • (2003) PROTEINS: Struct Funct Genet , vol.51 , pp. 68-73
    • Chen, Y.W.1
  • 7
    • 68749093787 scopus 로고    scopus 로고
    • Predicting intrinsic disorder in proteins: An overview
    • 19597536 1:CAS:528:DC%2BD1MXpsFyqtL0%3D
    • He B, Wang K, Li Y, Xue B, Uversky VN, Dunker AK (2009) Predicting intrinsic disorder in proteins: An overview. Cell Res 19:929-949
    • (2009) Cell Res , vol.19 , pp. 929-949
    • He, B.1    Wang, K.2    Li, Y.3    Xue, B.4    Uversky, V.N.5    Dunker, A.K.6
  • 8
    • 67650369989 scopus 로고    scopus 로고
    • Unfoldomics of human diseases: Linking protein intrinsic disorder with diseases
    • 10.1186/1471-2164-10-S1-S7 19594884
    • Uversky VN, Oldfield CJ, Midic U, Xie H, Xue B et al (2009) Unfoldomics of human diseases: Linking protein intrinsic disorder with diseases. BMC Genomics 10(Suppl 1):S7. doi: 10.1186/1471-2164-10-S1-S7
    • (2009) BMC Genomics , vol.10 , Issue.SUPPL. 1 , pp. 7
    • Uversky, V.N.1    Oldfield, C.J.2    Midic, U.3    Xie, H.4    Xue, B.5
  • 9
    • 0024044195 scopus 로고
    • Structural characterization of the core of the paired helical filament of Alzheimer disease
    • 2455299 1:CAS:528:DyaL1cXkslWnu7s%3D
    • Wischik CM, Novak M, Edwards PC, Klug A, Tichelaar W, Crowther RA (1988) Structural characterization of the core of the paired helical filament of Alzheimer disease. Proc Natl Acad Sci USA 85:4884-4888
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4884-4888
    • Wischik, C.M.1    Novak, M.2    Edwards, P.C.3    Klug, A.4    Tichelaar, W.5    Crowther, R.A.6
  • 10
    • 0003986552 scopus 로고
    • Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease
    • 3132715 1:CAS:528:DyaL1cXkslWnur8%3D
    • Wischik CM, Novak M, Thøgersen HC, Edwards PC, Runswick MJ et al (1988) Isolation of a fragment of tau derived from the core of the paired helical filament of Alzheimer disease. Proc Natl Acad Sci USA 85:4506-4510
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4506-4510
    • Wischik, C.M.1    Novak, M.2    Thøgersen, H.C.3    Edwards, P.C.4    Runswick, M.J.5
  • 11
    • 0027398169 scopus 로고
    • Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament
    • 7679073 1:CAS:528:DyaK3sXpvFKiug%3D%3D
    • Novak M, Kabat J, Wischik CM (1993) Molecular characterization of the minimal protease resistant tau unit of the Alzheimer's disease paired helical filament. EMBO J 12:365-370
    • (1993) EMBO J , vol.12 , pp. 365-370
    • Novak, M.1    Kabat, J.2    Wischik, C.M.3
  • 12
    • 0028458037 scopus 로고
    • Truncated tau protein as a new marker for Alzheimer's disease
    • 7817900 1:CAS:528:DyaK2MXhtVykurw%3D
    • Novak M (1994) Truncated tau protein as a new marker for Alzheimer's disease. Acta Virol 38:173-189
    • (1994) Acta Virol , vol.38 , pp. 173-189
    • Novak, M.1
  • 13
    • 77950584656 scopus 로고    scopus 로고
    • Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease
    • 20086007 1:CAS:528:DC%2BC3cXjtFShsLg%3D
    • Landles C, Sathasivam K, Weiss A, Woodman B, Moffitt H et al (2010) Proteolysis of mutant huntingtin produces an exon 1 fragment that accumulates as an aggregated protein in neuronal nuclei in Huntington disease. J Biol Chem 285:8808-8823
    • (2010) J Biol Chem , vol.285 , pp. 8808-8823
    • Landles, C.1    Sathasivam, K.2    Weiss, A.3    Woodman, B.4    Moffitt, H.5
  • 14
    • 0036671821 scopus 로고    scopus 로고
    • Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions
    • 12191472 1:CAS:528:DC%2BD38Xmslyrtbo%3D
    • Lunkes A, Lindenberg KS, Ben-Haiem L, Weber C, Devys D, Landwehrmeyer GB, Mandel JL, Trottier Y (2002) Proteases acting on mutant huntingtin generate cleaved products that differentially build up cytoplasmic and nuclear inclusions. Mol Cell 10:259-269
    • (2002) Mol Cell , vol.10 , pp. 259-269
    • Lunkes, A.1    Lindenberg, K.S.2    Ben-Haiem, L.3    Weber, C.4    Devys, D.5    Landwehrmeyer, G.B.6    Mandel, J.L.7    Trottier, Y.8
  • 15
    • 0022744803 scopus 로고
    • Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology
    • 3088567 1:CAS:528:DyaL28XksFyqtrg%3D
    • Grundke-Iqbal I, Iqbal K, Tung YC, Quinlan M, Wisniewski HM, Binder LI (1986) Abnormal phosphorylation of the microtubule-associated protein tau (tau) in Alzheimer cytoskeletal pathology. Proc Natl Acad Sci U S A 83:4913-4917
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 4913-4917
    • Grundke-Iqbal, I.1    Iqbal, K.2    Tung, Y.C.3    Quinlan, M.4    Wisniewski, H.M.5    Binder, L.I.6
  • 16
    • 33747633422 scopus 로고    scopus 로고
    • Huntingtin phosphorylation sites mapped by mass spectrometry. Modulation of cleavage and toxicity
    • 16782707 1:CAS:528:DC%2BD28XotVCmur4%3D
    • Schilling B, Gafni J, Torcassi C, Cong X, Row RH et al (2006) Huntingtin phosphorylation sites mapped by mass spectrometry. Modulation of cleavage and toxicity. J Biol Chem 281:23686-23697
    • (2006) J Biol Chem , vol.281 , pp. 23686-23697
    • Schilling, B.1    Gafni, J.2    Torcassi, C.3    Cong, X.4    Row, R.H.5
  • 17
    • 34247160537 scopus 로고    scopus 로고
    • Phosphorylation of ataxin-3 by glycogen synthase kinase 3beta at serine 256 regulates the aggregation of ataxin-3
    • 17434145 1:CAS:528:DC%2BD2sXksFeiu7s%3D
    • Fei E, Jia N, Zhang T, Ma X, Wang H et al (2007) Phosphorylation of ataxin-3 by glycogen synthase kinase 3beta at serine 256 regulates the aggregation of ataxin-3. Biochem Biophys Res Commun 357:487-492
    • (2007) Biochem Biophys Res Commun , vol.357 , pp. 487-492
    • Fei, E.1    Jia, N.2    Zhang, T.3    Ma, X.4    Wang, H.5
  • 18
    • 77949908515 scopus 로고    scopus 로고
    • Phosphorylated and cleaved TDP-43 in ALS, FTLD and other neurodegenerative disorders and in cellular models of TDP-43 proteinopathy
    • 20102522
    • Arai T, Hasegawa M, Nonoka T, Kametani F, Yamashita M et al (2010) Phosphorylated and cleaved TDP-43 in ALS, FTLD and other neurodegenerative disorders and in cellular models of TDP-43 proteinopathy. Neuropathology 30:170-181
    • (2010) Neuropathology , vol.30 , pp. 170-181
    • Arai, T.1    Hasegawa, M.2    Nonoka, T.3    Kametani, F.4    Yamashita, M.5
  • 19
    • 0024988546 scopus 로고
    • Molecular analysis of neurofibrillary degeneration in Alzheimer's disease. An immunohistochemical study
    • 2169192 1:STN:280:DyaK3cznvFanug%3D%3D
    • Bondareff W, Wischik CM, Novak M, Amos WB, Klug A, Roth M (1990) Molecular analysis of neurofibrillary degeneration in Alzheimer's disease. An immunohistochemical study. Am J Pathol 137:711-723
    • (1990) Am J Pathol , vol.137 , pp. 711-723
    • Bondareff, W.1    Wischik, C.M.2    Novak, M.3    Amos, W.B.4    Klug, A.5    Roth, M.6
  • 20
    • 9444239187 scopus 로고    scopus 로고
    • Huntingtin is ubiquitinated and interacts with a specific ubiquitin- conjugating enzyme
    • 8702625 1:CAS:528:DyaK28XkvFyms7c%3D
    • Kalchman MA, Graham RK, Xia G, Koide HB, Hodgson JG et al (1996) Huntingtin is ubiquitinated and interacts with a specific ubiquitin- conjugating enzyme. J Biol Chem 271:19385-19394
    • (1996) J Biol Chem , vol.271 , pp. 19385-19394
    • Kalchman, M.A.1    Graham, R.K.2    Xia, G.3    Koide, H.B.4    Hodgson, J.G.5
  • 21
    • 0034687807 scopus 로고    scopus 로고
    • Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1)
    • 11121022 1:CAS:528:DC%2BD3MXitVCgtg%3D%3D
    • Poukka H, Karvonen U, Janne OA, Palvimo JJ (2000) Covalent modification of the androgen receptor by small ubiquitin-like modifier 1 (SUMO-1). Proc Natl Acad Sci USA 97:14145-14150
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14145-14150
    • Poukka, H.1    Karvonen, U.2    Janne, O.A.3    Palvimo, J.J.4
  • 22
    • 33845898194 scopus 로고    scopus 로고
    • Ubiquitin-conjugating enzyme E2-25 K increases aggregate formation and cell death in polyglutamine diseases
    • 17092742
    • de Pril R, Fischer DF, Roos RA, van Leeuwen FW (2007) Ubiquitin-conjugating enzyme E2-25 K increases aggregate formation and cell death in polyglutamine diseases. Mol Cell Neurosci 34:10-19
    • (2007) Mol Cell Neurosci , vol.34 , pp. 10-19
    • De Pril, R.1    Fischer, D.F.2    Roos, R.A.3    Van Leeuwen, F.W.4
  • 23
    • 69549131138 scopus 로고    scopus 로고
    • Accumulation of ubiquitin conjugates in a polyglutamine disease model occurs without global ubiquitin/proteasome system impairment
    • 19666572 1:CAS:528:DC%2BD1MXhtFWgt7bM
    • Maynard CJ, Böttcher C, Ortega Z, Smith R, Florea BI et al (2009) Accumulation of ubiquitin conjugates in a polyglutamine disease model occurs without global ubiquitin/proteasome system impairment. Proc Natl Acad Sci U S A 106:13986-13991
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13986-13991
    • Maynard, C.J.1    Böttcher, C.2    Ortega, Z.3    Smith, R.4    Florea, B.I.5
  • 24
    • 0031669073 scopus 로고    scopus 로고
    • Advanced glycation end products in Alzheimer's disease and other neurodegenerative diseases
    • 9777946 1:CAS:528:DyaK1cXmvFGmsbc%3D
    • Sasaki N, Fukatsu R, Tsuzuki K, Hayashi Y, Yoshida T et al (1998) Advanced glycation end products in Alzheimer's disease and other neurodegenerative diseases. Am J Pathol 153:1149-1155
    • (1998) Am J Pathol , vol.153 , pp. 1149-1155
    • Sasaki, N.1    Fukatsu, R.2    Tsuzuki, K.3    Hayashi, Y.4    Yoshida, T.5
  • 25
    • 3242726002 scopus 로고    scopus 로고
    • Expression of the receptor for advanced glycation end products in Huntington's disease caudate nucleus
    • 15262199 1:CAS:528:DC%2BD2cXlsl2isLY%3D
    • Ma L, Nicholson LF (2004) Expression of the receptor for advanced glycation end products in Huntington's disease caudate nucleus. Brain Res 1018:10-17
    • (2004) Brain Res , vol.1018 , pp. 10-17
    • Ma, L.1    Nicholson, L.F.2
  • 26
    • 79955657305 scopus 로고    scopus 로고
    • Role of advanced glycation on aggregation and DNA binding properties of α-synuclein
    • 21441659 1:CAS:528:DC%2BC3MXltFGrsbY%3D
    • Padmaraju V, Bhaskar JJ, Prasada Rao UJ, Salimath PV, Rao KS (2011) Role of advanced glycation on aggregation and DNA binding properties of α-synuclein. J Alzheimers Dis 24(Suppl 2):211-221
    • (2011) J Alzheimers Dis , vol.24 , Issue.SUPPL. 2 , pp. 211-221
    • Padmaraju, V.1    Bhaskar, J.J.2    Prasada Rao, U.J.3    Salimath, P.V.4    Rao, K.S.5
  • 27
    • 0029815467 scopus 로고    scopus 로고
    • Glycosylation of microtubule-associated protein tau: An abnormal posttranslational modification in Alzheimer's disease
    • 8705855 1:CAS:528:DyaK28XkslGiu7Y%3D
    • Wang JZ, Grundke-Iqbal I, Iqbal K (1996) Glycosylation of microtubule-associated protein tau: An abnormal posttranslational modification in Alzheimer's disease. Nat Med 2:871-875
    • (1996) Nat Med , vol.2 , pp. 871-875
    • Wang, J.Z.1    Grundke-Iqbal, I.2    Iqbal, K.3
  • 28
    • 33745971404 scopus 로고    scopus 로고
    • Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain
    • 16714295
    • Marz P, Stetefeld J, Bendfeldt K, Nitsch C, Reinstein J et al (2006) Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain. J Biol Chem 281:20263-20270
    • (2006) J Biol Chem , vol.281 , pp. 20263-20270
    • Marz, P.1    Stetefeld, J.2    Bendfeldt, K.3    Nitsch, C.4    Reinstein, J.5
  • 29
    • 0042926482 scopus 로고    scopus 로고
    • Nitration of tau protein is linked to neurodegeneration in tauopathies
    • 12937143 1:CAS:528:DC%2BD3sXnsVCisr4%3D
    • Horiguchi T, Uryu K, Giasson BI, Ischiropoulos H, LightFoot R et al (2003) Nitration of tau protein is linked to neurodegeneration in tauopathies. Am J Pathol 163:1021-1031
    • (2003) Am J Pathol , vol.163 , pp. 1021-1031
    • Horiguchi, T.1    Uryu, K.2    Giasson, B.I.3    Ischiropoulos, H.4    Lightfoot, R.5
  • 30
    • 77956298994 scopus 로고    scopus 로고
    • Nitrated alpha-synuclein induces the loss of dopaminergic neurons in the substantia nigra of rats
    • 20386702
    • Yu Z, Xu X, Xiang Z, Zhou J, Zhang Z, Hu C, He C (2010) Nitrated alpha-synuclein induces the loss of dopaminergic neurons in the substantia nigra of rats. PLoS One 5:e9956
    • (2010) PLoS One , vol.5 , pp. 9956
    • Yu, Z.1    Xu, X.2    Xiang, Z.3    Zhou, J.4    Zhang, Z.5    Hu, C.6    He, C.7
  • 31
    • 11144353613 scopus 로고    scopus 로고
    • SUMO modification of huntingtin and Huntington's disease pathology
    • 15064418 1:CAS:528:DC%2BD2cXis1ansLs%3D
    • Steffan JS, Agrawal N, Pallos J, Rockabrand E, Trotman LC et al (2004) SUMO modification of huntingtin and Huntington's disease pathology. Science 304:100-104
    • (2004) Science , vol.304 , pp. 100-104
    • Steffan, J.S.1    Agrawal, N.2    Pallos, J.3    Rockabrand, E.4    Trotman, L.C.5
  • 32
    • 20444467297 scopus 로고    scopus 로고
    • SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal
    • 15824120 1:CAS:528:DC%2BD2MXksl2hs7w%3D
    • Riley BE, Zoghbi HY, Orr HT (2005) SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal. J Biol Chem 280:21942-21948
    • (2005) J Biol Chem , vol.280 , pp. 21942-21948
    • Riley, B.E.1    Zoghbi, H.Y.2    Orr, H.T.3
  • 33
    • 33744544785 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) modification of natively unfolded proteins tau and alpha-synuclein
    • 16464864 1:CAS:528:DC%2BD28Xjt1Knt7c%3D
    • Dorval V, Fraser PE (2006) Small ubiquitin-like modifier (SUMO) modification of natively unfolded proteins tau and alpha-synuclein. J Biol Chem 281:9919-9924
    • (2006) J Biol Chem , vol.281 , pp. 9919-9924
    • Dorval, V.1    Fraser, P.E.2
  • 34
    • 79959855550 scopus 로고    scopus 로고
    • Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation
    • 21641618 1:CAS:528:DC%2BC3MXosFeit7s%3D
    • Kim YM, Jang WH, Quezado MM, Oh Y, Chung KC, Junn E, Mouradian MM (2011) Proteasome inhibition induces α-synuclein SUMOylation and aggregate formation. J Neurol Sci 307:157-161
    • (2011) J Neurol Sci , vol.307 , pp. 157-161
    • Kim, Y.M.1    Jang, W.H.2    Quezado, M.M.3    Oh, Y.4    Chung, K.C.5    Junn, E.6    Mouradian, M.M.7
  • 35
    • 0022351939 scopus 로고
    • Genetic linkage between Huntington's disease and the DNA polymorphism G8 in South Wales families
    • 3001311 1:STN:280:DyaL28%2FovFSgsg%3D%3D
    • Harper PS, Youngman S, Anderson MA, Sarfarazi M, Quarrell O, Tanzi R et al (1985) Genetic linkage between Huntington's disease and the DNA polymorphism G8 in South Wales families. J Med Genet 22:447-450
    • (1985) J Med Genet , vol.22 , pp. 447-450
    • Harper, P.S.1    Youngman, S.2    Anderson, M.A.3    Sarfarazi, M.4    Quarrell, O.5    Tanzi, R.6
  • 36
    • 0025925236 scopus 로고
    • The 717Val-Ile substitution in amyloid precursor protein is associated with familial Alzheimer's disease regardless of ethnic groups
    • 1908231 1:CAS:528:DyaK3MXltlegs7Y%3D
    • Yoshioka K, Miki T, Katsuya T, Ogihara T, Sakaki Y (1991) The 717Val-Ile substitution in amyloid precursor protein is associated with familial Alzheimer's disease regardless of ethnic groups. Biochem Biophys Res Commun 178:1141-1146
    • (1991) Biochem Biophys Res Commun , vol.178 , pp. 1141-1146
    • Yoshioka, K.1    Miki, T.2    Katsuya, T.3    Ogihara, T.4    Sakaki, Y.5
  • 37
    • 0027279516 scopus 로고
    • Hereditary Parkinson disease: Report of 3 families with dominant autosomal inheritance
    • 8321342 1:STN:280:DyaK3szgvFKhtA%3D%3D
    • Wszolek ZK, Cordes M, Calne DB, Münter MD, Cordes I, Pfeifer RF (1993) Hereditary Parkinson disease: Report of 3 families with dominant autosomal inheritance. Nervenarzt 64:331-335
    • (1993) Nervenarzt , vol.64 , pp. 331-335
    • Wszolek, Z.K.1    Cordes, M.2    Calne, D.B.3    Münter, M.D.4    Cordes, I.5    Pfeifer, R.F.6
  • 38
    • 0030744876 scopus 로고    scopus 로고
    • Mutation in the alpha-synuclein gene identified in families with Parkinson's disease
    • 9197268 1:CAS:528:DyaK2sXkt1altr4%3D
    • Polymeropoulos MH, Lavedan C, Leroy E, Ide SE, Dehejia A et al (1997) Mutation in the alpha-synuclein gene identified in families with Parkinson's disease. Science 276:2045-2047
    • (1997) Science , vol.276 , pp. 2045-2047
    • Polymeropoulos, M.H.1    Lavedan, C.2    Leroy, E.3    Ide, S.E.4    Dehejia, A.5
  • 41
    • 0032477559 scopus 로고    scopus 로고
    • Analysis of the alpha-synuclein G209A mutation in familial Parkinson's disease
    • 9433434 1:STN:280:DyaK1c%2FpsFSiuw%3D%3D
    • Zareparsi S, Kaye J, Camicioli R, Kramer P, Nutt J, Bird T, Litt M, Payami H (1998) Analysis of the alpha-synuclein G209A mutation in familial Parkinson's disease. Lancet 351:37-38
    • (1998) Lancet , vol.351 , pp. 37-38
    • Zareparsi, S.1    Kaye, J.2    Camicioli, R.3    Kramer, P.4    Nutt, J.5    Bird, T.6    Litt, M.7    Payami, H.8
  • 42
    • 0035421638 scopus 로고    scopus 로고
    • Pathogenic APP mutations near the γ-secretase cleavage site differentially affect Aβ secretion and APP C-terminal fragment stability
    • 11487570
    • De Jonghe C, Esselens C, Singh SK, Craessaerts K, Serneels S et al (2001) Pathogenic APP mutations near the γ-secretase cleavage site differentially affect Aβ secretion and APP C-terminal fragment stability. Hum Mol Genet 10:1665-1671
    • (2001) Hum Mol Genet , vol.10 , pp. 1665-1671
    • De Jonghe, C.1    Esselens, C.2    Singh, S.K.3    Craessaerts, K.4    Serneels, S.5
  • 43
    • 0037379416 scopus 로고    scopus 로고
    • Homozygosity for CAG mutation in Huntington disease is associated with a more severe clinical course
    • 12615650
    • Squitieri F, Gellera C, Cannella M, Mariotti C, Cislaghi G et al (2003) Homozygosity for CAG mutation in Huntington disease is associated with a more severe clinical course. Brain 126:946-955
    • (2003) Brain , vol.126 , pp. 946-955
    • Squitieri, F.1    Gellera, C.2    Cannella, M.3    Mariotti, C.4    Cislaghi, G.5
  • 44
    • 76549087651 scopus 로고    scopus 로고
    • Transition of tau protein from disordered to misordered in Alzheimer's disease
    • 20160453 1:CAS:528:DC%2BC3cXks1Kjtrw%3D
    • Kovacech B, Skrabana R, Novak M (2010) Transition of tau protein from disordered to misordered in Alzheimer's disease. Neurodegener Dis 7:24-27
    • (2010) Neurodegener Dis , vol.7 , pp. 24-27
    • Kovacech, B.1    Skrabana, R.2    Novak, M.3
  • 45
    • 33747606218 scopus 로고    scopus 로고
    • Expression of a truncated tau protein induces oxidative stress in a rodent model of tauopathy
    • 16930434
    • Cente M, Filipcik P, Pevalova M, Novak M (2006) Expression of a truncated tau protein induces oxidative stress in a rodent model of tauopathy. Eur J Neurosci 24:1085-1090
    • (2006) Eur J Neurosci , vol.24 , pp. 1085-1090
    • Cente, M.1    Filipcik, P.2    Pevalova, M.3    Novak, M.4
  • 46
    • 67650556426 scopus 로고    scopus 로고
    • Caspase-cleaved tau expression induces mitochondrial dysfunction in immortalized cortical neurons: Implications for the pathogenesis of Alzheimer disease
    • 19389700 1:CAS:528:DC%2BD1MXotVKnsLs%3D
    • Quintanilla RA, Matthews-Roberson TA, Dolan PJ, Johnson GV (2009) Caspase-cleaved tau expression induces mitochondrial dysfunction in immortalized cortical neurons: Implications for the pathogenesis of Alzheimer disease. J Biol Chem 284:18754-18766
    • (2009) J Biol Chem , vol.284 , pp. 18754-18766
    • Quintanilla, R.A.1    Matthews-Roberson, T.A.2    Dolan, P.J.3    Johnson, G.V.4
  • 47
    • 77957563700 scopus 로고    scopus 로고
    • A NH2 tau fragment targets neuronal mitochondria at AD synapses: Possible implications for neurodegeneration
    • 20571215 1:CAS:528:DC%2BC3cXhtVKiurbK
    • Amadoro G, Corsetti V, Stringaro A, Colone M, D'Aguanno S et al (2010) A NH2 tau fragment targets neuronal mitochondria at AD synapses: Possible implications for neurodegeneration. J Alzheimers Dis 21:445-470
    • (2010) J Alzheimers Dis , vol.21 , pp. 445-470
    • Amadoro, G.1    Corsetti, V.2    Stringaro, A.3    Colone, M.4    D'Aguanno, S.5
  • 48
    • 0025452640 scopus 로고
    • Proteolytic processing β-amyloid precursor by calpain i
    • Siman R, Card JP, Davis LG (1990) Proteolytic processing β-amyloid precursor by calpain I. J Neurosci 70:2400-2411
    • (1990) J Neurosci , vol.70 , pp. 2400-2411
    • Siman, R.1    Card, J.P.2    Davis, L.G.3
  • 49
    • 0025828989 scopus 로고
    • Tau-related protein present in paired helical filaments has a decreased tubulin binding capacity as compared with microtubule-associated protein tau
    • 2018792 1:CAS:528:DyaK3MXit1Ojsr8%3D
    • Nieto A, Correas I, López-Otín C, Avila J (1991) Tau-related protein present in paired helical filaments has a decreased tubulin binding capacity as compared with microtubule-associated protein tau. Biochim Biophys Acta 1096:197-204
    • (1991) Biochim Biophys Acta , vol.1096 , pp. 197-204
    • Nieto, A.1    Correas, I.2    López-Otín, C.3    Avila, J.4
  • 50
    • 33745152289 scopus 로고    scopus 로고
    • Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo
    • 16753151 1:CAS:528:DC%2BD28XmtVOmsbs%3D
    • Zilka N, Filipcik P, Koson P, Fialova L, Skrabana R et al (2006) Truncated tau from sporadic Alzheimer's disease suffices to drive neurofibrillary degeneration in vivo. FEBS Lett 580:3582-3588
    • (2006) FEBS Lett , vol.580 , pp. 3582-3588
    • Zilka, N.1    Filipcik, P.2    Koson, P.3    Fialova, L.4    Skrabana, R.5
  • 51
    • 33646480747 scopus 로고    scopus 로고
    • Reversal of Alzheimer's-like pathology and behavior in human APP transgenic mice by mutation of Asp664
    • 1:CAS:528:DC%2BD28XkslCktLo%3D
    • Galvan V, Gorostiza OF, Banwait S, Ataie M, Logvinova AV et al (2006) Reversal of Alzheimer's-like pathology and behavior in human APP transgenic mice by mutation of Asp664. Proc Natl Acal Sci 103:7130-7135
    • (2006) Proc Natl Acal Sci , vol.103 , pp. 7130-7135
    • Galvan, V.1    Gorostiza, O.F.2    Banwait, S.3    Ataie, M.4    Logvinova, A.V.5
  • 52
    • 20744442130 scopus 로고    scopus 로고
    • A precipitating role for truncated alpha-synuclein and the proteasome in alpha-synuclein aggregation: Implications for pathogenesis of Parkinson's disease
    • 15840579 1:CAS:528:DC%2BD2MXltVyhsb8%3D
    • Liu CW, Giasson BI, Lewis KA, Lee VM, Demartino GN, Thomas PJ (2005) A precipitating role for truncated alpha-synuclein and the proteasome in alpha-synuclein aggregation: Implications for pathogenesis of Parkinson's disease. J Biol Chem 280:22670-22678
    • (2005) J Biol Chem , vol.280 , pp. 22670-22678
    • Liu, C.W.1    Giasson, B.I.2    Lewis, K.A.3    Lee, V.M.4    Demartino, G.N.5    Thomas, P.J.6
  • 53
    • 34250832784 scopus 로고    scopus 로고
    • Calpain-cleavage of α-synuclein connecting proteolytic processing to disease-linked aggregation
    • 17456777 1:CAS:528:DC%2BD2sXlvFCnsbo%3D
    • Dufty BM, Warner LR, Hou ST, Jiang SX, Gomez-Isla T et al (2007) Calpain-cleavage of α-synuclein connecting proteolytic processing to disease-linked aggregation. Am J Pathol 170:1725-1738
    • (2007) Am J Pathol , vol.170 , pp. 1725-1738
    • Dufty, B.M.1    Warner, L.R.2    Hou, S.T.3    Jiang, S.X.4    Gomez-Isla, T.5
  • 54
    • 0030752709 scopus 로고    scopus 로고
    • Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain
    • 9302293 1:CAS:528:DyaK2sXmt12rurs%3D
    • DiFiglia M, Sapp E, Chase KO, Davies SW, Bates GP, Vonsattel JP, Aronin N (1997) Aggregation of huntingtin in neuronal intranuclear inclusions and dystrophic neurites in brain. Science 277:1990-1993
    • (1997) Science , vol.277 , pp. 1990-1993
    • Difiglia, M.1    Sapp, E.2    Chase, K.O.3    Davies, S.W.4    Bates, G.P.5    Vonsattel, J.P.6    Aronin, N.7
  • 56
    • 0032946228 scopus 로고    scopus 로고
    • In vitro evidence for both the nucleus and cytoplasm as subcellular sites of pathogenesis in Huntington's disease
    • 9887328 1:CAS:528:DyaK1MXoslentQ%3D%3D
    • Hackam AS, Singaraja R, Zhang T, Gan L, Hayden MR (1999) In vitro evidence for both the nucleus and cytoplasm as subcellular sites of pathogenesis in Huntington's disease. Hum Mol Genet 8:25-33
    • (1999) Hum Mol Genet , vol.8 , pp. 25-33
    • Hackam, A.S.1    Singaraja, R.2    Zhang, T.3    Gan, L.4    Hayden, M.R.5
  • 57
    • 0034733607 scopus 로고    scopus 로고
    • Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal cells
    • 10770929 1:CAS:528:DC%2BD3cXkslahtLk%3D
    • Wellington CL, Singaraja R, Ellerby L, Savill J, Roy S et al (2000) Inhibiting caspase cleavage of huntingtin reduces toxicity and aggregate formation in neuronal and nonneuronal cells. J Biol Chem 275:19831-19838
    • (2000) J Biol Chem , vol.275 , pp. 19831-19838
    • Wellington, C.L.1    Singaraja, R.2    Ellerby, L.3    Savill, J.4    Roy, S.5
  • 58
    • 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
    • 11245667 1:CAS:528:DC%2BD3MXjslClsLk%3D
    • Mende-Mueller LM, Toneff T, Hwang SR, Chesselet MF, Hook VY (2001) 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 21:1830-1837
    • (2001) J Neurosci , vol.21 , pp. 1830-1837
    • Mende-Mueller, L.M.1    Toneff, T.2    Hwang, S.R.3    Chesselet, M.F.4    Hook, V.Y.5
  • 59
    • 0037096376 scopus 로고    scopus 로고
    • Calpain activation in Huntington's disease
    • 12077181 1:CAS:528:DC%2BD38Xlt1SgsrY%3D
    • Gafni J, Ellerby LM (2002) Calpain activation in Huntington's disease. J Neurosci 22:4842-4849
    • (2002) J Neurosci , vol.22 , pp. 4842-4849
    • Gafni, J.1    Ellerby, L.M.2
  • 60
    • 0030058208 scopus 로고    scopus 로고
    • Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo
    • 8640226 1:CAS:528:DyaK28XktlOhur8%3D
    • Ikeda H, Yamaguchi M, Sugai S, Aze Y, Narumiya S, Kakizuka A (1996) Expanded polyglutamine in the Machado-Joseph disease protein induces cell death in vitro and in vivo. Nat Genet 13:196-202
    • (1996) Nat Genet , vol.13 , pp. 196-202
    • Ikeda, H.1    Yamaguchi, M.2    Sugai, S.3    Aze, Y.4    Narumiya, S.5    Kakizuka, A.6
  • 61
    • 20844462057 scopus 로고    scopus 로고
    • A mutant ataxin-3 putative-cleavage fragment in brains of Machado-Joseph disease patients and transgenic mice is cytotoxic above a critical concentration
    • 15537899 1:CAS:528:DC%2BD2cXhtVeqtb%2FJ
    • Goti D, Katzen SM, Mez J, Kurtis N, Kiluk J et al (2004) A mutant ataxin-3 putative-cleavage fragment in brains of Machado-Joseph disease patients and transgenic mice is cytotoxic above a critical concentration. J Neurosci 24:10266-10279
    • (2004) J Neurosci , vol.24 , pp. 10266-10279
    • Goti, D.1    Katzen, S.M.2    Mez, J.3    Kurtis, N.4    Kiluk, J.5
  • 62
    • 34547129609 scopus 로고    scopus 로고
    • Calpain inhibition is sufficient to suppress aggregation of polyglutamine-expanded ataxin-3
    • 17488727 1:CAS:528:DC%2BD2sXmvVarsLY%3D
    • Haacke AF, Hartl U, Breuer P (2007) Calpain inhibition is sufficient to suppress aggregation of polyglutamine-expanded ataxin-3. J Biol Chem 282:18851-18856
    • (2007) J Biol Chem , vol.282 , pp. 18851-18856
    • Haacke, A.F.1    Hartl, U.2    Breuer, P.3
  • 63
    • 35648964788 scopus 로고    scopus 로고
    • Proteolytic cleavage of ataxin-7 by caspase-7 modulates cellular toxicity and transcriptional dysregulation
    • 17646170 1:CAS:528:DC%2BD2sXhtFagtbbI
    • Young JE, Gouw L, Propp S, Sopher BL, Taylor J et al (2007) Proteolytic cleavage of ataxin-7 by caspase-7 modulates cellular toxicity and transcriptional dysregulation. J Biol Chem 282:30150-30160
    • (2007) J Biol Chem , vol.282 , pp. 30150-30160
    • Young, J.E.1    Gouw, L.2    Propp, S.3    Sopher, B.L.4    Taylor, J.5
  • 64
    • 9144224301 scopus 로고    scopus 로고
    • Identification of amino-terminally cleaved tau fragments that distinguish progressive supranuclear palsy from corticobasal degeneration
    • 14705114 1:CAS:528:DC%2BD2cXhtVOmsr4%3D
    • Arai T, Ikeda K, Akiyama H, Nonaka T, Hasegawa M et al (2004) Identification of amino-terminally cleaved tau fragments that distinguish progressive supranuclear palsy from corticobasal degeneration. Ann Neurol 55:72-79
    • (2004) Ann Neurol , vol.55 , pp. 72-79
    • Arai, T.1    Ikeda, K.2    Akiyama, H.3    Nonaka, T.4    Hasegawa, M.5
  • 66
    • 67650113333 scopus 로고    scopus 로고
    • Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43
    • 19515851 1:CAS:528:DC%2BD1MXhtVehurbL
    • Nonaka T, Kametani F, Arai T, Akiyama H, Hasegawa M (2009) Truncation and pathogenic mutations facilitate the formation of intracellular aggregates of TDP-43. Hum Mol Genet 18:3353-3364
    • (2009) Hum Mol Genet , vol.18 , pp. 3353-3364
    • Nonaka, T.1    Kametani, F.2    Arai, T.3    Akiyama, H.4    Hasegawa, M.5
  • 67
    • 20044381844 scopus 로고    scopus 로고
    • Tau truncation during neurofibrillary tangle evolution in Alzheimer's disease
    • 15748781 1:CAS:528:DC%2BD2MXhvVektrc%3D
    • Guillozet-Bongaarts AL, Garcia-Sierra F, Reynolds MR, Horowitz PM et al (2005) Tau truncation during neurofibrillary tangle evolution in Alzheimer's disease. Neurobiol Aging 26:1015-1022
    • (2005) Neurobiol Aging , vol.26 , pp. 1015-1022
    • Guillozet-Bongaarts, A.L.1    Garcia-Sierra, F.2    Reynolds, M.R.3    Horowitz, P.M.4
  • 68
    • 0033597852 scopus 로고    scopus 로고
    • Proteolysis processing in the secretory pathway
    • 10409610 1:CAS:528:DyaK1MXkvVKktb4%3D
    • Zhou A, Webb G, Zhu X, Steiner DF (1999) Proteolysis processing in the secretory pathway. J Biol Chem 274:20745-20748
    • (1999) J Biol Chem , vol.274 , pp. 20745-20748
    • Zhou, A.1    Webb, G.2    Zhu, X.3    Steiner, D.F.4
  • 69
    • 0024814559 scopus 로고
    • Characterization of the first monoclonal antibody against the pronase resistant core of the Alzheimer PHF
    • 2602435 1:CAS:528:DyaL1MXmtlSgsL8%3D
    • Novak M, Wischik CM, Edwards PC, Panell R, Milstein C (1989) Characterization of the first monoclonal antibody against the pronase resistant core of the Alzheimer PHF. Prog Clin Biol Res 317:755-761
    • (1989) Prog Clin Biol Res , vol.317 , pp. 755-761
    • Novak, M.1    Wischik, C.M.2    Edwards, P.C.3    Panell, R.4    Milstein, C.5
  • 70
    • 0026053022 scopus 로고
    • Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51
    • 1712107 1:CAS:528:DyaK3MXmtVGjtro%3D
    • Novak M, Jakes R, Edwards PC, Milstein C, Wischik CM (1991) Difference between the tau protein of Alzheimer paired helical filament core and normal tau revealed by epitope analysis of monoclonal antibodies 423 and 7.51. Proc Natl Acad Sci USA 88:5837-5841
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 5837-5841
    • Novak, M.1    Jakes, R.2    Edwards, P.C.3    Milstein, C.4    Wischik, C.M.5
  • 71
    • 48249130806 scopus 로고    scopus 로고
    • Truncated tau expression levels determine life span of a rat model of tauopathy without causing neuronal loss or correlating with terminal neurofibrillary tangle load
    • 18702695
    • Koson P, Zilka N, Kovac A, Kovacech B, Korenova M, Filipcik P, Novak M (2008) Truncated tau expression levels determine life span of a rat model of tauopathy without causing neuronal loss or correlating with terminal neurofibrillary tangle load. Eur J Neurosci 28:239-246
    • (2008) Eur J Neurosci , vol.28 , pp. 239-246
    • Koson, P.1    Zilka, N.2    Kovac, A.3    Kovacech, B.4    Korenova, M.5    Filipcik, P.6    Novak, M.7
  • 72
  • 73
    • 0033677809 scopus 로고    scopus 로고
    • C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease
    • 11034902 1:CAS:528:DC%2BD3cXosVGmtLY%3D
    • Abraha A, Ghoshal N, Gamblin TC, Cryns V, Berry RW, Kuret J, Binder LI (2000) C-terminal inhibition of tau assembly in vitro and in Alzheimer's disease. J Cell Sci 113(Pt 21):3737-3745
    • (2000) J Cell Sci , vol.113 , Issue.PART 21 , pp. 3737-3745
    • Abraha, A.1    Ghoshal, N.2    Gamblin, T.C.3    Cryns, V.4    Berry, R.W.5    Kuret, J.6    Binder, L.I.7
  • 74
    • 0041689948 scopus 로고    scopus 로고
    • Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease
    • 12888622 1:CAS:528:DC%2BD3sXmvVeisrc%3D
    • Gamblin TC, Chen F, Zambrano A, Abraha A, Lagalwar S et al (2003) Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc Natl Acad Sci USA 100:10032-10037
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 10032-10037
    • Gamblin, T.C.1    Chen, F.2    Zambrano, A.3    Abraha, A.4    Lagalwar, S.5
  • 75
    • 3242749074 scopus 로고    scopus 로고
    • Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology
    • 15232619 1:CAS:528:DC%2BD2cXls1altb8%3D
    • Rissman RA, Poon WW, Blurton-Jones M, Oddo S, Torp R et al (2004) Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology. J Clin Invest 114:121-130
    • (2004) J Clin Invest , vol.114 , pp. 121-130
    • Rissman, R.A.1    Poon, W.W.2    Blurton-Jones, M.3    Oddo, S.4    Torp, R.5
  • 76
    • 14844328111 scopus 로고    scopus 로고
    • The role of caspase cleavage of tau in Alzheimer disease neuropathology
    • 15751224 1:CAS:528:DC%2BD2MXis1KhsL8%3D
    • Cotman CW, Poon WW, Rissman RA, Blurton-Jones M (2005) The role of caspase cleavage of tau in Alzheimer disease neuropathology. J Neuropathol Exp Neurol 64:104-112
    • (2005) J Neuropathol Exp Neurol , vol.64 , pp. 104-112
    • Cotman, C.W.1    Poon, W.W.2    Rissman, R.A.3    Blurton-Jones, M.4
  • 78
    • 38549120646 scopus 로고    scopus 로고
    • In vivo imaging reveals dissociation between caspase activation and acute neuronal death in tangle-bearing neurons
    • 18216194 1:CAS:528:DC%2BD1cXhs1CmtLo%3D
    • Spires-Jones TL, de Calignon A, Matsui T, Zehr C, Pitstick R et al (2008) In vivo imaging reveals dissociation between caspase activation and acute neuronal death in tangle-bearing neurons. J Neurosci 28:862-867
    • (2008) J Neurosci , vol.28 , pp. 862-867
    • Spires-Jones, T.L.1    De Calignon, A.2    Matsui, T.3    Zehr, C.4    Pitstick, R.5
  • 80
    • 79955646293 scopus 로고    scopus 로고
    • Hyperphosphorylated truncated protein tau induces caspase-3 independent apoptosis-like pathway in the Alzheimer's disease cellular model
    • 20966551 1:CAS:528:DC%2BC3MXitlygsQ%3D%3D
    • Zilkova M, Zilka N, Kovac A, Kovacech B, Skrabana R, Skrabanova M, Novak M (2011) Hyperphosphorylated truncated protein tau induces caspase-3 independent apoptosis-like pathway in the Alzheimer's disease cellular model. J Alzheimers Dis 23:161-169
    • (2011) J Alzheimers Dis , vol.23 , pp. 161-169
    • Zilkova, M.1    Zilka, N.2    Kovac, A.3    Kovacech, B.4    Skrabana, R.5    Skrabanova, M.6    Novak, M.7
  • 82
    • 0031918640 scopus 로고    scopus 로고
    • Intranuclear neuronal inclusions in Huntington's disease and dentatorubral and pallidoluysian atrophy: Correlation between the density of inclusions and IT15 CAG triplet repeat length
    • 9666478 1:CAS:528:DyaK1cXjtFSqurs%3D
    • Becher MW, Kotzuk JA, Sharp AH, Davies SW, Bates GP, Price DL, Ross C (1998) Intranuclear neuronal inclusions in Huntington's disease and dentatorubral and pallidoluysian atrophy: Correlation between the density of inclusions and IT15 CAG triplet repeat length. Neurobiol Dis 4:387-397
    • (1998) Neurobiol Dis , vol.4 , pp. 387-397
    • Becher, M.W.1    Kotzuk, J.A.2    Sharp, A.H.3    Davies, S.W.4    Bates, G.P.5    Price, D.L.6    Ross, C.7
  • 83
    • 0032502715 scopus 로고    scopus 로고
    • Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract
    • 9535906 1:CAS:528:DyaK1cXis1ers7g%3D
    • Wellington CL, Ellerby LM, Hackam AS, Margolis RL, Trifiro MA et al (1998) Caspase cleavage of gene products associated with triplet expansion disorders generates truncated fragments containing the polyglutamine tract. J Biol Chem 273:9158-6917
    • (1998) J Biol Chem , vol.273 , pp. 9158-6917
    • Wellington, C.L.1    Ellerby, L.M.2    Hackam, A.S.3    Margolis, R.L.4    Trifiro, M.A.5
  • 84
    • 0033037919 scopus 로고    scopus 로고
    • Huntington's disease intranuclear inclusions contain truncated, ubiquitinated huntingtin protein
    • 10192780 1:CAS:528:DyaK1MXis1Cjs7Y%3D
    • Sieradzan KA, Mechan AO, Jones L, Wanker EE, Nukina N, Mann DM (1999) Huntington's disease intranuclear inclusions contain truncated, ubiquitinated huntingtin protein. Exp Neurol 156:92-99
    • (1999) Exp Neurol , vol.156 , pp. 92-99
    • Sieradzan, K.A.1    Mechan, A.O.2    Jones, L.3    Wanker, E.E.4    Nukina, N.5    Mann, D.M.6
  • 85
    • 0037380956 scopus 로고    scopus 로고
    • Aggregate formation and the impairment of long-term synaptic facilitation by ectopic expression of mutant huntingtin in Aplysia neurons
    • 12641738 1:CAS:528:DC%2BD3sXislOlurw%3D
    • Lee JA, Lim CS, Lee SH, Kim H, Nukina N, Kaang BK (2003) Aggregate formation and the impairment of long-term synaptic facilitation by ectopic expression of mutant huntingtin in Aplysia neurons. J Neurochem 85:160-169
    • (2003) J Neurochem , vol.85 , pp. 160-169
    • Lee, J.A.1    Lim, C.S.2    Lee, S.H.3    Kim, H.4    Nukina, N.5    Kaang, B.K.6
  • 86
    • 17344363559 scopus 로고    scopus 로고
    • Length of huntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates
    • 9462744 1:CAS:528:DyaK1cXos1Slsg%3D%3D
    • Martindale D, Hackam A, Wieczorek A, Ellerby L, Wellington C et al (1998) Length of huntingtin and its polyglutamine tract influences localization and frequency of intracellular aggregates. Nat Genet 18:150-154
    • (1998) Nat Genet , vol.18 , pp. 150-154
    • Martindale, D.1    Hackam, A.2    Wieczorek, A.3    Ellerby, L.4    Wellington, C.5
  • 87
    • 7144253143 scopus 로고    scopus 로고
    • Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture
    • 9536081 1:CAS:528:DyaK1cXjsVaksLY%3D
    • Cooper JK, Schilling G, Peters MF, Herring WJ, Sharp AH et al (1998) Truncated N-terminal fragments of huntingtin with expanded glutamine repeats form nuclear and cytoplasmic aggregates in cell culture. Hum Mol Genet 7:783-790
    • (1998) Hum Mol Genet , vol.7 , pp. 783-790
    • Cooper, J.K.1    Schilling, G.2    Peters, M.F.3    Herring, W.J.4    Sharp, A.H.5
  • 88
    • 0033617402 scopus 로고    scopus 로고
    • Involvement of caspases in proteolytic cleavage of Alzheimer's b-amyloid precursor protein and amyloidogenic b-peptide formation
    • 10319819 1:CAS:528:DyaK1MXjtVKltbs%3D
    • Gervais F, Xu D, Robertson G, Vaillancourt J, Zhu Y et al (1999) Involvement of caspases in proteolytic cleavage of Alzheimer's b-amyloid precursor protein and amyloidogenic b-peptide formation. Cell 97:395-406
    • (1999) Cell , vol.97 , pp. 395-406
    • Gervais, F.1    Xu, D.2    Robertson, G.3    Vaillancourt, J.4    Zhu, Y.5
  • 89
    • 58149497521 scopus 로고    scopus 로고
    • Biochemistry and molecular biology of amyloid beta-protein and the mechanism of Alzheimer's disease
    • 18631749
    • Selkoe DJ (2008) Biochemistry and molecular biology of amyloid beta-protein and the mechanism of Alzheimer's disease. Handb Clin Neurol 89:245-260
    • (2008) Handb Clin Neurol , vol.89 , pp. 245-260
    • Selkoe, D.J.1
  • 90
    • 77952515576 scopus 로고    scopus 로고
    • An overview of APP processing enzymes and products
    • 1:CAS:528:DC%2BC3cXislyktrs%3D
    • Chow VW, Mattson MP, Wong PC, Gleichmann M (2010) An overview of APP processing enzymes and products. Neuromol Med 12:1-12
    • (2010) Neuromol Med , vol.12 , pp. 1-12
    • Chow, V.W.1    Mattson, M.P.2    Wong, P.C.3    Gleichmann, M.4
  • 91
    • 33748283747 scopus 로고    scopus 로고
    • Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction
    • Devi L, Prabhu BM, Galati DF, Avadhani NG, Anandatheerthavarada HK (2006). Accumulation of amyloid precursor protein in the mitochondrial import channels of human Alzheimer's disease brain is associated with mitochondrial dysfunction. J Neurosci 26:9057-9068
    • (2006) J Neurosci , vol.26 , pp. 9057-9068
    • Devi, L.1    Prabhu, B.M.2    Galati, D.F.3    Avadhani, N.G.4    Anandatheerthavarada, H.K.5
  • 92
    • 0031941058 scopus 로고    scopus 로고
    • Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies
    • 9546347 1:CAS:528:DyaK1cXivVKgsbc%3D
    • Baba M, Nakajo S, Tu PH, Tomita T, Nakaya K, Lee VM, Trojanowski JQ, Iwatsubo T (1998) Aggregation of alpha-synuclein in Lewy bodies of sporadic Parkinson's disease and dementia with Lewy bodies. Am J Pathol 152:879-884
    • (1998) Am J Pathol , vol.152 , pp. 879-884
    • Baba, M.1    Nakajo, S.2    Tu, P.H.3    Tomita, T.4    Nakaya, K.5    Lee, V.M.6    Trojanowski, J.Q.7    Iwatsubo, T.8
  • 93
    • 33749570292 scopus 로고    scopus 로고
    • Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease
    • Anderson JP, Walker DE, Goldstein JM, de Laat R, Banducci K et al (2000) Phosphorylation of Ser-129 is the dominant pathological modification of alpha-synuclein in familial and sporadic Lewy body disease. J Biol Chem 281:29739-29752
    • (2000) J Biol Chem , vol.281 , pp. 29739-29752
    • Anderson, J.P.1    Walker, D.E.2    Goldstein, J.M.3    De Laat, R.4    Banducci, K.5
  • 94
    • 0035163412 scopus 로고    scopus 로고
    • The solubility of alpha-synuclein in multiple system atrophy differs from that of dementia with Lewy bodies and Parkinson's disease
    • 11145981 1:CAS:528:DC%2BD3MXhtVGlsL8%3D
    • Campbell BC, McLean CA, Culvenor JG, Gai WP, Blumbergs PC et al (2001) The solubility of alpha-synuclein in multiple system atrophy differs from that of dementia with Lewy bodies and Parkinson's disease. J Neurochem 76:87-96
    • (2001) J Neurochem , vol.76 , pp. 87-96
    • Campbell, B.C.1    McLean, C.A.2    Culvenor, J.G.3    Gai, W.P.4    Blumbergs, P.C.5
  • 95
    • 8544264002 scopus 로고    scopus 로고
    • Impact of the acidic C-terminal region comprising amino acids 109-140 on alphasynuclein aggregation in vitro
    • 15610017 1:CAS:528:DC%2BD2cXhtVaisr3N
    • Hoyer W, Cherny D, Subramaniam V, Jovin TM (2004) Impact of the acidic C-terminal region comprising amino acids 109-140 on alphasynuclein aggregation in vitro. Biochemistry 43:16233-16242
    • (2004) Biochemistry , vol.43 , pp. 16233-16242
    • Hoyer, W.1    Cherny, D.2    Subramaniam, V.3    Jovin, T.M.4
  • 96
    • 21644446495 scopus 로고    scopus 로고
    • Proteolytic cleavage of extracellular secreted α-synuclein via matrix metalloproteinases
    • 15863497 1:CAS:528:DC%2BD2MXlsFyqtLo%3D
    • Sung JY, Park SM, Lee CH, Um JW, Lee HJ et al (2005) Proteolytic cleavage of extracellular secreted α-synuclein via matrix metalloproteinases. J Biol Chem 280:25216-25224
    • (2005) J Biol Chem , vol.280 , pp. 25216-25224
    • Sung, J.Y.1    Park, S.M.2    Lee, C.H.3    Um, J.W.4    Lee, H.J.5
  • 97
    • 13844320376 scopus 로고    scopus 로고
    • Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations
    • 15684072 1:CAS:528:DC%2BD2MXhvFGqs7g%3D
    • Li W, West N, Colla E, Pletnikova O, Troncoso JC et al (2005) Aggregation promoting C-terminal truncation of alpha-synuclein is a normal cellular process and is enhanced by the familial Parkinson's disease-linked mutations. Proc Natl Acad Sci USA 102:2162-2167
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2162-2167
    • Li, W.1    West, N.2    Colla, E.3    Pletnikova, O.4    Troncoso, J.C.5
  • 98
    • 79960712793 scopus 로고    scopus 로고
    • Conserved C-terminal charge exerts a profound influence on the aggregation rate of α-synuclein
    • 21689664 1:CAS:528:DC%2BC3MXpt1ygtrw%3D
    • Levitan K, Chereau D, Cohen SI, Knowles TP, Dobson CM et al (2011) Conserved C-terminal charge exerts a profound influence on the aggregation rate of α-synuclein. J Mol Biol 411:329-333
    • (2011) J Mol Biol , vol.411 , pp. 329-333
    • Levitan, K.1    Chereau, D.2    Cohen, S.I.3    Knowles, T.P.4    Dobson, C.M.5
  • 99
    • 34548341065 scopus 로고    scopus 로고
    • The effect of truncated human alpha-synuclein (1-120) on dopaminergic cells in a transgenic mouse model of Parkinson's disease
    • 17708336 1:STN:280:DC%2BD2svovFOhsQ%3D%3D
    • Michell AW, Tofaris GK, Gossage H, Tyers P, Spillantini MG, Barker RA (2007) The effect of truncated human alpha-synuclein (1-120) on dopaminergic cells in a transgenic mouse model of Parkinson's disease. Cell Transplant 16:461-474
    • (2007) Cell Transplant , vol.16 , pp. 461-474
    • Michell, A.W.1    Tofaris, G.K.2    Gossage, H.3    Tyers, P.4    Spillantini, M.G.5    Barker, R.A.6
  • 100
    • 69049119262 scopus 로고    scopus 로고
    • Conditional transgenic mice expressing C-terminally truncated human α-synuclein (αSyn119) exhibit reduced striatal dopamine without loss of nigrostriatal pathway dopaminergic neurons
    • 10.1186/1750-1326-4-34 19630976
    • Daher JPL, Ying M, Banerjee R, McDonald RS, Hahn MD et al (2009) Conditional transgenic mice expressing C-terminally truncated human α-synuclein (αSyn119) exhibit reduced striatal dopamine without loss of nigrostriatal pathway dopaminergic neurons. Mol Neurodegener 4:34. doi: 10.1186/1750-1326-4-34
    • (2009) Mol Neurodegener , vol.4 , pp. 34
    • Daher, J.P.L.1    Ying, M.2    Banerjee, R.3    McDonald, R.S.4    Hahn, M.D.5
  • 101
    • 0034712918 scopus 로고    scopus 로고
    • Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation
    • 10781096 1:CAS:528:DC%2BD3cXivFKju7k%3D
    • Serpell LC, Berriman J, Jakes R, Goedert M, Crowther RA (2000) Fiber diffraction of synthetic α-synuclein filaments shows amyloid-like cross-β conformation. Proc Natl Acad Sci USA 97:4897-4902
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 4897-4902
    • Serpell, L.C.1    Berriman, J.2    Jakes, R.3    Goedert, M.4    Crowther, R.A.5
  • 102
    • 46749138739 scopus 로고    scopus 로고
    • Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • 18535185 1:CAS:528:DC%2BD1cXptVGqu7o%3D
    • Igaz LM, Kwong LK, Xu Y, Truax AC, Uryu K, Neumann M et al (2008) Enrichment of C-terminal fragments in TAR DNA-binding protein-43 cytoplasmic inclusions in brain but not in spinal cord of frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Am J Pathol 173:182-194
    • (2008) Am J Pathol , vol.173 , pp. 182-194
    • Igaz, L.M.1    Kwong, L.K.2    Xu, Y.3    Truax, A.C.4    Uryu, K.5    Neumann, M.6
  • 103
    • 67649797399 scopus 로고    scopus 로고
    • Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 proteinopathies
    • 19164285 1:CAS:528:DC%2BD1MXjsVSitr4%3D
    • Igaz LM, Kwong LK, Chen-Plotkin A, Winton MJ, Unger TL et al (2009) Expression of TDP-43 C-terminal fragments in vitro recapitulates pathological features of TDP-43 proteinopathies. J Biol Chem 284:8516-8524
    • (2009) J Biol Chem , vol.284 , pp. 8516-8524
    • Igaz, L.M.1    Kwong, L.K.2    Chen-Plotkin, A.3    Winton, M.J.4    Unger, T.L.5
  • 104
    • 33845480311 scopus 로고    scopus 로고
    • Caspase substrates
    • 17082814 1:CAS:528:DC%2BD28XhtlSqur%2FE
    • Timmer JC, Salvesan GS (2007) Caspase substrates. Cell Death Differ 14:66-72
    • (2007) Cell Death Differ , vol.14 , pp. 66-72
    • Timmer, J.C.1    Salvesan, G.S.2
  • 105
    • 2442718801 scopus 로고    scopus 로고
    • On the sequential determinants of calpain cleavage
    • 14988399 1:CAS:528:DC%2BD2cXjvV2ns7s%3D
    • Tompa P et al (2004) On the sequential determinants of calpain cleavage. J Biol Chem 279:20775-20785
    • (2004) J Biol Chem , vol.279 , pp. 20775-20785
    • Tompa, P.1
  • 106
    • 2442631459 scopus 로고    scopus 로고
    • Inhibition of calpain cleavage of huntingtin reduces toxicity: Accumulation of calpain/caspase fragments in the nucleus
    • 14981075 1:CAS:528:DC%2BD2cXjs1Whtb8%3D
    • Gafni J, Hermel E, Young JE, Wellington CL, Hayden MR, Ellerby LM (2004) Inhibition of calpain cleavage of huntingtin reduces toxicity: Accumulation of calpain/caspase fragments in the nucleus. J Biol Chem 279:20211-20220
    • (2004) J Biol Chem , vol.279 , pp. 20211-20220
    • Gafni, J.1    Hermel, E.2    Young, J.E.3    Wellington, C.L.4    Hayden, M.R.5    Ellerby, L.M.6
  • 107
    • 0028785672 scopus 로고
    • Calpain induced proteolysis of normal human tau and tau associated with paired helical filaments
    • 7588778 1:CAS:528:DyaK2MXptVChtbY%3D
    • Yang LS, Ksiezak-Reding H (1995) Calpain induced proteolysis of normal human tau and tau associated with paired helical filaments. Eur J Biochem 233:9-17
    • (1995) Eur J Biochem , vol.233 , pp. 9-17
    • Yang, L.S.1    Ksiezak-Reding, H.2
  • 108
    • 33750151957 scopus 로고    scopus 로고
    • Calpain-resistant fragment(s) of alpha-synuclein regulates the synuclein-cleaving activity of 20S proteasome
    • 1:CAS:528:DC%2BD28XhtFertbfF
    • Kim HJ, Lee D, Lee CH, Chung KC, Kim J, Paik SR (2006) Calpain-resistant fragment(s) of alpha-synuclein regulates the synuclein-cleaving activity of 20S proteasome. Arch Biochem Biophy 455:40-47
    • (2006) Arch Biochem Biophy , vol.455 , pp. 40-47
    • Kim, H.J.1    Lee, D.2    Lee, C.H.3    Chung, K.C.4    Kim, J.5    Paik, S.R.6
  • 110
    • 0009744392 scopus 로고    scopus 로고
    • Nuclear accumulation of truncated atrophin-1 fragments in a transgenic mouse model of DRPLA
    • 10677044 1:CAS:528:DyaK1MXmsVOrs7c%3D
    • Schilling G, Wood JD, Duan K, Slunt HH, Gonzales V et al (1999) Nuclear accumulation of truncated atrophin-1 fragments in a transgenic mouse model of DRPLA. Neuron 24:275-286
    • (1999) Neuron , vol.24 , pp. 275-286
    • Schilling, G.1    Wood, J.D.2    Duan, K.3    Slunt, H.H.4    Gonzales, V.5
  • 112
    • 45149107487 scopus 로고    scopus 로고
    • Mechanisms of neurodegeneration in Huntington's disease
    • 18588526
    • Gil JM, Rego AC (2008) Mechanisms of neurodegeneration in Huntington's disease. Eur J Neurosci 27:2803-2820
    • (2008) Eur J Neurosci , vol.27 , pp. 2803-2820
    • Gil, J.M.1    Rego, A.C.2
  • 114
    • 0032475931 scopus 로고    scopus 로고
    • Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions
    • 9778247 1:CAS:528:DyaK1cXmslWlsrs%3D
    • Saudou F, Finkbeiner S, Devys D, Greenberg ME (1998) Huntingtin acts in the nucleus to induce apoptosis but death does not correlate with the formation of intranuclear inclusions. Cell 95:55-66
    • (1998) Cell , vol.95 , pp. 55-66
    • Saudou, F.1    Finkbeiner, S.2    Devys, D.3    Greenberg, M.E.4
  • 115
    • 7244236320 scopus 로고    scopus 로고
    • Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death
    • 15483602 1:CAS:528:DC%2BD2cXotl2ktrc%3D
    • Arrasate M, Mitra S, Schweitzer ES, Segal MR, Finkbeiner S (2004) Inclusion body formation reduces levels of mutant huntingtin and the risk of neuronal death. Nature 431:805-810
    • (2004) Nature , vol.431 , pp. 805-810
    • Arrasate, M.1    Mitra, S.2    Schweitzer, E.S.3    Segal, M.R.4    Finkbeiner, S.5
  • 116
    • 32644467781 scopus 로고    scopus 로고
    • Oxidative stress induces nuclear translocation of C-terminus of alpha-synuclein in dopaminergic cells
    • 16480958 1:CAS:528:DC%2BD28Xhs1Wlsrs%3D
    • Xu S, Zhou M, Yu S, Cai Y, Zhang A, Uéda K, Chan P (2006) Oxidative stress induces nuclear translocation of C-terminus of alpha-synuclein in dopaminergic cells. Biochem Biophys Res Commun 342:330-335
    • (2006) Biochem Biophys Res Commun , vol.342 , pp. 330-335
    • Xu, S.1    Zhou, M.2    Yu, S.3    Cai, Y.4    Zhang, A.5    Uéda, K.6    Chan, P.7
  • 117
    • 33749632259 scopus 로고    scopus 로고
    • Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis
    • 17023659 1:CAS:528:DC%2BD28XhtVCiurrL
    • Neumann M, Sampathu DM, Kwong LK, Truax AD, Micsenyi MC et al (2006) Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis. Science 314:130-133
    • (2006) Science , vol.314 , pp. 130-133
    • Neumann, M.1    Sampathu, D.M.2    Kwong, L.K.3    Truax, A.D.4    Micsenyi, M.C.5
  • 118
    • 79956304001 scopus 로고    scopus 로고
    • A "two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport
    • 21454607 1:CAS:528:DC%2BC3MXmtlGltbw%3D
    • Pesiridis GS, Tripathy K, Tanik S, Trojanowski JQ, Lee VM (2011) A "two-hit" hypothesis for inclusion formation by carboxyl-terminal fragments of TDP-43 protein linked to RNA depletion and impaired microtubule-dependent transport. J Biol Chem 286:18845-18855
    • (2011) J Biol Chem , vol.286 , pp. 18845-18855
    • Pesiridis, G.S.1    Tripathy, K.2    Tanik, S.3    Trojanowski, J.Q.4    Lee, V.M.5
  • 119
    • 0032517816 scopus 로고    scopus 로고
    • Recruitment and the role of nuclear localization in polyglutamine- mediated aggregation
    • 9852144 1:CAS:528:DyaK1MXlsA%3D%3D
    • Perez MK, Paulson HL, Pendse SJ, Saionz SJ, Bonini NM, Pittman RN (1998) Recruitment and the role of nuclear localization in polyglutamine-mediated aggregation. J Cell Biol 143:1457-1470
    • (1998) J Cell Biol , vol.143 , pp. 1457-1470
    • Perez, M.K.1    Paulson, H.L.2    Pendse, S.J.3    Saionz, S.J.4    Bonini, N.M.5    Pittman, R.N.6
  • 120
    • 0030774852 scopus 로고    scopus 로고
    • Degradation of tau by lysosomal enzyme cathepsin D: Implication for Alzheimer neurofibrillary degeneration
    • 9349548 1:CAS:528:DyaK2sXmvVKktr0%3D
    • Kenessey A, Nacharaju P, Ko LW, Yen SH (1997) Degradation of tau by lysosomal enzyme cathepsin D: Implication for Alzheimer neurofibrillary degeneration. J Neurochem 69:2026-2038
    • (1997) J Neurochem , vol.69 , pp. 2026-2038
    • Kenessey, A.1    Nacharaju, P.2    Ko, L.W.3    Yen, S.H.4
  • 121
    • 68549111280 scopus 로고    scopus 로고
    • The lysozome and neurodegenerative diseases
    • 19499146 1:CAS:528:DC%2BD1MXntF2gtr4%3D
    • Zhang L, Sheng R, Qin Z (2009) The lysozome and neurodegenerative diseases. Acta Biochim Biophys Sin 41:437-445
    • (2009) Acta Biochim Biophys Sin , vol.41 , pp. 437-445
    • Zhang, L.1    Sheng, R.2    Qin, Z.3
  • 123
    • 0034903587 scopus 로고    scopus 로고
    • The calpain family and human disease
    • 11516996 1:CAS:528:DC%2BD3MXmtFaks7c%3D
    • Huang Y, Wang KK (2001) The calpain family and human disease. Trends Mol Med 7:355-362
    • (2001) Trends Mol Med , vol.7 , pp. 355-362
    • Huang, Y.1    Wang, K.K.2
  • 124
    • 0024407571 scopus 로고
    • Calmodulin-binding proteins as calpain substrates
    • 1:CAS:528:DyaL1MXlvV2qsLw%3D
    • Wang KK, Villalobo A, Roufogalis BD (1989) Calmodulin-binding proteins as calpain substrates. J Biol Chem 262:693-706
    • (1989) J Biol Chem , vol.262 , pp. 693-706
    • Wang, K.K.1    Villalobo, A.2    Roufogalis, B.D.3
  • 125
    • 0033954643 scopus 로고    scopus 로고
    • The sensitivity of c-Jun and c-Fos proteins to calpains depends on conformational determinants of the monomers and not on formation of dimers
    • Pariat M et al (2001) The sensitivity of c-Jun and c-Fos proteins to calpains depends on conformational determinants of the monomers and not on formation of dimers. Biochem J 345(pt1):129-138
    • (2001) Biochem J , vol.345 , Issue.PART1 , pp. 129-138
    • Pariat, M.1
  • 126
    • 0021683468 scopus 로고
    • Comparative specificity and kinetic studies on porcine calpain i and calpain II with naturally occurring peptides and synthetic fluorogenic substrates
    • 6092335 1:CAS:528:DyaL2MXhsVGhtLY%3D
    • Sasaki T, Kikuchi T, Yumoto N, Yoshimura N, Murachi T (1984) Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates. J Biol Chem 259:12489-12494
    • (1984) J Biol Chem , vol.259 , pp. 12489-12494
    • Sasaki, T.1    Kikuchi, T.2    Yumoto, N.3    Yoshimura, N.4    Murachi, T.5
  • 128
    • 0027474051 scopus 로고
    • A. Wide spread activation of calpain activated neutral proteinase (calpain) in brain in Alzheimer's disease: A potential molecular basis for neuronal degeneration
    • 8464868 1:CAS:528:DyaK3sXisFamu74%3D
    • Saito K, Elce JS, Hamos JE, Nixon R (1993) A. wide spread activation of calpain activated neutral proteinase (calpain) in brain in Alzheimer's disease: A potential molecular basis for neuronal degeneration. Proc Natl Acad Sci USA 90:2628-2632
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 2628-2632
    • Saito, K.1    Elce, J.S.2    Hamos, J.E.3    Nixon, R.4
  • 129
    • 0030836467 scopus 로고    scopus 로고
    • Active site-directed antibodies identify calpain II as an early-appearing and pervasive component of neurofibrillary pathology in Alzheimer's disease
    • 9296555 1:CAS:528:DyaK2sXksFantb0%3D
    • Grynspan F, Griffin WR, Cataldo A, Katayama S, Nixon RA (1997) Active site-directed antibodies identify calpain II as an early-appearing and pervasive component of neurofibrillary pathology in Alzheimer's disease. Brain Res 763:145-158
    • (1997) Brain Res , vol.763 , pp. 145-158
    • Grynspan, F.1    Griffin, W.R.2    Cataldo, A.3    Katayama, S.4    Nixon, R.A.5
  • 130
    • 20044370830 scopus 로고    scopus 로고
    • The generation of a 17 kDa neurotoxic fragment: An alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration
    • 15930385 1:CAS:528:DC%2BD2MXlt1ygu7o%3D
    • Park SY, Ferreira A (2005) The generation of a 17 kDa neurotoxic fragment: An alternative mechanism by which tau mediates beta-amyloid-induced neurodegeneration. J Neurosci 25:5365-5375
    • (2005) J Neurosci , vol.25 , pp. 5365-5375
    • Park, S.Y.1    Ferreira, A.2
  • 131
    • 79960735446 scopus 로고    scopus 로고
    • Calpain-mediated tau cleavage: A mechanism leading to neurodegeneration shared by multiple tauopathies
    • 21442128 1:CAS:528:DC%2BC3MXhtVemurzK
    • Ferreira A, Bigio EH (2011) Calpain-mediated tau cleavage: A mechanism leading to neurodegeneration shared by multiple tauopathies. Mol Med 17:676-685
    • (2011) Mol Med , vol.17 , pp. 676-685
    • Ferreira, A.1    Bigio, E.H.2
  • 133
    • 0028987849 scopus 로고
    • Inhibition of beta-amyloid formation identifies proteolytic precursors and subcellular site of catabolism
    • 7695912 1:CAS:528:DyaK2MXkvVegtbo%3D
    • Higaki J, Quon D, Zhong Z, Cordell B (1995) Inhibition of beta-amyloid formation identifies proteolytic precursors and subcellular site of catabolism. Neuron 14:651-659
    • (1995) Neuron , vol.14 , pp. 651-659
    • Higaki, J.1    Quon, D.2    Zhong, Z.3    Cordell, B.4
  • 134
    • 0000732988 scopus 로고
    • Protein-structure and intracellular stability
    • 1:CAS:528:DyaL2sXmtlWmsLY%3D
    • Rechsteiner M, Rogers S, Rote K (1987) Protein-structure and intracellular stability. Trends Biochem Sci 12:390-394
    • (1987) Trends Biochem Sci , vol.12 , pp. 390-394
    • Rechsteiner, M.1    Rogers, S.2    Rote, K.3
  • 135
    • 33644895682 scopus 로고    scopus 로고
    • Calpain inhibitor MDL 28170 modulates A β formation by inhibiting the formation of intermediate Aβ46 and protecting A β from degradation
    • doi: 10.1096/fj.05-4524fje
    • Dong Y, Tan J, Cui MZ, Zhao G, Mao G, Singh N, Xu X (2005) Calpain inhibitor MDL 28170 modulates A β formation by inhibiting the formation of intermediate Aβ46 and protecting A β from degradation. FASEB J. doi: 10.1096/fj.05-4524fje
    • (2005) FASEB J
    • Dong, Y.1    Tan, J.2    Cui, M.Z.3    Zhao, G.4    Mao, G.5    Singh, N.6    Xu, X.7
  • 136
    • 0033034785 scopus 로고    scopus 로고
    • Distinct secretases, a cysteine protease and a serine protease, generate the C termini of amyloid b-proteins Ab1-40 and Ab1-42, respectively J
    • 1:CAS:528:DyaK1MXitFCks78%3D
    • Figueiredo-Pereira ME, Efthimiopoulos S, Tezapsidis N, Buku GJ, Mehta P, Robakis NK (1999) Distinct secretases, a cysteine protease and a serine protease, generate the C termini of amyloid b-proteins Ab1-40 and Ab1-42, respectively J. Neurochem 72:1417-1422
    • (1999) Neurochem , vol.72 , pp. 1417-1422
    • Figueiredo-Pereira, M.E.1    Efthimiopoulos, S.2    Tezapsidis, N.3    Buku, G.J.4    Mehta, P.5    Robakis, N.K.6
  • 138
    • 0033103523 scopus 로고    scopus 로고
    • Caspase-8 is required for cell death induced by expanded polyglutamine repeats
    • 10197541 1:CAS:528:DyaK1MXit1emt7o%3D
    • Sanchez I, Xu CJ, Juo P, Kakizaka A, Blenis J, Yuan J (1999) Caspase-8 is required for cell death induced by expanded polyglutamine repeats. Neuron 22:623-633
    • (1999) Neuron , vol.22 , pp. 623-633
    • Sanchez, I.1    Xu, C.J.2    Juo, P.3    Kakizaka, A.4    Blenis, J.5    Yuan, J.6
  • 139
    • 0033136692 scopus 로고    scopus 로고
    • A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration
    • 10402204 1:CAS:528:DyaK1MXjvVSjurw%3D
    • Hodgson JG, Agopyan N, Gutekunst CA, Leavitt BR, LePiane F et al (1999) A YAC mouse model for Huntington's disease with full-length mutant huntingtin, cytoplasmic toxicity, and selective striatal neurodegeneration. Neuron 23(1):181-92
    • (1999) Neuron , vol.23 , Issue.1 , pp. 181-192
    • Hodgson, J.G.1    Agopyan, N.2    Gutekunst, C.A.3    Leavitt, B.R.4    Lepiane, F.5
  • 140
    • 0030850412 scopus 로고    scopus 로고
    • Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3
    • 9292723 1:CAS:528:DyaK2sXlvFensL8%3D
    • Paulson HL, Perez MK, Trottier Y, Trojanowski JQ, Subramony SH et al (1997) Intranuclear inclusions of expanded polyglutamine protein in spinocerebellar ataxia type 3. Neuron 19:333-344
    • (1997) Neuron , vol.19 , pp. 333-344
    • Paulson, H.L.1    Perez, M.K.2    Trottier, Y.3    Trojanowski, J.Q.4    Subramony, S.H.5
  • 141
    • 34548329581 scopus 로고    scopus 로고
    • A Mutant Ataxin-3 Fragment results from processing at a site nterminal to amino acid 190 in brain of Machado-Joseph disease-like transgenic mice
    • Gould VFC, Goti D, Pearce D, Gonzalez GA, Gao H et al (2003) A Mutant Ataxin-3 Fragment results from processing at a site nterminal to amino acid 190 in brain of Machado-Joseph disease-like transgenic mice. Neurobiol Dis 27:362-369
    • (2003) Neurobiol Dis , vol.27 , pp. 362-369
    • Gould, V.F.C.1    Goti, D.2    Pearce, D.3    Gonzalez, G.A.4    Gao, H.5
  • 142
    • 0032885388 scopus 로고    scopus 로고
    • Mammalian caspases: Structure, activation, substrates, and functions during apoptosis
    • 10872455 1:CAS:528:DyaK1MXlvFajsb0%3D
    • Earnshaw WC, Martins LM, Kaufmann SH (1999) Mammalian caspases: Structure, activation, substrates, and functions during apoptosis. Annu Rev Biochem 68:383-424
    • (1999) Annu Rev Biochem , vol.68 , pp. 383-424
    • Earnshaw, W.C.1    Martins, L.M.2    Kaufmann, S.H.3
  • 143
    • 0037107151 scopus 로고    scopus 로고
    • Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease
    • 12223539 1:CAS:528:DC%2BD38Xnt12lt7s%3D
    • Wellington CL, Ellerby LM, Gutekunst CA, Rogers D, Warby S et al (2002) Caspase cleavage of mutant huntingtin precedes neurodegeneration in Huntington's disease. J Neurosci 22:7862-7872
    • (2002) J Neurosci , vol.22 , pp. 7862-7872
    • Wellington, C.L.1    Ellerby, L.M.2    Gutekunst, C.A.3    Rogers, D.4    Warby, S.5
  • 144
    • 0347479366 scopus 로고    scopus 로고
    • Accumulation of caspase cleaved amyloid precursor protein represents an early neurodegenerative event in aging and in Alzheimer's disease
    • 14678756 1:CAS:528:DC%2BD3sXpvVWksLg%3D
    • Zhao M, Sua J, Heada E, Cotman CW (2003) Accumulation of caspase cleaved amyloid precursor protein represents an early neurodegenerative event in aging and in Alzheimer's disease. Neurobiol Dis 14:391-403
    • (2003) Neurobiol Dis , vol.14 , pp. 391-403
    • Zhao, M.1    Sua, J.2    Heada, E.3    Cotman, C.W.4
  • 146
    • 0036434880 scopus 로고    scopus 로고
    • Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease
    • 12429193 1:CAS:528:DC%2BD38XotlKisr8%3D
    • Ghoshal N, García-Sierra F, Wuu J, Leurgans S, Bennett DA, Berry RW, Binder LI (2002) Tau conformational changes correspond to impairments of episodic memory in mild cognitive impairment and Alzheimer's disease. Exp Neurol 177:475-493
    • (2002) Exp Neurol , vol.177 , pp. 475-493
    • Ghoshal, N.1    García-Sierra, F.2    Wuu, J.3    Leurgans, S.4    Bennett, D.A.5    Berry, R.W.6    Binder, L.I.7
  • 147
    • 84859732718 scopus 로고    scopus 로고
    • Development of a high-throughput screen targeting caspase-8-mediated cleavage of the amyloid precursor protein
    • 22178911 1:CAS:528:DC%2BC38XhvVWrsrg%3D
    • Hart MJ, Glicksman M, Liu M, Sharma MK, Cuny G, Galvan V (2012) Development of a high-throughput screen targeting caspase-8-mediated cleavage of the amyloid precursor protein. Anal Biochem 421:467-476
    • (2012) Anal Biochem , vol.421 , pp. 467-476
    • Hart, M.J.1    Glicksman, M.2    Liu, M.3    Sharma, M.K.4    Cuny, G.5    Galvan, V.6
  • 149
    • 78149487690 scopus 로고    scopus 로고
    • Cleavage at the 586 amino acid caspase-6 site in mutant huntingtin influences caspase-6 activation in vivo
    • 21068307 1:CAS:528:DC%2BC3cXhsV2nurjP
    • Graham RK, Deng Y, Carroll J, Vaid K, Cowan C et al (2010) Cleavage at
    • (2010) J Neurosci , vol.30 , pp. 15019-15029
    • Graham, R.K.1    Deng, Y.2    Carroll, J.3    Vaid, K.4    Cowan, C.5
  • 150
    • 0344010993 scopus 로고    scopus 로고
    • Sequential activation of individual caspases, and of alterations in Bcl-2 proapoptotic signals in a mouse model of Huntington's disease
    • 14622098 1:CAS:528:DC%2BD3sXps1Ohs7c%3D
    • Zhang Y, Ona VO, Li M, Drozda M, Dubois-Dauphin M et al (2003) Sequential activation of individual caspases, and of alterations in Bcl-2 proapoptotic signals in a mouse model of Huntington's disease. J Neurochem 87:1184-1192
    • (2003) J Neurochem , vol.87 , pp. 1184-1192
    • Zhang, Y.1    Ona, V.O.2    Li, M.3    Drozda, M.4    Dubois-Dauphin, M.5
  • 151
    • 0033912716 scopus 로고    scopus 로고
    • Minocycline inhibits caspase-1 and caspase-3 expression and delays mortality in a transgenic mouse model of Huntington disease
    • 10888929 1:CAS:528:DC%2BD3cXltValtLs%3D
    • Chen M, Ona VO, Li M, Ferrante RJ, Fink KB et al (2000) Minocycline inhibits caspase-1 and caspase-3 expression and delays mortality in a transgenic mouse model of Huntington disease. Nat Med 6:797-801
    • (2000) Nat Med , vol.6 , pp. 797-801
    • Chen, M.1    Ona, V.O.2    Li, M.3    Ferrante, R.J.4    Fink, K.B.5
  • 152
    • 0033588476 scopus 로고    scopus 로고
    • Caspase activation during apoptotic cell death induced by expanded polyglutamine in N2a cells
    • 10574348 1:CAS:528:DyaK1MXlvF2jurs%3D
    • Wang GH, Mitsui K, Kotliarova S, Yamashita A, Nagao Y et al (1999) Caspase activation during apoptotic cell death induced by expanded polyglutamine in N2a cells. Neuroreport 10:2435-2438
    • (1999) Neuroreport , vol.10 , pp. 2435-2438
    • Wang, G.H.1    Mitsui, K.2    Kotliarova, S.3    Yamashita, A.4    Nagao, Y.5
  • 153
    • 0034657112 scopus 로고    scopus 로고
    • Wild-type huntingtin protects from apoptosis upstream of caspase-3
    • 10804212 1:CAS:528:DC%2BD3cXjtlKqsLo%3D
    • Rigamonti D, Bauer JH, De-Fraja C, Conti L, Sipione S et al (2000) Wild-type huntingtin protects from apoptosis upstream of caspase-3. J Neurosci 20:3705-3713
    • (2000) J Neurosci , vol.20 , pp. 3705-3713
    • Rigamonti, D.1    Bauer, J.H.2    De-Fraja, C.3    Conti, L.4    Sipione, S.5
  • 155
    • 0033587128 scopus 로고    scopus 로고
    • Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease
    • 10353249 1:CAS:528:DyaK1MXjsFyqsrs%3D
    • Ona VO, Li M, Vonsattel JP, Andrews LJ, Khan SQ et al (1999) Inhibition of caspase-1 slows disease progression in a mouse model of Huntington's disease. Nature 399:263-267
    • (1999) Nature , vol.399 , pp. 263-267
    • Ona, V.O.1    Li, M.2    Vonsattel, J.P.3    Andrews, L.J.4    Khan, S.Q.5
  • 156
    • 49349104833 scopus 로고    scopus 로고
    • Caspase-Cleaved TAR DNA Binding protein-43 is a major pathological finding in Alzheimer's disease
    • 18634762 1:CAS:528:DC%2BD1cXpvFKgt7Y%3D
    • Rohn TY (2008) Caspase-Cleaved TAR DNA Binding protein-43 is a major pathological finding in Alzheimer's disease. Brain Res 1228:189-198
    • (2008) Brain Res , vol.1228 , pp. 189-198
    • Rohn, T.Y.1
  • 157
    • 2542445545 scopus 로고    scopus 로고
    • Caspase-mediated proteolysis of polyglutamine disease protein ataxin-3
    • 15140190 1:CAS:528:DC%2BD2cXksVyksLc%3D
    • Berke SJS, Schmied FAF, Brunt ER, Ellerby LM, Paulson HL (2004) Caspase-mediated proteolysis of polyglutamine disease protein ataxin-3. J Neurochem 89:908-918
    • (2004) J Neurochem , vol.89 , pp. 908-918
    • Berke, S.J.S.1    Schmied, F.A.F.2    Brunt, E.R.3    Ellerby, L.M.4    Paulson, H.L.5
  • 158
    • 77953426148 scopus 로고    scopus 로고
    • Caspase-cleaved TAR DNA-binding protein-43 in Pick's disease
    • Rohn TT, Kokoulina P (2009) Caspase-cleaved TAR DNA-binding protein-43 in Pick's disease. Int J Physio Pathophysio Pharmacol 20:24-31
    • (2009) Int J Physio Pathophysio Pharmacol , vol.20 , pp. 24-31
    • Rohn, T.T.1    Kokoulina, P.2
  • 159
    • 34848921202 scopus 로고    scopus 로고
    • Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43
    • 17898224 1:CAS:528:DC%2BD2sXhtFGmt7fO
    • Zhang YJ, Xu YF, Dickey CA, Buratti E, Baralle F et al (2007) Progranulin mediates caspase-dependent cleavage of TAR DNA binding protein-43. J Neurosci 27:10530-10534
    • (2007) J Neurosci , vol.27 , pp. 10530-10534
    • Zhang, Y.J.1    Xu, Y.F.2    Dickey, C.A.3    Buratti, E.4    Baralle, F.5
  • 160
    • 44049097065 scopus 로고    scopus 로고
    • A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity
    • 18434538 1:CAS:528:DC%2BD1cXlsFGku70%3D
    • Johnson BS, McCaffery M, Lindquist S, Gitler AD (2008) A yeast TDP-43 proteinopathy model: Exploring the molecular determinants of TDP-43 aggregation and cellular toxicity. Proc Natl Acad Sci USA 105:6439-6444
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6439-6444
    • Johnson, B.S.1    McCaffery, M.2    Lindquist, S.3    Gitler, A.D.4
  • 161
    • 0026637316 scopus 로고
    • Structure and function of the mannose 6-phosphate/insulin like growth factor II receptors
    • 1323236 1:CAS:528:DyaK38Xlt1Cmtb8%3D
    • Kornfeld S (1992) Structure and function of the mannose 6-phosphate/insulin like growth factor II receptors. Ann Rev Biochem 61:307-330
    • (1992) Ann Rev Biochem , vol.61 , pp. 307-330
    • Kornfeld, S.1
  • 162
    • 0025195944 scopus 로고
    • Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain
    • 1692625 1:CAS:528:DyaK3cXkt1WksLk%3D
    • Cataldo AM, Nixon RA (1990) Enzymatically active lysosomal proteases are associated with amyloid deposits in Alzheimer brain. Proc Natl Acad Sci USA 87:3861-3865
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3861-3865
    • Cataldo, A.M.1    Nixon, R.A.2
  • 163
    • 0026327404 scopus 로고
    • Lysosomal hydrolases of different classes are abnormally distributed in Alzheimer brain
    • 1837142 1:CAS:528:DyaK38XhtVeks78%3D
    • Cataldo AM, Paskevich PA, Kominami E, Nixon RA (1991) Lysosomal hydrolases of different classes are abnormally distributed in Alzheimer brain. Proc Natl Acad Sci USA 88:10998-11002
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10998-11002
    • Cataldo, A.M.1    Paskevich, P.A.2    Kominami, E.3    Nixon, R.A.4
  • 164
    • 0028220243 scopus 로고
    • Lysosomal abnormalities in degenerating neurons link neuronal compromise to senile plaque development in Alzheimer's disease
    • 8004466 1:CAS:528:DyaK2cXisVWksbg%3D
    • Cataldo AM, Hamilton DJ, Nixon RA (1994) Lysosomal abnormalities in degenerating neurons link neuronal compromise to senile plaque development in Alzheimer's disease. Brain Res 640:68-80
    • (1994) Brain Res , vol.640 , pp. 68-80
    • Cataldo, A.M.1    Hamilton, D.J.2    Nixon, R.A.3
  • 165
    • 0028947294 scopus 로고
    • Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system
    • 7695914 1:CAS:528:DyaK2MXkvVegtbg%3D
    • Cataldo AM, Barnett JL, Berman SA, Quarless S, Burztajn S, Lippa C, Nixon RA (1995) Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: Evidence for early up-regulation of the endosomal-lysosomal system. Neuron 14:671-680
    • (1995) Neuron , vol.14 , pp. 671-680
    • Cataldo, A.M.1    Barnett, J.L.2    Berman, S.A.3    Quarless, S.4    Burztajn, S.5    Lippa, C.6    Nixon, R.A.7
  • 166
    • 1242316263 scopus 로고    scopus 로고
    • Intracellular accumulation of amyloidogenic fragments of amyloid-β precursor protein in neurons with Niemann-Pick type C defects is associated with endosomal abnormalities
    • 14982851 1:CAS:528:DC%2BD2cXitl2jt7s%3D
    • Jin LW, Maezawa I, Vincent I, Bird T (2004) Intracellular accumulation of amyloidogenic fragments of amyloid-β precursor protein in neurons with Niemann-Pick type C defects is associated with endosomal abnormalities. Am J Pathol 164:975-985
    • (2004) Am J Pathol , vol.164 , pp. 975-985
    • Jin, L.W.1    Maezawa, I.2    Vincent, I.3    Bird, T.4
  • 167
    • 77955661185 scopus 로고    scopus 로고
    • Increased neuronal Rab5 immunoreactive endosomes do not colocalize with TDP-43 in motor neuron disease
    • 20558162 1:CAS:528:DC%2BC3cXhtVersr7L
    • Matej R, Botond G, László L, Kopitar-Jerala N, Rusina R, Budka H, Kovacs GG (2010) Increased neuronal Rab5 immunoreactive endosomes do not colocalize with TDP-43 in motor neuron disease. Exp Neurol 225:133-139
    • (2010) Exp Neurol , vol.225 , pp. 133-139
    • Matej, R.1    Botond, G.2    László, L.3    Kopitar-Jerala, N.4    Rusina, R.5    Budka, H.6    Kovacs, G.G.7
  • 168
    • 33747388358 scopus 로고    scopus 로고
    • Lysosomal system pathways: Genes to neurodegeneration in Alzheimer's disease
    • 16914867 1:CAS:528:DC%2BD28XotFKktL0%3D
    • Nixon RA, Cataldo AM (2006) Lysosomal system pathways: Genes to neurodegeneration in Alzheimer's disease. J Alzheimers Dis 9:277-289
    • (2006) J Alzheimers Dis , vol.9 , pp. 277-289
    • Nixon, R.A.1    Cataldo, A.M.2
  • 169
    • 8044250876 scopus 로고    scopus 로고
    • A possible role for cathepsins D, E, and B in the processing of beta-amyloid precursor protein in Alzheimer's disease
    • 9119007 1:CAS:528:DyaK2sXhvVKlurY%3D
    • Mackay EA, Ehrhard A, Moniatte M, Guenet C, Tardif C et al (1997) A possible role for cathepsins D, E, and B in the processing of beta-amyloid precursor protein in Alzheimer's disease. Eur J Biochem 244:414-425
    • (1997) Eur J Biochem , vol.244 , pp. 414-425
    • Mackay, E.A.1    Ehrhard, A.2    Moniatte, M.3    Guenet, C.4    Tardif, C.5
  • 170
    • 0028168276 scopus 로고
    • Processing of the pre-beta-amyloid protein by cathepsin D is enhanced by a familial Alzheimer's disease mutation
    • 7523115 1:CAS:528:DyaK2cXlslKkuro%3D
    • Dreyer RN, Bausch KM, Fracasso P, Hammond LJ, Wunderlich D et al (1994) Processing of the pre-beta-amyloid protein by cathepsin D is enhanced by a familial Alzheimer's disease mutation. Eur J Biochem 224:265-271
    • (1994) Eur J Biochem , vol.224 , pp. 265-271
    • Dreyer, R.N.1    Bausch, K.M.2    Fracasso, P.3    Hammond, L.J.4    Wunderlich, D.5
  • 172
    • 0027379395 scopus 로고
    • Characterization of beta-amyloid peptide from human cerebrospinal fluid
    • 8229004 1:CAS:528:DyaK3sXms1OhtL0%3D
    • Vigo-Pelfrey C, Lee D, Keim P, Lieberburg I, Schenk DB (1993) Characterization of beta-amyloid peptide from human cerebrospinal fluid. J Neurochem 61:1965-1968
    • (1993) J Neurochem , vol.61 , pp. 1965-1968
    • Vigo-Pelfrey, C.1    Lee, D.2    Keim, P.3    Lieberburg, I.4    Schenk, D.B.5
  • 174
    • 43149100823 scopus 로고    scopus 로고
    • Inhibitors of cathepsin B improve memory and reduce β-amyloid in transgenic Alzheimer disease mice expressing the wild-type, but not the Swedish mutant, β-secretase site of the amyloid precursor protein
    • 18184658 1:CAS:528:DC%2BD1cXjt1els7k%3D
    • Hook VYH, Kindy M, Hook G (2008) Inhibitors of cathepsin B improve memory and reduce β-amyloid in transgenic Alzheimer disease mice expressing the wild-type, but not the Swedish mutant, β-secretase site of the amyloid precursor protein. J Biol Chem 283:7745-7753
    • (2008) J Biol Chem , vol.283 , pp. 7745-7753
    • Hook, V.Y.H.1    Kindy, M.2    Hook, G.3
  • 175
    • 0028929324 scopus 로고
    • Full-length and truncated APP in chromaffin granules: Solubilization of granule membrane APP by a proteolytic mechanism
    • 7722498 1:CAS:528:DyaK2MXltFygtbY%3D
    • Vassilacopoulou D, Ripellino JA, Tezapsidis N, Hook VYH, Robakis NK (1995) Full-length and truncated APP in chromaffin granules: Solubilization of granule membrane APP by a proteolytic mechanism. J Neurochem 64:2140-2146
    • (1995) J Neurochem , vol.64 , pp. 2140-2146
    • Vassilacopoulou, D.1    Ripellino, J.A.2    Tezapsidis, N.3    Hook, V.Y.H.4    Robakis, N.K.5
  • 176
    • 26844559355 scopus 로고    scopus 로고
    • Inhibition of cathepsin B reduces b-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: Evidence for cathepsin B as a candidate b-secretase of Alzheimer's disease
    • 16164418 1:CAS:528:DC%2BD2MXhtVygs7bM
    • Hook V, Toneff T, Bogyo M, Greenbaum D, Medzihradszky KF et al (2005) Inhibition of cathepsin B reduces b-amyloid production in regulated secretory vesicles of neuronal chromaffin cells: Evidence for cathepsin B as a candidate b-secretase of Alzheimer's disease. Biol Chem 386:931-940
    • (2005) Biol Chem , vol.386 , pp. 931-940
    • Hook, V.1    Toneff, T.2    Bogyo, M.3    Greenbaum, D.4    Medzihradszky, K.F.5
  • 177
    • 34547975971 scopus 로고    scopus 로고
    • Oxidative stress-induced phosphorylation, degradation and aggregation of α-synuclein are linked to upregulated CK2 and cathepsin D
    • 17714183
    • Takahashi M, Ko L, Kulathingal J, Jiang P, Sevlever D, Yen SC (2007) Oxidative stress-induced phosphorylation, degradation and aggregation of α-synuclein are linked to upregulated CK2 and cathepsin D. Eur J Neurosci 26:863-874
    • (2007) Eur J Neurosci , vol.26 , pp. 863-874
    • Takahashi, M.1    Ko, L.2    Kulathingal, J.3    Jiang, P.4    Sevlever, D.5    Yen, S.C.6
  • 178
    • 51549106105 scopus 로고    scopus 로고
    • Cathepsin D is the main lysosomal enzyme involved in the degradation of α-synuclein and generation of its carboxy-terminally truncated species
    • 1:CAS:528:DC%2BD1cXpvFSlsL0%3D
    • Sevlever D, Jiang P, Yen SC (2008) Cathepsin D is the main lysosomal enzyme involved in the degradation of α-synuclein and generation of its carboxy-terminally truncated species. Biochem 47:9678-9687
    • (2008) Biochem , vol.47 , pp. 9678-9687
    • Sevlever, D.1    Jiang, P.2    Yen, S.C.3
  • 179
    • 64949185378 scopus 로고    scopus 로고
    • Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo
    • 10.1186/1756-6606-2-5 19203374
    • Cullen V, Lindfors M, Ng J, Paetau A, Swinton E et al (2009) Cathepsin D expression level affects alpha-synuclein processing, aggregation, and toxicity in vivo. Mol Brain 2:5. doi: 10.1186/1756-6606-2-5
    • (2009) Mol Brain , vol.2 , pp. 5
    • Cullen, V.1    Lindfors, M.2    Ng, J.3    Paetau, A.4    Swinton, E.5
  • 180
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation
    • 3805008 1:CAS:528:DyaL2sXksFyitQ%3D%3D
    • Geiger T, Clarke S (1987) Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. J Biol Chem 262:785-94
    • (1987) J Biol Chem , vol.262 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 181
    • 0026320363 scopus 로고
    • Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins
    • 1678690 1:CAS:528:DyaK3MXlsFeit7w%3D
    • Wright HT (1991) Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Crit Rev Biochem Mol Biol 26:1-52
    • (1991) Crit Rev Biochem Mol Biol , vol.26 , pp. 1-52
    • Wright, H.T.1
  • 182
    • 4544300178 scopus 로고    scopus 로고
    • Molecular aging of tau: Disulfide-independent aggregation and non-enzymatic degradation in vitro and in vivo
    • 15341514 1:CAS:528:DC%2BD2cXnvVGqs7k%3D
    • Watanabe A, Hong WK, Dohmae N, Takio K, Morishima-Kawashima M, Ihara Y (2004) Molecular aging of tau: Disulfide-independent aggregation and non-enzymatic degradation in vitro and in vivo. J Neurochem 90:1302-1311
    • (2004) J Neurochem , vol.90 , pp. 1302-1311
    • Watanabe, A.1    Hong, W.K.2    Dohmae, N.3    Takio, K.4    Morishima-Kawashima, M.5    Ihara, Y.6
  • 183
    • 0033548661 scopus 로고    scopus 로고
    • Deamidation and isoaspartate formation in smeared tau in paired helical filaments. Unusual properties of the microtubule-binding domain of tau
    • 10066801 1:CAS:528:DyaK1MXhvFWqt7o%3D
    • Watanabe A, Takio K, Ihara Y (1999) Deamidation and isoaspartate formation in smeared tau in paired helical filaments. Unusual properties of the microtubule-binding domain of tau. J Biol Chem 274:7368-7378
    • (1999) J Biol Chem , vol.274 , pp. 7368-7378
    • Watanabe, A.1    Takio, K.2    Ihara, Y.3
  • 184
    • 84864448462 scopus 로고    scopus 로고
    • Deamidation accelerates amyloid formation and alters amylin fiber structure
    • 22734583 1:CAS:528:DC%2BC38Xpt1Chsbk%3D
    • Dunkelberger EB, Buchanan LE, Marek P, Cao P, Raleigh DP, Zanni MT (2012) Deamidation accelerates amyloid formation and alters amylin fiber structure. J Am Chem Soc 134:12658-12667
    • (2012) J Am Chem Soc , vol.134 , pp. 12658-12667
    • Dunkelberger, E.B.1    Buchanan, L.E.2    Marek, P.3    Cao, P.4    Raleigh, D.P.5    Zanni, M.T.6
  • 186
    • 33744948924 scopus 로고    scopus 로고
    • Role of glutamine deamidation in neurodegenerative diseases associated with triplet repeat expansion - A hypothesis
    • 16757807 1:CAS:528:DC%2BD28XlsF2rsL0%3D
    • Hasan Q, Alluri RV, Rao P, Ahuja YR (2006) Role of glutamine deamidation in neurodegenerative diseases associated with triplet repeat expansion - a hypothesis. J Mol Neurosci 29:29-33
    • (2006) J Mol Neurosci , vol.29 , pp. 29-33
    • Hasan, Q.1    Alluri, R.V.2    Rao, P.3    Ahuja, Y.R.4
  • 188
    • 3242811902 scopus 로고    scopus 로고
    • Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease
    • 15277226 1:CAS:528:DC%2BD2cXmvFWjsr0%3D
    • Guo H, Albrecht S, Bourdeau M, Petzke T, Bergeron C, LeBlanc AC (2004) Active caspase-6 and caspase-6-cleaved tau in neuropil threads, neuritic plaques, and neurofibrillary tangles of Alzheimer's disease. Am J Pathol 165:523-531
    • (2004) Am J Pathol , vol.165 , pp. 523-531
    • Guo, H.1    Albrecht, S.2    Bourdeau, M.3    Petzke, T.4    Bergeron, C.5    Leblanc, A.C.6
  • 189
    • 66149114101 scopus 로고    scopus 로고
    • Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity
    • 19383787 1:CAS:528:DC%2BD1MXmt1KktLo%3D
    • Zhang Y, Xu Y, Cook C, Gendron TF, Roettges P et al (2009) Aberrant cleavage of TDP-43 enhances aggregation and cellular toxicity. Proc Natl Acad Sci USA 106:7607-7612
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7607-7612
    • Zhang, Y.1    Xu, Y.2    Cook, C.3    Gendron, T.F.4    Roettges, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.