메뉴 건너뛰기




Volumn 4, Issue 1, 2011, Pages 8-18

Damaged proteins bearing l-isoaspartyl residues and aging: A dynamic equilibrium between generation of isomerized forms and repair by pimt

Author keywords

Aging; Damaged proteins; L isoaspartyl residues; PIMT

Indexed keywords

ALPHA CRYSTALLIN; ALPHA SYNUCLEIN; ALPHA TUBULIN; AMYLOID BETA PROTEIN; BETA SYNUCLEIN; BETA TUBULIN; COMPLEMENTARY DNA; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN BINDING PROTEIN; ENZYME; ESTRADIOL; FIBRONECTIN; INTEGRIN; MESSENGER RNA; METHYLTRANSFERASE; PROTEASOME; PROTEIN ISOASPARTYL METHYLTRANSFERASE; S ADENOSYLMETHIONINE; SOMATOMEDIN C; UNCLASSIFIED DRUG; ISOASPARTIC ACID; PCMT1 PROTEIN, HUMAN; PROTEIN; PROTEIN DEXTRO ASPARTATE METHYLTRANSFERASE;

EID: 79958792815     PISSN: 18746098     EISSN: 18746128     Source Type: Journal    
DOI: 10.2174/1874609811104010008     Document Type: Review
Times cited : (66)

References (91)
  • 1
    • 3442898781 scopus 로고    scopus 로고
    • Post-translational modifications of proteins: Implications for aging, antigen recognition, and autoimmunity
    • Cloos PA and Christgau S. Post-translational modifications of proteins: implications for aging, antigen recognition, and autoimmunity. Biogerontology 2004; 5(3): 139-158.
    • (2004) Biogerontology , vol.5 , Issue.3 , pp. 139-158
    • Cloos, P.A.1    Christgau, S.2
  • 2
    • 0346690069 scopus 로고    scopus 로고
    • Protein L-isoaspartyl methyltransferase repairs abnormal aspartyl residues accumulated in vivo in type-I collagen and restores cell migration
    • Lanthier J and Desrosiers RR. Protein L-isoaspartyl methyltransferase repairs abnormal aspartyl residues accumulated in vivo in type-I collagen and restores cell migration. Exp Cell Res 2004; 293: 96-105.
    • (2004) Exp Cell Res , vol.293 , pp. 96-105
    • Lanthier, J.1    Desrosiers, R.R.2
  • 3
    • 0348099030 scopus 로고    scopus 로고
    • Aging as war between chemical and biochemical processes: Protein methylation and the recognition of age-damaged proteins for repair
    • Clarke S. Aging as war between chemical and biochemical processes: protein methylation and the recognition of age-damaged proteins for repair. Ageing Res Rev 2003; 2(3): 263-285.
    • (2003) Ageing Res Rev , vol.2 , Issue.3 , pp. 263-285
    • Clarke, S.1
  • 4
    • 24944532072 scopus 로고    scopus 로고
    • Biological significance of isoaspartate and its repair system
    • Shimuzu T, Matsuoka Y and Shirasawa T. Biological significance of isoaspartate and its repair system. Biol Pharm Bull 2004; 28: 1590-1596.
    • (2004) Biol Pharm Bull , vol.28 , pp. 1590-1596
    • Shimuzu, T.1    Matsuoka, Y.2    Shirasawa, T.3
  • 5
    • 0347358073 scopus 로고    scopus 로고
    • Effect of deamidation of asparagine 146 on functional and structural properties of human lens alphaBcrystallin
    • Gupta R and Srivastava OP. Effect of deamidation of asparagine 146 on functional and structural properties of human lens alphaBcrystallin. Invest Ophthalmol Vis Sci 2004a; 45(1): 206-214.
    • (2004) Invest Ophthalmol Vis Sci , vol.45 , Issue.1 , pp. 206-214
    • Gupta, R.1    Srivastava, O.P.2
  • 6
    • 7244227985 scopus 로고    scopus 로고
    • Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin
    • Gupta R and Srivastava OP. Deamidation affects structural and functional properties of human alphaA-crystallin and its oligomerization with alphaB-crystallin. J Biol Chem 2004b; 279(43): 44258-44269.
    • (2004) J Biol Chem , vol.279 , Issue.43 , pp. 44258-44269
    • Gupta, R.1    Srivastava, O.P.2
  • 7
    • 69949083415 scopus 로고    scopus 로고
    • Lens aging: Effects of crystallins
    • Sharma KK and Santhoshkumar P. Lens aging: effects of crystallins. Biochim Biophys Acta 2009; 1790(10): 1095-1108.
    • (2009) Biochim Biophys Acta , vol.1790 , Issue.10 , pp. 1095-1108
    • Sharma, K.K.1    Santhoshkumar, P.2
  • 8
    • 0034487092 scopus 로고    scopus 로고
    • The amino terminus of PKA catalytic subunit--a site for introduction of posttranslational heterogeneities by deamidation: D-Asp2 and D-isoAsp2 containing isozymes
    • Kinzel V, König N, Pipkorn R, Bossemeyer D and Lehmann WD. The amino terminus of PKA catalytic subunit--a site for introduction of posttranslational heterogeneities by deamidation: D-Asp2 and D-isoAsp2 containing isozymes. Protein Sci 2000; 9(11): 2269-2277.
    • (2000) Protein Sci , vol.9 , Issue.11 , pp. 2269-2277
    • Kinzel, V.1    König, N.2    Pipkorn, R.3    Bossemeyer, D.4    Lehmann, W.D.5
  • 9
    • 0034695932 scopus 로고    scopus 로고
    • Intracellular distribution of mammalian protein kinase A catalytic subunit altered by conserved Asn2 deamidation
    • Pepperkok R, Hotz-Wagenblatt A, König N, Girod A, Bossemeyer D and Kinzel V. Intracellular distribution of mammalian protein kinase A catalytic subunit altered by conserved Asn2 deamidation. J Cell Biol 2000; 148(4): 715-726.
    • (2000) J Cell Biol , vol.148 , Issue.4 , pp. 715-726
    • Pepperkok, R.1    Hotz-Wagenblatt, A.2    König, N.3    Girod, A.4    Bossemeyer, D.5    Kinzel, V.6
  • 10
    • 33846020967 scopus 로고    scopus 로고
    • Spontaneous formation of L-isoaspartate and gain of function in fibronectin
    • Curnis F, Longhi R, Crippa L, Cattaneo A, Dondossola E, Bachi A, et al. Spontaneous formation of L-isoaspartate and gain of function in fibronectin. J Biol Chem 2006; 281(47): 36466-36476.
    • (2006) J Biol Chem , vol.281 , Issue.47 , pp. 36466-36476
    • Curnis, F.1    Longhi, R.2    Crippa, L.3    Cattaneo, A.4    Dondossola, E.5    Bachi, A.6
  • 11
    • 0041367295 scopus 로고    scopus 로고
    • Deamidation and isoaspartate formation in proteins: Unwanted alterations or surreptitious signals?
    • Reissner, KJ and Aswad DW. Deamidation and isoaspartate formation in proteins: unwanted alterations or surreptitious signals? Cell Mol Life Sci 2003; 60(7): 1281-1295.
    • (2003) Cell Mol Life Sci , vol.60 , Issue.7 , pp. 1281-1295
    • Reissner, K.J.1    Aswad, D.W.2
  • 12
    • 0024398664 scopus 로고
    • Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA, and small molecule S-adenosylmethionine-dependent methyltransferases
    • Ingrosso D, Fowler AV, Bleibaum J and Clarke S. Sequence of the D-aspartyl/L-isoaspartyl protein methyltransferase from human erythrocytes. Common sequence motifs for protein, DNA, RNA, and small molecule S-adenosylmethionine-dependent methyltransferases. J Biol Chem 1989; 264(33): 20131-20139.
    • (1989) J Biol Chem , vol.264 , Issue.33 , pp. 20131-20139
    • Ingrosso, D.1    Fowler, A.V.2    Bleibaum, J.3    Clarke, S.4
  • 13
    • 34247558033 scopus 로고    scopus 로고
    • Accumulation of proteins bearing atypical isoaspartyl residues in livers of alcohol-fed rats is prevented by betaine administration: Effects on protein-L-isoaspartyl methyltransferase activity
    • Kharbanda KK, Mailliard ME, Baldwin CR, Sorrell MF and Tuma DJ. Accumulation of proteins bearing atypical isoaspartyl residues in livers of alcohol-fed rats is prevented by betaine administration: effects on protein-L-isoaspartyl methyltransferase activity. J Hepatol 2007; 46(6): 1119-25.
    • (2007) J Hepatol , vol.46 , Issue.6 , pp. 1119-1125
    • Kharbanda, K.K.1    Mailliard, M.E.2    Baldwin, C.R.3    Sorrell, M.F.4    Tuma, D.J.5
  • 14
    • 64249093838 scopus 로고    scopus 로고
    • Mechanistic insights into nitrite-induced cardioprotection using an integrated metabolomic/proteomic approach
    • Perlman DH, Bauer SM, Ashrafian H, Bryan NS, Garcia-Saura MF, Lim CC, et al. Mechanistic insights into nitrite-induced cardioprotection using an integrated metabolomic/proteomic approach. Circ Res 2009; 104(6): 796-804.
    • (2009) Circ Res , vol.104 , Issue.6 , pp. 796-804
    • Perlman, D.H.1    Bauer, S.M.2    Ashrafian, H.3    Bryan, N.S.4    Garcia-Saura, M.F.5    Lim, C.C.6
  • 15
    • 0023664638 scopus 로고
    • Regulation and subcellular distribution of a protein methyltransferase and its damaged aspartyl substrate sites in developing Xenopus oocytes
    • O'Connor CM. Regulation and subcellular distribution of a protein methyltransferase and its damaged aspartyl substrate sites in developing Xenopus oocytes. J Biol Chem 1987; 262(21): 10398-403.
    • (1987) J Biol Chem , vol.262 , Issue.21 , pp. 10398-10403
    • O'Connor, C.M.1
  • 16
    • 0023118384 scopus 로고
    • The characterization of a membrane-bound protein carboxymethylation system in brain
    • Sellinger OZ, Kramer CM, Fischer-Bovenkerk C and Adams CM. The characterization of a membrane-bound protein carboxymethylation system in brain. Neurochem Int 1987; 10(2): 155-66.
    • (1987) Neurochem Int , vol.10 , Issue.2 , pp. 155-166
    • Sellinger, O.Z.1    Kramer, C.M.2    Fischer-Bovenkerk, C.3    Adams, C.M.4
  • 17
    • 0028979610 scopus 로고
    • Immunochemical characterization of L-isoaspartyl-protein carboxyl methyltransferase from mammalian tissues
    • Boivin D, Bilodeau D and Béliveau R. Immunochemical characterization of L-isoaspartyl-protein carboxyl methyltransferase from mammalian tissues. Biochem J 1995; 309(Pt 3): 993-8.
    • (1995) Biochem J , vol.309 , Issue.Pt 3 , pp. 993-998
    • Boivin, D.1    Bilodeau, D.2    Béliveau, R.3
  • 18
    • 34547200525 scopus 로고    scopus 로고
    • Microtubuleassociated protein 1B binds glyceraldehyde-3-phosphate dehydrogenase
    • Cueille N, Blanc CT, Riederer IM and Riederer BM. Microtubuleassociated protein 1B binds glyceraldehyde-3-phosphate dehydrogenase. J Proteome Res 2007; 6(7): 2640-7.
    • (2007) J Proteome Res , vol.6 , Issue.7 , pp. 2640-2647
    • Cueille, N.1    Blanc, C.T.2    Riederer, I.M.3    Riederer, B.M.4
  • 20
    • 70449358615 scopus 로고    scopus 로고
    • Identification of protein clusters predictive of response to chemotherapy in breast cancer patients
    • Cortesi L, Barchetti A, De Matteis E, Rossi E, Della Casa L, Marcheselli L, et al. Identification of protein clusters predictive of response to chemotherapy in breast cancer patients. J Proteome Res 2009; 8(11): 4916-33.
    • (2009) J Proteome Res , vol.8 , Issue.11 , pp. 4916-4933
    • Cortesi, L.1    Barchetti, A.2    de Matteis, E.3    Rossi, E.4    della Casa, L.5    Marcheselli, L.6
  • 21
    • 33745810970 scopus 로고    scopus 로고
    • Identification of brain cell death associated proteins in human post-mortem cerebrospinal fluid
    • Burgess JA, Lescuyer P, Hainard A, Burkhard PR, Turck N, Michel P, et al. Identification of brain cell death associated proteins in human post-mortem cerebrospinal fluid. J Proteome Res 2006; 5(7): 1674-81.
    • (2006) J Proteome Res , vol.5 , Issue.7 , pp. 1674-1681
    • Burgess, J.A.1    Lescuyer, P.2    Hainard, A.3    Burkhard, P.R.4    Turck, N.5    Michel, P.6
  • 22
    • 67249088582 scopus 로고    scopus 로고
    • Functional genomic analysis of amniotic fluid cellfree mRNA suggests that oxidative stress is significant in Down syndrome fetuses
    • Slonim DK, Koide K, Johnson KL, Tantravahi U, Cowan JM, Jarrah Z, et al. Functional genomic analysis of amniotic fluid cellfree mRNA suggests that oxidative stress is significant in Down syndrome fetuses. Proc Natl Acad Sci USA 2009; 106(23): 9425-9.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.23 , pp. 9425-9429
    • Slonim, D.K.1    Koide, K.2    Johnson, K.L.3    Tantravahi, U.4    Cowan, J.M.5    Jarrah, Z.6
  • 23
    • 0017074189 scopus 로고
    • Regional and subcellular distribution of protein carboxymethylase in brain and other tissues
    • EJ Jr and Axelrod J. Regional and subcellular distribution of protein carboxymethylase in brain and other tissues. J Neurochem 1976; 26(6): 1159-65.
    • (1976) J Neurochem , vol.26 , Issue.6 , pp. 1159-1165
    • Jr, E.J.1    Axelrod, J.2
  • 24
    • 0028157699 scopus 로고
    • Tissuespecific expression of isoaspartyl protein carboxyl methyltransferase gene in rat brain and testis
    • Mizobuchi M, Murao K, Takeda R and Kakimoto Y. Tissuespecific expression of isoaspartyl protein carboxyl methyltransferase gene in rat brain and testis. J Neurochem 1994; 62(1): 322-8.
    • (1994) J Neurochem , vol.62 , Issue.1 , pp. 322-328
    • Mizobuchi, M.1    Murao, K.2    Takeda, R.3    Kakimoto, Y.4
  • 26
    • 74449083888 scopus 로고    scopus 로고
    • A proteomic analysis of the ventral hippocampus of rats subjected to maternal separation and escitalopram treatment
    • Marais L, Hattingh SM, Stein DJ and Daniels WM. A proteomic analysis of the ventral hippocampus of rats subjected to maternal separation and escitalopram treatment. Metab Brain Dis 2009; 24(4): 569-86.
    • (2009) Metab Brain Dis , vol.24 , Issue.4 , pp. 569-586
    • Marais, L.1    Hattingh, S.M.2    Stein, D.J.3    Daniels, W.M.4
  • 27
    • 0022259076 scopus 로고
    • Immunohistochemical localization of protein-O-carboxylmethyltransferase in rat brain neurons
    • Billingsley ML, Kim S and Kuhn DM. Immunohistochemical localization of protein-O-carboxylmethyltransferase in rat brain neurons. Neuroscience 1985; 15(1): 159-71.
    • (1985) Neuroscience , vol.15 , Issue.1 , pp. 159-171
    • Billingsley, M.L.1    Kim, S.2    Kuhn, D.M.3
  • 28
    • 74449084485 scopus 로고    scopus 로고
    • Proteomic analysis reveals differentially expressed proteins in the rat frontal cortex after methamphetamine treatment
    • Faure JJ, Hattingh SM, Stein DJ and Daniels WM. Proteomic analysis reveals differentially expressed proteins in the rat frontal cortex after methamphetamine treatment. Metab Brain Dis 2009; 24(4): 685-700.
    • (2009) Metab Brain Dis , vol.24 , Issue.4 , pp. 685-700
    • Faure, J.J.1    Hattingh, S.M.2    Stein, D.J.3    Daniels, W.M.4
  • 29
    • 33748688816 scopus 로고    scopus 로고
    • Effects of chronic risperidone treatment on the striatal protein profiles in rats
    • O'Brien E, Dedova I, Duffy L, Cordwell S, Karl T and Matsumoto I. Effects of chronic risperidone treatment on the striatal protein profiles in rats. Brain Res 2006; 1113(1): 24-32.
    • (2006) Brain Res , vol.1113 , Issue.1 , pp. 24-32
    • O'Brien, E.1    Dedova, I.2    Duffy, L.3    Cordwell, S.4    Karl, T.5    Matsumoto, I.6
  • 31
    • 33749235698 scopus 로고    scopus 로고
    • Gelfree analysis of the human brain proteome: Application of liquid chromatography and mass spectrometry on biopsy and autopsy samples
    • Dumont D, Noben JP, Verhaert P, Stinissen P and Robben J. Gelfree analysis of the human brain proteome: application of liquid chromatography and mass spectrometry on biopsy and autopsy samples. Proteomics 2006; 6(18): 4967-77.
    • (2006) Proteomics , vol.6 , Issue.18 , pp. 4967-4977
    • Dumont, D.1    Noben, J.P.2    Verhaert, P.3    Stinissen, P.4    Robben, J.5
  • 34
    • 33845633819 scopus 로고    scopus 로고
    • Biomarker discovery: A proteomic approach for brain cancer profiling
    • Khalil AA. Biomarker discovery: a proteomic approach for brain cancer profiling. Cancer Sci 2007; 98(2): 201-13.
    • (2007) Cancer Sci , vol.98 , Issue.2 , pp. 201-213
    • Khalil, A.A.1
  • 35
    • 67649226736 scopus 로고    scopus 로고
    • Proteomic analysis of dorsolateral prefrontal cortex indicates the involvement of cytoskeleton, oligodendrocyte, energy metabolism and new potential markers in schizophrenia
    • Martins-de-Souza D, Gattaz WF, Schmitt A, Maccarrone G, Hunyadi- Gulyás E, Eberlin MN, et al. Proteomic analysis of dorsolateral prefrontal cortex indicates the involvement of cytoskeleton, oligodendrocyte, energy metabolism and new potential markers in schizophrenia. J Psychiatr Res 2009; 43(11): 978-86.
    • (2009) J Psychiatr Res , vol.43 , Issue.11 , pp. 978-986
    • Martins-de-Souza, D.1    Gattaz, W.F.2    Schmitt, A.3    Maccarrone, G.4    Hunyadi-Gulyás, E.5    Eberlin, M.N.6
  • 36
    • 67650726655 scopus 로고    scopus 로고
    • 2-D DIGE analysis implicates cytoskeletal abnormalities in psychiatric disease
    • English JA, Dicker P, Föcking M, Dunn MJ and Cotter DR. 2-D DIGE analysis implicates cytoskeletal abnormalities in psychiatric disease. Proteomics 2009; 9(12): 3368-82.
    • (2009) Proteomics , vol.9 , Issue.12 , pp. 3368-3382
    • English, J.A.1    Dicker, P.2    Föcking, M.3    Dunn, M.J.4    Cotter, D.R.5
  • 37
    • 85047696344 scopus 로고    scopus 로고
    • Proteomic analysis of corticobasal degeneration: A case study of corticobasal degeneration at the proteome level
    • Chen W, Ji J and Ru B. Proteomic analysis of corticobasal degeneration: a case study of corticobasal degeneration at the proteome level. J Neuropsychiatry Clin Neurosci 2005; 17(3): 364-71.
    • (2005) J Neuropsychiatry Clin Neurosci , vol.17 , Issue.3 , pp. 364-371
    • Chen, W.1    Ji, J.2    Ru, B.3
  • 38
    • 33644783812 scopus 로고    scopus 로고
    • Regional and cellular gene expression changes in human Huntington's disease brain
    • Hodges A, Strand AD, Aragaki AK, Kuhn A, Sengstag T, Hughes G, et al. Regional and cellular gene expression changes in human Huntington's disease brain. Hum Mol Genet 2006 15; 15(6): 965-77.
    • (2006) Hum Mol Genet , vol.15 , Issue.6 , pp. 965-977
    • Hodges, A.1    Strand, A.D.2    Aragaki, A.K.3    Kuhn, A.4    Sengstag, T.5    Hughes, G.6
  • 39
    • 0022370732 scopus 로고
    • Protein-O-carboxylmethyltransferase in the rat brain: High regional levels in the substantia nigra, locus coeruleus and paraventricular nucleus
    • Billingsley ML and Balaban CD. Protein-O-carboxylmethyltransferase in the rat brain: high regional levels in the substantia nigra, locus coeruleus and paraventricular nucleus. Brain Res 1985; 358(1-2): 96-103.
    • (1985) Brain Res , vol.358 , Issue.1-2 , pp. 96-103
    • Billingsley, M.L.1    Balaban, C.D.2
  • 40
    • 0028905409 scopus 로고
    • Protein L-isoaspartyl methyltransferase: Developmentally regulated gene expression and protein localization in the central nervous system of aged rat
    • Shirasawa T, Endoh R, Zeng YX, Sakamoto K and Mori H. Protein L-isoaspartyl methyltransferase: developmentally regulated gene expression and protein localization in the central nervous system of aged rat. Neurosci Lett 1995; 188(1): 37-40.
    • (1995) Neurosci Lett , vol.188 , Issue.1 , pp. 37-40
    • Shirasawa, T.1    Endoh, R.2    Zeng, Y.X.3    Sakamoto, K.4    Mori, H.5
  • 43
    • 70350087346 scopus 로고    scopus 로고
    • Synaptic proteome changes in the superior frontal gyrus and occipital cortex of the alcoholic brain
    • Etheridge N, Lewohl JM, Mayfield RD, Harris RA and Dodd PR. Synaptic proteome changes in the superior frontal gyrus and occipital cortex of the alcoholic brain. Proteomics Clin Appl 2009; 3(6): 730-42.
    • (2009) Proteomics Clin Appl , vol.3 , Issue.6 , pp. 730-742
    • Etheridge, N.1    Lewohl, J.M.2    Mayfield, R.D.3    Harris, R.A.4    Dodd, P.R.5
  • 44
    • 0034932858 scopus 로고    scopus 로고
    • Aberrant synaptic transmission in the hippocampal CA3 region and cognitive deterioration in protein-repair enzymedeficient mice
    • Ikegaya Y, Yamada M, Fukuda T, Kuroyanagi H, Shirasawa T and Nishiyama, N. Aberrant synaptic transmission in the hippocampal CA3 region and cognitive deterioration in protein-repair enzymedeficient mice. Hippocampus 2001; 11(3): 287-98.
    • (2001) Hippocampus , vol.11 , Issue.3 , pp. 287-298
    • Ikegaya, Y.1    Yamada, M.2    Fukuda, T.3    Kuroyanagi, H.4    Shirasawa, T.5    Nishiyama, N.6
  • 45
    • 0022203606 scopus 로고
    • Identification and topography of substrates for protein carboxyl methyltransferase in synaptic membrane and myelin-enriched fractions of bovine and rat brain
    • Johnson BA and Aswad DW. Identification and topography of substrates for protein carboxyl methyltransferase in synaptic membrane and myelin-enriched fractions of bovine and rat brain. J Neurochem 1985; 45(4): 1119-27.
    • (1985) J Neurochem , vol.45 , Issue.4 , pp. 1119-1127
    • Johnson, B.A.1    Aswad, D.W.2
  • 46
    • 33845945907 scopus 로고    scopus 로고
    • Proteomic identification of novel substrates of a protein isoaspartyl methyltransferase repair enzyme
    • Vigneswara V, Lowenson JD, Powell CD, Thakur M, Bailey K, Clarke S, et al. Proteomic identification of novel substrates of a protein isoaspartyl methyltransferase repair enzyme. J Biol Chem 2006; 281(43): 32619-29.
    • (2006) J Biol Chem , vol.281 , Issue.43 , pp. 32619-32629
    • Vigneswara, V.1    Lowenson, J.D.2    Powell, C.D.3    Thakur, M.4    Bailey, K.5    Clarke, S.6
  • 47
    • 33845918167 scopus 로고    scopus 로고
    • Protein repair in the brain, proteomic analysis of endogenous substrates for protein L-isoaspartyl methyltransferase in mouse brain
    • Zhu JX, Doyle HA, Mamula MJ and Aswad DW. Protein repair in the brain, proteomic analysis of endogenous substrates for protein L-isoaspartyl methyltransferase in mouse brain. J Biol Chem 2006; 281(44): 33802-13.
    • (2006) J Biol Chem , vol.281 , Issue.44 , pp. 33802-33813
    • Zhu, J.X.1    Doyle, H.A.2    Mamula, M.J.3    Aswad, D.W.4
  • 48
    • 61549111872 scopus 로고    scopus 로고
    • Alpha-Synuclein and neuronal cell death
    • Cookson MR. alpha-Synuclein and neuronal cell death. Mol Neurodegener 2009; 4: 9.
    • (2009) Mol Neurodegener , vol.4 , pp. 9
    • Cookson, M.R.1
  • 51
    • 84987471502 scopus 로고
    • Age-Related Changes of Protein Carboxyl Methylation in Rat Brain and Liver
    • Hye-Ryan L and Gil-Ja J. Age-Related Changes of Protein Carboxyl Methylation in Rat Brain and Liver. Korean Biochem J 1991; 24(1): 65-70.
    • (1991) Korean Biochem J , vol.24 , Issue.1 , pp. 65-70
    • Hye-Ryan, L.1    Gil-Ja, J.2
  • 52
    • 0030029281 scopus 로고    scopus 로고
    • Age-related changes in carboxyl methylation of proteins in the kidney
    • Pelletier J, Desrosiers RR and Béliveau R. Age-related changes in carboxyl methylation of proteins in the kidney. Mech Ageing Dev 1996; 86(2): 115-35.
    • (1996) Mech Ageing Dev , vol.86 , Issue.2 , pp. 115-135
    • Pelletier, J.1    Desrosiers, R.R.2    Béliveau, R.3
  • 53
    • 0036273830 scopus 로고    scopus 로고
    • Folate status and age affect the accumulation of L-isoaspartyl residues in rat liver proteins
    • Ghandour H, Lin BF, Choi SW, Mason JB and Selhub J. Folate status and age affect the accumulation of L-isoaspartyl residues in rat liver proteins. J Nutr 2002; 132(6): 1357-60.
    • (2002) J Nutr , vol.132 , Issue.6 , pp. 1357-1360
    • Ghandour, H.1    Lin, B.F.2    Choi, S.W.3    Mason, J.B.4    Selhub, J.5
  • 55
    • 3042631024 scopus 로고    scopus 로고
    • Gene regulation and DNA damage in the ageing human brain
    • Lu T, Pan Y, Kao SY, Li C, Kohane I, Chan J, et al. Gene regulation and DNA damage in the ageing human brain. Nature 2004; 429(6994): 883-91.
    • (2004) Nature , vol.429 , Issue.6994 , pp. 883-891
    • Lu, T.1    Pan, Y.2    Kao, S.Y.3    Li, C.4    Kohane, I.5    Chan, J.6
  • 56
    • 0037288292 scopus 로고    scopus 로고
    • Influence of ageing, heat shock treatment and in vivo total antioxidant status on gene-expression profile and protein synthesis in human peripheral lymphocytes
    • Visala Rao D, Boyle GM, Parsons PG, Watson K and Jones GL. Influence of ageing, heat shock treatment and in vivo total antioxidant status on gene-expression profile and protein synthesis in human peripheral lymphocytes. Mech Ageing Dev 2003; 124(1): 55-69.
    • (2003) Mech Ageing Dev , vol.124 , Issue.1 , pp. 55-69
    • Visala, R.D.1    Boyle, G.M.2    Parsons, P.G.3    Watson, K.4    Jones, G.L.5
  • 57
    • 0022457847 scopus 로고
    • Protein carboxyl methyltransferase and methyl acceptor proteins in aging and cataractous tissue of the human eye lens
    • McFadden PN and Clarke S. Protein carboxyl methyltransferase and methyl acceptor proteins in aging and cataractous tissue of the human eye lens. Mech Ageing Dev 1986; 34(1): 91-105.
    • (1986) Mech Ageing Dev , vol.34 , Issue.1 , pp. 91-105
    • McFadden, P.N.1    Clarke, S.2
  • 58
    • 0028790462 scopus 로고
    • Hampered expression of isoaspartyl protein carboxyl methyltransferase gene in the human cataractous lens
    • Kodama T, Mizobuchi M, Takeda R, Torikai H, Shinomiya H and Ohashi Y. Hampered expression of isoaspartyl protein carboxyl methyltransferase gene in the human cataractous lens. Biochim Biophys Acta 1995; 1245(2): 269-72.
    • (1995) Biochim Biophys Acta , vol.1245 , Issue.2 , pp. 269-272
    • Kodama, T.1    Mizobuchi, M.2    Takeda, R.3    Torikai, H.4    Shinomiya, H.5    Ohashi, Y.6
  • 59
    • 0030962591 scopus 로고    scopus 로고
    • Post-Transcriptional Regulation of Synaptic Vesicle Protein Expression and the Developmental Control of Synaptic Vesicle Formation
    • Christopher D and Edward BZ. Post-Transcriptional Regulation of Synaptic Vesicle Protein Expression and the Developmental Control of Synaptic Vesicle Formation. J Neurosci 1997; 17(7): 2365-75.
    • (1997) J Neurosci , vol.17 , Issue.7 , pp. 2365-2375
    • Christopher, D.1    Edward, B.Z.2
  • 60
    • 0025080764 scopus 로고
    • Turnover of cytoskeletal proteins in vivo
    • Safaei R and Fischer I. Turnover of cytoskeletal proteins in vivo. Brain Res 1990; 533(1): 83-90.
    • (1990) Brain Res , vol.533 , Issue.1 , pp. 83-90
    • Safaei, R.1    Fischer, I.2
  • 61
    • 0029876218 scopus 로고    scopus 로고
    • Molecular Aging of Tubulin: Accumulation of Isoaspartyl Sites in Vitro and in Vivo
    • 35916
    • Najbauer J, Orpiszeeski J and Aswad DW. Molecular Aging of Tubulin: Accumulation of Isoaspartyl Sites in Vitro and in Vivo. Biochemistry 1996, 35916): 5183-90.
    • (1996) Biochemistry , pp. 5183-5190
    • Najbauer, J.1    Orpiszeeski, J.2    Aswad, D.W.3
  • 62
    • 0036828328 scopus 로고    scopus 로고
    • Down-regulation of protein L-isoaspartyl methyltransferase in human epileptic hippocampus contributes to generation of damaged tubulin
    • Lanthier J, Bouthillier A, Lapointe M, Demeule M, Béliveau R and Desrosiers RR. Down-regulation of protein L-isoaspartyl methyltransferase in human epileptic hippocampus contributes to generation of damaged tubulin. J Neurochem 2002, 83(3): 581-91.
    • (2002) J Neurochem , vol.83 , Issue.3 , pp. 581-591
    • Lanthier, J.1    Bouthillier, A.2    Lapointe, M.3    Demeule, M.4    Béliveau, R.5    Desrosiers, R.R.6
  • 63
    • 7244243876 scopus 로고    scopus 로고
    • Stabilization of alpha-synuclein protein with aging and familial parkinson's disease-linked A53T mutation
    • Li W, Lesuisse C, Xu Y, Troncoso JC, Price DL, Lee MK. Stabilization of alpha-synuclein protein with aging and familial parkinson's disease-linked A53T mutation. J Neurosci 2004; 24(33): 7400-9.
    • (2004) J Neurosci , vol.24 , Issue.33 , pp. 7400-7409
    • Li, W.1    Lesuisse, C.2    Xu, Y.3    Troncoso, J.C.4    Price, D.L.5    Lee, M.K.6
  • 64
    • 0345549316 scopus 로고    scopus 로고
    • Resistance to obesity in Lou/C rats prevents ageing-associated metabolic alterations
    • Perrin D, Soulage C, Pequignot JM and Géloën A. Resistance to obesity in Lou/C rats prevents ageing-associated metabolic alterations. Diabetologia 2003; 46(11): 1489-96.
    • (2003) Diabetologia , vol.46 , Issue.11 , pp. 1489-1496
    • Perrin, D.1    Soulage, C.2    Pequignot, J.M.3    Géloën, A.4
  • 66
    • 64549094253 scopus 로고    scopus 로고
    • Neuroprotective effect of sodium ferulate and signal transduction mechanisms in the aged rat hippocampus
    • Jin Y, Yan EZ, Li XM, Fan Y, Zhao YJ, Liu Z, et al. Neuroprotective effect of sodium ferulate and signal transduction mechanisms in the aged rat hippocampus. Acta Pharmacol Sin 2008; 29(12): 1399-408.
    • (2008) Acta Pharmacol Sin , vol.29 , Issue.12 , pp. 1399-1408
    • Jin, Y.1    Yan, E.Z.2    Li, X.M.3    Fan, Y.4    Zhao, Y.J.5    Liu, Z.6
  • 67
    • 50849134835 scopus 로고    scopus 로고
    • Up-regulation of protein Lisoaspartyl methyltransferase expression by lithium is mediated by glycogen synthase kinase-3 inactivation and beta-catenin stabilization
    • Lamarre M and Desrosiers RR. Up-regulation of protein Lisoaspartyl methyltransferase expression by lithium is mediated by glycogen synthase kinase-3 inactivation and beta-catenin stabilization. Neuropharmacology 2008; 55(5): 669-76.
    • (2008) Neuropharmacology , vol.55 , Issue.5 , pp. 669-676
    • Lamarre, M.1    Desrosiers, R.R.2
  • 68
    • 63049099412 scopus 로고    scopus 로고
    • Valproic acid enhances protein Lisoaspartyl methyltransferase expression by stimulating extracellular signal-regulated kinase signaling pathway
    • Cournoyer P and Desrosiers RR. Valproic acid enhances protein Lisoaspartyl methyltransferase expression by stimulating extracellular signal-regulated kinase signaling pathway. Neuropharmacology 2009; 56(5): 839-48.
    • (2009) Neuropharmacology , vol.56 , Issue.5 , pp. 839-848
    • Cournoyer, P.1    Desrosiers, R.R.2
  • 69
    • 20044376670 scopus 로고    scopus 로고
    • Hydroxytyrosol, a natural antioxidant from olive oil, prevents protein damage induced by long-wave ultraviolet radiation in melanoma cells
    • D'Angelo S, Ingrosso D, Migliardi V, Sorrentino A, Donnarumma G, Baroni A, et al. Hydroxytyrosol, a natural antioxidant from olive oil, prevents protein damage induced by long-wave ultraviolet radiation in melanoma cells. Free Radic Biol Med 2005; 38(7): 908-19.
    • (2005) Free Radic Biol Med , vol.38 , Issue.7 , pp. 908-919
    • D'Angelo, S.1    Ingrosso, D.2    Migliardi, V.3    Sorrentino, A.4    Donnarumma, G.5    Baroni, A.6
  • 70
    • 67650376373 scopus 로고    scopus 로고
    • Oxidized proteins: Mechanisms of removal and consequences of accumulation
    • Dunlop RA, Brunk UT and Rodgers KJ. Oxidized proteins: mechanisms of removal and consequences of accumulation. IUBMB Life 2009; 61(5): 522-7.
    • (2009) IUBMB Life , vol.61 , Issue.5 , pp. 522-527
    • Dunlop, R.A.1    Brunk, U.T.2    Rodgers, K.J.3
  • 71
    • 27944510125 scopus 로고    scopus 로고
    • Proteasome dysfunction in mammalian aging: Steps and factors involved
    • Chondrogianni N and Gonos ES. Proteasome dysfunction in mammalian aging: steps and factors involved. Exp Gerontol 2005; 40(12): 931-8.
    • (2005) Exp Gerontol , vol.40 , Issue.12 , pp. 931-938
    • Chondrogianni, N.1    Gonos, E.S.2
  • 72
    • 0028181491 scopus 로고
    • Automethylation of protein (Daspartyl/ L-isoaspartyl) carboxyl methyltransferase, a response to enzyme aging
    • Lindquist JA and McFadden PN. Automethylation of protein (Daspartyl/ L-isoaspartyl) carboxyl methyltransferase, a response to enzyme aging. J Protein Chem 1994; 13(1): 23-30.
    • (1994) J Protein Chem , vol.13 , Issue.1 , pp. 23-30
    • Lindquist, J.A.1    McFadden, P.N.2
  • 73
    • 0032859445 scopus 로고    scopus 로고
    • Polymorphic forms of the protein Lisoaspartate (D-aspartate) O-methyltransferase involved in the repair of age-damaged proteins
    • DeVry CG and Clarke S. Polymorphic forms of the protein Lisoaspartate (D-aspartate) O-methyltransferase involved in the repair of age-damaged proteins. J Hum Genet 1999; 44(5): 275-88.
    • (1999) J Hum Genet , vol.44 , Issue.5 , pp. 275-288
    • Devry, C.G.1    Clarke, S.2
  • 74
    • 72649084172 scopus 로고    scopus 로고
    • The V119I polymorphism in protein L-isoaspartate O-methyltransferase alters the substrate-binding interface
    • Rutherford K and Daggett V. The V119I polymorphism in protein L-isoaspartate O-methyltransferase alters the substrate-binding interface. Protein Eng Des Sel 2009; 22(12): 713-21.
    • (2009) Protein Eng Des Sel , vol.22 , Issue.12 , pp. 713-721
    • Rutherford, K.1    Daggett, V.2
  • 75
    • 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
    • Watanabe A, Takio K and Ihara Y. Deamidation and isoaspartate formation in smeared tau in paired helical filaments. Unusual properties of the microtubule-binding domain of tau. J Biol Chem 1999; 274(11): 7368-78.
    • (1999) J Biol Chem , vol.274 , Issue.11 , pp. 7368-7378
    • Watanabe, A.1    Takio, K.2    Ihara, Y.3
  • 77
    • 0032842432 scopus 로고    scopus 로고
    • Methylation of cortical brain proteins from patients with HIV infection
    • Goggins M, Scott JM and Weir DG. Methylation of cortical brain proteins from patients with HIV infection. Acta Neurol Scand 1999; 100(5): 326-31.
    • (1999) Acta Neurol Scand , vol.100 , Issue.5 , pp. 326-331
    • Goggins, M.1    Scott, J.M.2    Weir, D.G.3
  • 79
    • 58149387579 scopus 로고    scopus 로고
    • Effects of misdiagnosis in input data on the identification of differential expression genes in incipient Alzheimer patients
    • Joseph S, Robbins K, Zhang W and Rekaya R. Effects of misdiagnosis in input data on the identification of differential expression genes in incipient Alzheimer patients. In Silico Biol 2008; 8(5-6): 545-54.
    • (2008) In Silico Biol , vol.8 , Issue.5-6 , pp. 545-554
    • Joseph, S.1    Robbins, K.2    Zhang, W.3    Rekaya, R.4
  • 80
    • 0029992233 scopus 로고    scopus 로고
    • Embryonic genes expressed in Alzheimer's disease brains
    • Kondo T, Shirasawa T, Itoyama Y and Mori H. Embryonic genes expressed in Alzheimer's disease brains. Neurosci Lett 1996; 209(3): 157-60.
    • (1996) Neurosci Lett , vol.209 , Issue.3 , pp. 157-160
    • Kondo, T.1    Shirasawa, T.2    Itoyama, Y.3    Mori, H.4
  • 81
    • 77951083963 scopus 로고    scopus 로고
    • Animal models for Alzheimer's disease and frontotemporal dementia: A perspective
    • Götz J and Götz NN. Animal models for Alzheimer's disease and frontotemporal dementia: a perspective. ASN Neuro 2009; 1(4): 251-64.
    • (2009) ASN Neuro , vol.1 , Issue.4 , pp. 251-264
    • Götz, J.1    Götz, N.N.2
  • 82
    • 0027477463 scopus 로고
    • Structural alterations in the peptide backbone of betaamyloid core protein may account for its deposition and stability in Alzheimer's disease
    • Roher AE, Lowenson JD, Clarke S, Wolkow C, Wang R, Cotter RJ, et al. Structural alterations in the peptide backbone of betaamyloid core protein may account for its deposition and stability in Alzheimer's disease. J Biol Chem 1993; 268(5): 3072-83.
    • (1993) J Biol Chem , vol.268 , Issue.5 , pp. 3072-3083
    • Roher, A.E.1    Lowenson, J.D.2    Clarke, S.3    Wolkow, C.4    Wang, R.5    Cotter, R.J.6
  • 83
    • 0037010294 scopus 로고    scopus 로고
    • Isoaspartate formation at position 23 of amyloid beta peptide enhanced fibril formation and deposited onto senile plaques and vascular amyloids in Alzheimer's disease
    • Shimizu T, Fukuda H, Murayama S, Izumiyama N and Shirasawa T. Isoaspartate formation at position 23 of amyloid beta peptide enhanced fibril formation and deposited onto senile plaques and vascular amyloids in Alzheimer's disease. J Neurosci Res 2002; 70(3): 451-61.
    • (2002) J Neurosci Res , vol.70 , Issue.3 , pp. 451-461
    • Shimizu, T.1    Fukuda, H.2    Murayama, S.3    Izumiyama, N.4    Shirasawa, T.5
  • 84
    • 0033014981 scopus 로고    scopus 로고
    • The presence of isoaspartic acid in beta-amyloid plaques indicates plaque age
    • Fonseca MI, Head E, Velazquez P, Cotman CW and Tenner AJ. The presence of isoaspartic acid in beta-amyloid plaques indicates plaque age. Exp Neurol 1999; 157(2): 277-88.
    • (1999) Exp Neurol , vol.157 , Issue.2 , pp. 277-288
    • Fonseca, M.I.1    Head, E.2    Velazquez, P.3    Cotman, C.W.4    Tenner, A.J.5
  • 85
    • 0031729335 scopus 로고    scopus 로고
    • Quantification of modified amyloid beta peptides in Alzheimer disease and Down syndrome brains
    • Hosoda R, Saido TC, Otvos L Jr, Arai T, Mann DM, Lee VM, et al. Quantification of modified amyloid beta peptides in Alzheimer disease and Down syndrome brains. J Neuropathol Exp Neurol 1998; 57(11): 1089-95.
    • (1998) J Neuropathol Exp Neurol , vol.57 , Issue.11 , pp. 1089-1095
    • Hosoda, R.1    Saido, T.C.2    Otvos Jr., L.3    Arai, T.4    Mann, D.M.5    Lee, V.M.6
  • 86
    • 0028544334 scopus 로고
    • Racemization: Its biological significance on neuropathogenesis of Alzheimer's disease
    • Mori H, Ishii K, Tomiyama T, Furiya Y, Sahara N, Asano S, et al. Racemization: its biological significance on neuropathogenesis of Alzheimer's disease. Tohoku J Exp Med 1994; 174(3): 251-62.
    • (1994) Tohoku J Exp Med , vol.174 , Issue.3 , pp. 251-262
    • Mori, H.1    Ishii, K.2    Tomiyama, T.3    Furiya, Y.4    Sahara, N.5    Asano, S.6
  • 87
    • 0028177534 scopus 로고
    • Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid beta protein analogues
    • Tomiyama T, Asano S, Furiya Y, Shirasawa T, Endo N and Mori H. Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid beta protein analogues. J Biol Chem 1994; 269(14): 10205-8.
    • (1994) J Biol Chem , vol.269 , Issue.14 , pp. 10205-10208
    • Tomiyama, T.1    Asano, S.2    Furiya, Y.3    Shirasawa, T.4    Endo, N.5    Mori, H.6
  • 89
    • 50849124783 scopus 로고    scopus 로고
    • Isoaspartate residues dramatically influence substrate recognition and turnover by proteases
    • Böhme L, Bär JW, Hoffmann T, Manhart S, Ludwig HH, Rosche F, et al. Isoaspartate residues dramatically influence substrate recognition and turnover by proteases. Biol Chem 2008; 389(8): 1043-53.
    • (2008) Biol Chem , vol.389 , Issue.8 , pp. 1043-1053
    • Böhme, L.1    Bär, J.W.2    Hoffmann, T.3    Manhart, S.4    Ludwig, H.H.5    Rosche, F.6
  • 90
    • 48249121176 scopus 로고    scopus 로고
    • New insights into the roles of endolysosomal cathepsins in the pathogenesis of Alzheimer's disease: Cathepsin inhibitors as potential therapeutics
    • Haque A, Banik NL and Ray SK. New insights into the roles of endolysosomal cathepsins in the pathogenesis of Alzheimer's disease: cathepsin inhibitors as potential therapeutics. CNS Neurol Disord Drug Targets 2008; 7(3): 270-7.
    • (2008) CNS Neurol Disord Drug Targets , vol.7 , Issue.3 , pp. 270-277
    • Haque, A.1    Banik, N.L.2    Ray, S.K.3
  • 91
    • 0028179364 scopus 로고
    • Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes
    • Kagan RM and Clarke S. Widespread occurrence of three sequence motifs in diverse S-adenosylmethionine-dependent methyltransferases suggests a common structure for these enzymes. Arch Biochem Biophys 1994; 310(2): 417-27.
    • (1994) Arch Biochem Biophys , vol.310 , Issue.2 , pp. 417-427
    • Kagan, R.M.1    Clarke, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.