메뉴 건너뛰기




Volumn 8, Issue 11, 2013, Pages

Isoaspartate accumulation in mouse brain is associated with altered patterns of protein phosphorylation and acetylation, some of which are highly sex-dependent

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA TUBULIN; BETA TUBULIN; COLLAPSIN RESPONSE MEDIATOR PROTEIN 2; DYNAMIN I; ISOASPARTIC ACID; PROTEIN DEXTRO ASPARTATE METHYLTRANSFERASE; SYNAPSIN I; SYNAPSIN II;

EID: 84892386029     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0080758     Document Type: Article
Times cited : (16)

References (54)
  • 1
    • 79958792815 scopus 로고    scopus 로고
    • Damaged proteins bearing Lisoaspartyl residues and aging: A dynamic equilibrium between generation of isomerized forms and repair by PIMT
    • doi:10.2174/1874612811104010008. PubMed: 21204776
    • Desrosiers RR, Fanélus I (2011) Damaged proteins bearing Lisoaspartyl residues and aging: a dynamic equilibrium between generation of isomerized forms and repair by PIMT. Curr Aging Sci 4: 8-18. doi:10.2174/1874612811104010008. PubMed: 21204776.
    • (2011) Curr Aging Sci , vol.4 , pp. 8-18
    • Desrosiers, R.R.1    Fanélus, I.2
  • 2
    • 24944532072 scopus 로고    scopus 로고
    • Biological significance of isoaspartate and its repair system
    • doi: 10.1248/bpb.28.1590. PubMed: 16141521
    • Shimizu T, Matsuoka Y, Shirasawa T (2005) Biological significance of isoaspartate and its repair system. Biol Pharm Bull 28: 1590-1596. doi: 10.1248/bpb.28.1590. PubMed: 16141521.
    • (2005) Biol Pharm Bull , vol.28 , pp. 1590-1596
    • Shimizu, T.1    Matsuoka, Y.2    Shirasawa, T.3
  • 3
    • 2542535235 scopus 로고    scopus 로고
    • Structure-dependent nonenzymatic deamidation of glutaminyl and asparaginyl pentapeptides
    • doi: 10.1111/j.1399-3011.2004.00151.x. PubMed: 15140160
    • Robinson NE, Robinson ZW, Robinson BR, Robinson AL, Robinson JA et al. (2004) Structure-dependent nonenzymatic deamidation of glutaminyl and asparaginyl pentapeptides. J Pept Res 63: 426-436. doi: 10.1111/j.1399-3011. 2004.00151.x. PubMed: 15140160.
    • (2004) J Pept Res , vol.63 , pp. 426-436
    • Robinson, N.E.1    Robinson, Z.W.2    Robinson, B.R.3    Robinson, A.L.4    Robinson, J.A.5
  • 4
    • 0041367295 scopus 로고    scopus 로고
    • Deamidation and isoaspartate formation in proteins: Unwanted alterations or surreptitious signals?
    • doi:10.1007/s00018-003-2287-5. PubMed: 12943218
    • Reissner KJ, Aswad DW (2003) Deamidation and isoaspartate formation in proteins: unwanted alterations or surreptitious signals? Cell Mol Life Sci 60: 1281-1295. doi:10.1007/s00018-003-2287-5. PubMed: 12943218.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1281-1295
    • Reissner, K.J.1    Aswad, D.W.2
  • 5
    • 0348099030 scopus 로고    scopus 로고
    • Aging as war between chemical and biochemical processes: Protein methylation and the recognition of age-damaged proteins for repair
    • doi:10.1016/S1568-1637(03)00011-4. PubMed: 12726775
    • Clarke S (2003) Aging as war between chemical and biochemical processes: protein methylation and the recognition of age-damaged proteins for repair. Ageing Res Rev 2: 263-285. doi:10.1016/S1568-1637(03)00011-4. PubMed: 12726775.
    • (2003) Ageing Res Rev , vol.2 , pp. 263-285
    • Clarke, S.1
  • 6
    • 0034885731 scopus 로고    scopus 로고
    • Age-dependent deamidation of asparagine residues in proteins
    • doi: 10.1016/S0531-5565(01)00140-1. PubMed: 11525877
    • Lindner H, Helliger W (2001) Age-dependent deamidation of asparagine residues in proteins. Exp Gerontol 36: 1551-1563. doi: 10.1016/S0531-5565(01) 00140-1. PubMed: 11525877.
    • (2001) Exp Gerontol , vol.36 , pp. 1551-1563
    • Lindner, H.1    Helliger, W.2
  • 7
    • 0031241608 scopus 로고    scopus 로고
    • Degradative covalent reactions important to protein stability
    • doi: 10.1007/BF02752255. PubMed: 9406181
    • Volkin DB, Mach H, Middaugh CR (1997) Degradative covalent reactions important to protein stability. Mol Biotechnol 8: 105-122. doi: 10.1007/BF02752255. PubMed: 9406181.
    • (1997) Mol Biotechnol , vol.8 , pp. 105-122
    • Volkin, D.B.1    Mach, H.2    Middaugh, C.R.3
  • 8
    • 0021759664 scopus 로고
    • Stoichiometric methylation of porcine adrenocorticotropin by protein carboxyl methyltransferase requires deamidation of asparagine 25. Evidence for methylation at the alphacarboxyl group of atypical L-isoaspartyl residues
    • PubMed: 6088513
    • Aswad DW (1984) Stoichiometric methylation of porcine adrenocorticotropin by protein carboxyl methyltransferase requires deamidation of asparagine 25. Evidence for methylation at the alphacarboxyl group of atypical L-isoaspartyl residues. J Biol Chem 259: 10714-10721. PubMed: 6088513.
    • (1984) J Biol Chem , vol.259 , pp. 10714-10721
    • Aswad, D.W.1
  • 9
    • 0021759648 scopus 로고
    • Synthetic peptide substrates for the erythrocyte protein carboxyl methyltransferase. Detection of a new site of methylation at isomerized L-aspartyl residues
    • PubMed: 6469980
    • Murray ED Jr., Clarke S (1984) Synthetic peptide substrates for the erythrocyte protein carboxyl methyltransferase. Detection of a new site of methylation at isomerized L-aspartyl residues. J Biol Chem 259: 10722-10732. PubMed: 6469980.
    • (1984) J Biol Chem , vol.259 , pp. 10722-10732
    • Murray Jr., E.D.1    Clarke, S.2
  • 10
    • 0025788030 scopus 로고
    • Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides
    • PubMed: 1939272
    • Tyler-Cross R, Schirch V (1991) Effects of amino acid sequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides. J Biol Chem 266: 22549-22556. PubMed: 1939272.
    • (1991) J Biol Chem , vol.266 , pp. 22549-22556
    • Tyler-Cross, R.1    Schirch, V.2
  • 11
    • 0021810201 scopus 로고
    • Enzymatic protein carboxyl methylation at physiological pH: Cyclic imide formation explains rapid methyl turnover
    • doi:10.1021/bi00331a028. PubMed: 4016073
    • Johnson BA, Aswad DW (1985) Enzymatic protein carboxyl methylation at physiological pH: cyclic imide formation explains rapid methyl turnover. Biochemistry 24: 2581-2586. doi:10.1021/bi00331a028. PubMed: 4016073.
    • (1985) Biochemistry , vol.24 , pp. 2581-2586
    • Johnson, B.A.1    Aswad, D.W.2
  • 12
    • 0023109951 scopus 로고
    • Deamidation, isomerization, and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation
    • PubMed: 3805008
    • 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: 785-794. PubMed: 3805008.
    • (1987) J Biol Chem , vol.262 , pp. 785-794
    • Geiger, T.1    Clarke, S.2
  • 13
    • 0023664284 scopus 로고
    • Protein carboxyl methyltransferase facilitates conversion of atypical Lisoaspartyl peptides to normal L-aspartyl peptides
    • PubMed: 3571226
    • Johnson BA, Murray ED Jr., Clarke S, Glass DB, Aswad DW (1987) Protein carboxyl methyltransferase facilitates conversion of atypical Lisoaspartyl peptides to normal L-aspartyl peptides. J Biol Chem 262: 5622-5629. PubMed: 3571226.
    • (1987) J Biol Chem , vol.262 , pp. 5622-5629
    • Johnson, B.A.1    Murray Jr., E.D.2    Clarke, S.3    Glass, D.B.4    Aswad, D.W.5
  • 14
    • 0023645473 scopus 로고
    • Partial repair of deamidation-damaged calmodulin by protein carboxyl methyltransferase
    • PubMed: 3624258
    • Johnson BA, Langmack EL, Aswad DW (1987) Partial repair of deamidation-damaged calmodulin by protein carboxyl methyltransferase. J Biol Chem 262: 12283-12287. PubMed: 3624258.
    • (1987) J Biol Chem , vol.262 , pp. 12283-12287
    • Johnson, B.A.1    Langmack, E.L.2    Aswad, D.W.3
  • 15
    • 0008123901 scopus 로고
    • Conversion of isoaspartyl peptides to normal peptides: Implications for the cellular repair of damaged proteins
    • doi:10.1073/pnas.84.9.2595. PubMed: 3472227
    • McFadden PN, Clarke S (1987) Conversion of isoaspartyl peptides to normal peptides: implications for the cellular repair of damaged proteins. Proc Natl Acad Sci U S A 84: 2595-2599. doi:10.1073/pnas.84.9.2595. PubMed: 3472227.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 2595-2599
    • McFadden, P.N.1    Clarke, S.2
  • 16
    • 0023860707 scopus 로고
    • Repair of isopeptide bonds by protein carboxyl O-methyltransferase: Seminal ribonuclease as a model system
    • doi:10.1021/bi00405a055. PubMed: 3365422
    • Galletti P, Ciardiello A, Ingrosso D, Di Donato A, D'Alessio G (1988) Repair of isopeptide bonds by protein carboxyl O-methyltransferase: seminal ribonuclease as a model system. Biochemistry 27: 1752-1757. doi:10.1021/ bi00405a055. PubMed: 3365422.
    • (1988) Biochemistry , vol.27 , pp. 1752-1757
    • Galletti, P.1    Ciardiello, A.2    Ingrosso, D.3    Di Donato, A.4    D'Alessio, G.5
  • 17
    • 0027992730 scopus 로고
    • Repair of spontaneously deamidated HPr phosphocarrier protein catalyzed by the L-isoaspartate-(D-aspartate) O-methyltransferase
    • PubMed: 7929130
    • Brennan TV, Anderson JW, Jia Z, Waygood EB, Clarke S (1994) Repair of spontaneously deamidated HPr phosphocarrier protein catalyzed by the L-isoaspartate-(D-aspartate) O-methyltransferase. J Biol Chem 269: 24586-24595. PubMed: 7929130.
    • (1994) J Biol Chem , vol.269 , pp. 24586-24595
    • Brennan, T.V.1    Anderson, J.W.2    Jia, Z.3    Waygood, E.B.4    Clarke, S.5
  • 18
    • 0027414075 scopus 로고
    • Accumulation of substrates for protein L-isoaspartyl methyltransferase in adenosine dialdehyde-treated PC12 cells
    • PubMed: 8454593
    • Johnson BA, Najbauer J, Aswad DW (1993) Accumulation of substrates for protein L-isoaspartyl methyltransferase in adenosine dialdehyde-treated PC12 cells. J Biol Chem 268: 6174-6181. PubMed: 8454593.
    • (1993) J Biol Chem , vol.268 , pp. 6174-6181
    • Johnson, B.A.1    Najbauer, J.2    Aswad, D.W.3
  • 19
    • 0030995490 scopus 로고    scopus 로고
    • Deficiency of a protein-repair enzyme results in the accumulation of altered proteins, retardation of growth, and fatal seizures in mice
    • doi:10.1073/pnas.94.12.6132. PubMed: 9177182
    • Kim E, Lowenson JD, MacLaren DC, Clarke S, Young SG (1997) Deficiency of a protein-repair enzyme results in the accumulation of altered proteins, retardation of growth, and fatal seizures in mice. Proc Natl Acad Sci U S A 94: 6132-6137. doi:10.1073/pnas.94.12.6132. PubMed: 9177182.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 6132-6137
    • Kim, E.1    Lowenson, J.D.2    MacLaren, D.C.3    Clarke, S.4    Young, S.G.5
  • 20
    • 0032520844 scopus 로고    scopus 로고
    • Deficiency in protein L-isoaspartyl methyltransferase results in a fatal progressive epilepsy
    • PubMed: 9482793
    • Yamamoto A, Takagi H, Kitamura D, Tatsuoka H, Nakano H et al. (1998) Deficiency in protein L-isoaspartyl methyltransferase results in a fatal progressive epilepsy. J Neurosci 18: 2063-2074. PubMed: 9482793.
    • (1998) J Neurosci , vol.18 , pp. 2063-2074
    • Yamamoto, A.1    Takagi, H.2    Kitamura, D.3    Tatsuoka, H.4    Nakano, H.5
  • 21
    • 42749084972 scopus 로고    scopus 로고
    • Suppression of protein l-isoaspartyl (d-aspartyl) methyltransferase results in hyperactivation of EGF-stimulated MEK-ERK signaling in cultured mammalian cells
    • doi:10.1016/j.bbrc.2008.03.109. PubMed: 18381200
    • Kosugi S, Furuchi T, Katane M, Sekine M, Shirasawa T et al. (2008) Suppression of protein l-isoaspartyl (d-aspartyl) methyltransferase results in hyperactivation of EGF-stimulated MEK-ERK signaling in cultured mammalian cells. Biochem Biophys Res Commun 371: 22-27. doi:10.1016/j.bbrc.2008.03.109. PubMed: 18381200.
    • (2008) Biochem Biophys Res Commun , vol.371 , pp. 22-27
    • Kosugi, S.1    Furuchi, T.2    Katane, M.3    Sekine, M.4    Shirasawa, T.5
  • 22
    • 0017074189 scopus 로고
    • Regional and subcellular distribution of protein carboxymethylase in brain and other tissues
    • doi:10.1111/j.1471-4159.1976.tb07001.x. PubMed: 6627
    • Diliberto EJ Jr., Axelrod J (1976) Regional and subcellular distribution of protein carboxymethylase in brain and other tissues. J Neurochem 26: 1159-1165. doi:10.1111/j.1471-4159.1976.tb07001.x. PubMed: 6627.
    • (1976) J Neurochem , vol.26 , pp. 1159-1165
    • Diliberto Jr., E.J.1    Axelrod, J.2
  • 23
    • 0028979610 scopus 로고
    • Immunochemical characterization of L-isoaspartyl-protein carboxyl methyltransferase from mammalian tissues
    • PubMed: 7639720
    • Boivin D, Bilodeau D, Béliveau R (1995) Immunochemical characterization of L-isoaspartyl-protein carboxyl methyltransferase from mammalian tissues. Biochem J 309 (3): 993-998. PubMed: 7639720.
    • (1995) Biochem J , vol.309 , Issue.3 , pp. 993-998
    • Boivin, D.1    Bilodeau, D.2    Béliveau, R.3
  • 24
    • 0033575260 scopus 로고    scopus 로고
    • Phenotypic analysis of seizure-prone mice lacking L-isoaspartate (D-aspartate) Omethyltransferase
    • doi:10.1074/jbc.274.29.20671. PubMed: 10400700
    • Kim E, Lowenson JD, Clarke S, Young SG (1999) Phenotypic analysis of seizure-prone mice lacking L-isoaspartate (D-aspartate) Omethyltransferase. J Biol Chem 274: 20671-20678. doi:10.1074/jbc.274.29.20671. PubMed: 10400700.
    • (1999) J Biol Chem , vol.274 , pp. 20671-20678
    • Kim, E.1    Lowenson, J.D.2    Clarke, S.3    Young, S.G.4
  • 25
    • 0034932858 scopus 로고    scopus 로고
    • Aberrant synaptic transmission in the hippocampal CA3 region and cognitive deterioration in protein-repair enzyme-deficient mice
    • doi:10.1002/hipo.1043. PubMed: 11769310
    • Ikegaya Y, Yamada M, Fukuda T, Kuroyanagi H, Shirasawa T et al. (2001) Aberrant synaptic transmission in the hippocampal CA3 region and cognitive deterioration in protein-repair enzyme-deficient mice. Hippocampus 11: 287-298. doi:10.1002/hipo.1043. PubMed: 11769310.
    • (2001) Hippocampus , vol.11 , pp. 287-298
    • Ikegaya, Y.1    Yamada, M.2    Fukuda, T.3    Kuroyanagi, H.4    Shirasawa, T.5
  • 26
    • 3042546080 scopus 로고    scopus 로고
    • Improved rotorod performance and hyperactivity in mice deficient in a protein repair methyltransferase
    • doi:10.1016/j.bbr.2003.11.007. PubMed: 15219714
    • Vitali R, Clarke S (2004) Improved rotorod performance and hyperactivity in mice deficient in a protein repair methyltransferase. Behav Brain Res 153: 129-141. doi:10.1016/j.bbr.2003.11.007. PubMed: 15219714.
    • (2004) Behav Brain Res , vol.153 , pp. 129-141
    • Vitali, R.1    Clarke, S.2
  • 27
    • 53249144153 scopus 로고    scopus 로고
    • Formation, localization, and repair of Lisoaspartyl sites in histones H2A and H2B in nucleosomes from rat liver and chicken erythrocytes
    • doi:10.1021/bi8013467. PubMed: 18795804
    • Carter WG, Aswad DW (2008) Formation, localization, and repair of Lisoaspartyl sites in histones H2A and H2B in nucleosomes from rat liver and chicken erythrocytes. Biochemistry 47: 10757-10764. doi:10.1021/bi8013467. PubMed: 18795804.
    • (2008) Biochemistry , vol.47 , pp. 10757-10764
    • Carter, W.G.1    Aswad, D.W.2
  • 28
    • 0035813128 scopus 로고    scopus 로고
    • Structural integrity of histone H2B in vivo requires the activity of protein L-isoaspartyl O-methyltransferase, a putative repair enzyme
    • doi:10.1074/jbc.M106682200. PubMed: 11479322
    • Young AL, Carter WG, Doyle HA, Mamula MJ, Aswad DW (2001) Structural integrity of histone H2B in vivo requires the activity of protein L-isoaspartyl O-methyltransferase, a putative repair enzyme. J Biol Chem 276: 37161-37165. doi:10.1074/jbc.M106682200. PubMed: 11479322.
    • (2001) J Biol Chem , vol.276 , pp. 37161-37165
    • Young, A.L.1    Carter, W.G.2    Doyle, H.A.3    Mamula, M.J.4    Aswad, D.W.5
  • 29
    • 77949554923 scopus 로고    scopus 로고
    • Postnatal deamidation of 4E-BP2 in brain enhances its association with raptor and alters kinetics of excitatory synaptic transmission
    • doi:10.1016/j.molcel.2010.02.022. PubMed: 20347422
    • Bidinosti M, Ran I, Sanchez-Carbente MR, Martineau Y, Gingras AC et al. (2010) Postnatal deamidation of 4E-BP2 in brain enhances its association with raptor and alters kinetics of excitatory synaptic transmission. Mol Cell 37: 797-808. doi:10.1016/j.molcel.2010.02.022. PubMed: 20347422.
    • (2010) Mol Cell , vol.37 , pp. 797-808
    • Bidinosti, M.1    Ran, I.2    Sanchez-Carbente, M.R.3    Martineau, Y.4    Gingras, A.C.5
  • 30
    • 77953499323 scopus 로고    scopus 로고
    • Repair of isoaspartate formation modulates the interaction of deamidated 4E-BP2 with mTORC1 in brain
    • doi:10.1074/jbc.M110.120774. PubMed: 20424163
    • Bidinosti M, Martineau Y, Frank F, Sonenberg N (2010) Repair of isoaspartate formation modulates the interaction of deamidated 4E-BP2 with mTORC1 in brain. J Biol Chem 285: 19402-19408. doi:10.1074/jbc.M110.120774. PubMed: 20424163.
    • (2010) J Biol Chem , vol.285 , pp. 19402-19408
    • Bidinosti, M.1    Martineau, Y.2    Frank, F.3    Sonenberg, N.4
  • 31
    • 23844547049 scopus 로고    scopus 로고
    • Activation of the PI3K/Akt signal transduction pathway and increased levels of insulin receptor in protein repair-deficient mice
    • doi:10.1111/j.1474-9728.2004.00136.x. PubMed: 15659208
    • Farrar C, Houser CR, Clarke S (2005) Activation of the PI3K/Akt signal transduction pathway and increased levels of insulin receptor in protein repair-deficient mice. Aging Cell 4: 1-12. doi:10.1111/j.1474-9728.2004.00136.x. PubMed: 15659208.
    • (2005) Aging Cell , vol.4 , pp. 1-12
    • Farrar, C.1    Houser, C.R.2    Clarke, S.3
  • 32
    • 33845918167 scopus 로고    scopus 로고
    • Protein repair in the brain, proteomic analysis of endogenous substrates for protein Lisoaspartyl methyltransferase in mouse brain
    • doi:10.1074/jbc.M606958200. PubMed: 16959769
    • Zhu JX, Doyle HA, Mamula MJ, Aswad DW (2006) Protein repair in the brain, proteomic analysis of endogenous substrates for protein Lisoaspartyl methyltransferase in mouse brain. J Biol Chem 281: 33802-33813. doi:10.1074/jbc.M606958200. PubMed: 16959769.
    • (2006) J Biol Chem , vol.281 , pp. 33802-33813
    • Zhu, J.X.1    Doyle, H.A.2    Mamula, M.J.3    Aswad, D.W.4
  • 33
    • 71749109184 scopus 로고    scopus 로고
    • Acquisition of chemiluminescent signals from immunoblots with a digital single-lens reflex camera
    • doi:10.1016/j.ab. 2009.09.041. PubMed: 19788886
    • Khoury MK, Parker I, Aswad DW (2010) Acquisition of chemiluminescent signals from immunoblots with a digital single-lens reflex camera. Anal Biochem 397: 129-131. doi:10.1016/j.ab. 2009.09.041. PubMed: 19788886.
    • (2010) Anal Biochem , vol.397 , pp. 129-131
    • Khoury, M.K.1    Parker, I.2    Aswad, D.W.3
  • 34
    • 77954202334 scopus 로고    scopus 로고
    • The synapsins: Key actors of synapse function and plasticity
    • doi:10.1016/j.pneurobio.2010.04.006. PubMed: 20438797
    • Cesca F, Baldelli P, Valtorta F, Benfenati F (2010) The synapsins: key actors of synapse function and plasticity. Prog Neurobiol 91: 313-348. doi:10.1016/j.pneurobio.2010.04.006. PubMed: 20438797.
    • (2010) Prog Neurobiol , vol.91 , pp. 313-348
    • Cesca, F.1    Baldelli, P.2    Valtorta, F.3    Benfenati, F.4
  • 35
    • 84856111189 scopus 로고    scopus 로고
    • Dynamin, a membrane-remodelling GTPase
    • PubMed: 22233676
    • Ferguson SM, De Camilli P (2012) Dynamin, a membrane-remodelling GTPase. Nat Rev Mol Cell Biol 13: 75-88. PubMed: 22233676.
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 75-88
    • Ferguson, S.M.1    De Camilli, P.2
  • 36
    • 79958282898 scopus 로고    scopus 로고
    • Collapsin response mediator protein-2: An emerging pathologic feature and therapeutic target for neurodisease indications
    • doi:10.1007/s12035-011-8166-4. PubMed: 21271304
    • Hensley K, Venkova K, Christov A, Gunning W, Park J (2011) Collapsin response mediator protein-2: an emerging pathologic feature and therapeutic target for neurodisease indications. Mol Neurobiol 43: 180-191. doi:10.1007/s12035-011-8166-4. PubMed: 21271304.
    • (2011) Mol Neurobiol , vol.43 , pp. 180-191
    • Hensley, K.1    Venkova, K.2    Christov, A.3    Gunning, W.4    Park, J.5
  • 37
    • 47749087436 scopus 로고    scopus 로고
    • DARPP-32: Molecular integration of phosphorylation potential
    • doi:10.1007/s00018-008-8150-y. PubMed: 18488140
    • Le Novère N, Li L, Girault JA (2008) DARPP-32: molecular integration of phosphorylation potential. Cell Mol Life Sci 65: 2125-2127. doi:10.1007/s00018-008-8150-y. PubMed: 18488140.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2125-2127
    • Le Novère, N.1    Li, L.2    Girault, J.A.3
  • 38
    • 0023608514 scopus 로고
    • Tubulin and high molecular weight microtubule-associated proteins as endogenous substrates for protein carboxymethyltransferase in brain
    • doi:10.1016/0300-9084(87)90150-7. PubMed: 3129027
    • Ohta K, Seo N, Yoshida T, Hiraga K, Tuboi S (1987) Tubulin and high molecular weight microtubule-associated proteins as endogenous substrates for protein carboxymethyltransferase in brain. Biochimie 69: 1227-1234. doi:10.1016/0300-9084(87)90150-7. PubMed: 3129027.
    • (1987) Biochimie , vol.69 , pp. 1227-1234
    • Ohta, K.1    Seo, N.2    Yoshida, T.3    Hiraga, K.4    Tuboi, S.5
  • 39
    • 79951855247 scopus 로고    scopus 로고
    • The ins and outs of tubulin acetylation: More than just a post-translational modification?
    • doi:10.1016/j.cellsig.2010.10.014. PubMed: 20940043
    • Perdiz D, Mackeh R, Poüs C, Baillet A (2011) The ins and outs of tubulin acetylation: more than just a post-translational modification? Cell Signal 23: 763-771. doi:10.1016/j.cellsig.2010.10.014. PubMed: 20940043.
    • (2011) Cell Signal , vol.23 , pp. 763-771
    • Perdiz, D.1    Mackeh, R.2    Poüs, C.3    Baillet, A.4
  • 40
    • 0029059605 scopus 로고
    • Impairment of synaptic vesicle clustering and of synaptic transmission, and increased seizure propensity, in synapsin I-deficient mice
    • doi:10.1073/pnas.92.20.9235. PubMed: 7568108
    • Li L, Chin LS, Shupliakov O, Brodin L, Sihra TS et al. (1995) Impairment of synaptic vesicle clustering and of synaptic transmission, and increased seizure propensity, in synapsin I-deficient mice. Proc Natl Acad Sci U S A 92: 9235-9239. doi:10.1073/pnas.92.20.9235. PubMed: 7568108.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 9235-9239
    • Li, L.1    Chin, L.S.2    Shupliakov, O.3    Brodin, L.4    Sihra, T.S.5
  • 41
    • 55049101007 scopus 로고    scopus 로고
    • Synapsin-I- and synapsin-II-null mice display an increased age-dependent cognitive impairment
    • doi: 10.1242/jcs.035063. PubMed: 18713831
    • Corradi A, Zanardi A, Giacomini C, Onofri F, Valtorta F et al. (2008) Synapsin-I- and synapsin-II-null mice display an increased age-dependent cognitive impairment. J Cell Sci 121: 3042-3051. doi: 10.1242/jcs.035063. PubMed: 18713831.
    • (2008) J Cell Sci , vol.121 , pp. 3042-3051
    • Corradi, A.1    Zanardi, A.2    Giacomini, C.3    Onofri, F.4    Valtorta, F.5
  • 42
    • 10644264473 scopus 로고    scopus 로고
    • Different presynaptic roles of synapsins at excitatory and inhibitory synapses
    • doi:10.1523/JNEUROSCI.3795-04.2004. PubMed: 15601943
    • Gitler D, Takagishi Y, Feng J, Ren Y, Rodriguiz RM et al. (2004) Different presynaptic roles of synapsins at excitatory and inhibitory synapses. J Neurosci 24: 11368-11380. doi:10.1523/JNEUROSCI.3795-04.2004. PubMed: 15601943.
    • (2004) J Neurosci , vol.24 , pp. 11368-11380
    • Gitler, D.1    Takagishi, Y.2    Feng, J.3    Ren, Y.4    Rodriguiz, R.M.5
  • 43
    • 33646833620 scopus 로고    scopus 로고
    • Synapsin I is a major endogenous substrate for protein Lisoaspartyl methyltransferase in mammalian brain
    • doi:10.1074/jbc.M510716200. PubMed: 16443604
    • Reissner KJ, Paranandi MV, Luc TM, Doyle HA, Mamula MJ et al. (2006) Synapsin I is a major endogenous substrate for protein Lisoaspartyl methyltransferase in mammalian brain. J Biol Chem 281: 8389-8398. doi:10.1074/jbc.M510716200. PubMed: 16443604.
    • (2006) J Biol Chem , vol.281 , pp. 8389-8398
    • Reissner, K.J.1    Paranandi, M.V.2    Luc, T.M.3    Doyle, H.A.4    Mamula, M.J.5
  • 44
    • 0024506755 scopus 로고
    • Electrostatic and Hydrophobic Interactions of Synapsin I and Synapsin I Fragments with Phospholipid Bilayers
    • doi:10.1083/jcb.108.5.1851. PubMed: 2497105
    • Benfenati F, Greengard P, Brunner J, Bähler M (1989) Electrostatic and Hydrophobic Interactions of Synapsin I and Synapsin I Fragments with Phospholipid Bilayers. J Cell Biol 108: 1851-1862. doi:10.1083/jcb.108.5.1851. PubMed: 2497105.
    • (1989) J Cell Biol , vol.108 , pp. 1851-1862
    • Benfenati, F.1    Greengard, P.2    Brunner, J.3    Bähler, M.4
  • 45
    • 0030729884 scopus 로고    scopus 로고
    • Kinetic analysis of the phosphorylation-dependent interactions of synapsin I with rat brain synaptic vesicles
    • doi: 10.1111/j.1469-7793.1997.501bd.x. PubMed: 9401959
    • Stefani G, Onofri F, Valtorta F, Vaccaro P, Greengard P et al. (1997) Kinetic analysis of the phosphorylation-dependent interactions of synapsin I with rat brain synaptic vesicles. J Physiol 504: 501-515. doi: 10.1111/j.1469-7793.1997.501bd.x. PubMed: 9401959.
    • (1997) J Physiol , vol.504 , pp. 501-515
    • Stefani, G.1    Onofri, F.2    Valtorta, F.3    Vaccaro, P.4    Greengard, P.5
  • 46
    • 0035865590 scopus 로고    scopus 로고
    • Identification of synapsin I peptides that insert into lipid membranes
    • doi:10.1042/0264-6021:3540057. PubMed: 11171079
    • Cheetham JJ, Hilfiker S, Benfenati F, Weber T, Greengard P et al. (2001) Identification of synapsin I peptides that insert into lipid membranes. Biochem J 354: 57-66. doi:10.1042/0264-6021:3540057. PubMed: 11171079.
    • (2001) Biochem J , vol.354 , pp. 57-66
    • Cheetham, J.J.1    Hilfiker, S.2    Benfenati, F.3    Weber, T.4    Greengard, P.5
  • 47
    • 0033213603 scopus 로고    scopus 로고
    • A phospho-switch controls the dynamic association of synapsins with synaptic vesicles
    • doi:10.1016/S0896-6273(00)80851-X. PubMed: 10571231
    • Hosaka M, Hammer RE, Südhof TC (1999) A phospho-switch controls the dynamic association of synapsins with synaptic vesicles. Neuron 24: 377-387. doi:10.1016/S0896-6273(00)80851-X. PubMed: 10571231.
    • (1999) Neuron , vol.24 , pp. 377-387
    • Hosaka, M.1    Hammer, R.E.2    Südhof, T.C.3
  • 48
    • 0018647023 scopus 로고
    • Regulation of the state of phosphorylation of specific neuronal proteins in mouse brain by in vivo administration of anesthetic and convulsant agents
    • doi:10.1073/pnas.76.9.4687. PubMed: 291996
    • Strömbom U, Forn J, Dolphin AC, Greengard P (1979) Regulation of the state of phosphorylation of specific neuronal proteins in mouse brain by in vivo administration of anesthetic and convulsant agents. Proc Natl Acad Sci U S A 76: 4687-4690. doi:10.1073/pnas.76.9.4687. PubMed: 291996.
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 4687-4690
    • Strömbom, U.1    Forn, J.2    Dolphin, A.C.3    Greengard, P.4
  • 49
    • 0028833705 scopus 로고
    • Increase in synapsin I phosphorylation implicates a presynaptic component in septal kindling
    • doi:10.1016/0306-4522(94)00492-N. PubMed: 7708197
    • Yamagata Y, Obata K, Greengard P, Czernik AJ (1995) Increase in synapsin I phosphorylation implicates a presynaptic component in septal kindling. Neuroscience 64: 1-4. doi:10.1016/0306-4522(94)00492-N. PubMed: 7708197.
    • (1995) Neuroscience , vol.64 , pp. 1-4
    • Yamagata, Y.1    Obata, K.2    Greengard, P.3    Czernik, A.J.4
  • 50
    • 0030434262 scopus 로고    scopus 로고
    • Increased in vivo phosphorylation state of neuromodulin and synapsin I in striatum from rats treated with repeated amphetamine
    • PubMed: 8819530
    • Iwata S, Hewlett GH, Ferrell ST, Czernik AJ, Meiri KF et al. (1996) Increased in vivo phosphorylation state of neuromodulin and synapsin I in striatum from rats treated with repeated amphetamine. J Pharmacol Exp Ther 278: 1428-1434. PubMed: 8819530.
    • (1996) J Pharmacol Exp Ther , vol.278 , pp. 1428-1434
    • Iwata, S.1    Hewlett, G.H.2    Ferrell, S.T.3    Czernik, A.J.4    Meiri, K.F.5
  • 51
    • 72849131622 scopus 로고    scopus 로고
    • Sex differences in molecular neuroscience: From fruit flies to humans
    • doi:10.1038/nrn2754. PubMed: 20019686
    • Jazin E, Cahill L (2010) Sex differences in molecular neuroscience: from fruit flies to humans. Nat Rev Neurosci 11: 9-17. doi:10.1038/nrn2754. PubMed: 20019686.
    • (2010) Nat Rev Neurosci , vol.11 , pp. 9-17
    • Jazin, E.1    Cahill, L.2
  • 52
    • 84861313753 scopus 로고    scopus 로고
    • A half-truth is a whole lie: On the necessity of investigating sex influences on the brain
    • doi:10.1210/en.2011-2167. PubMed: 22492307
    • Cahill L (2012) A half-truth is a whole lie: on the necessity of investigating sex influences on the brain. Endocrinology 153: 2541-2543. doi:10.1210/en.2011-2167. PubMed: 22492307.
    • (2012) Endocrinology , vol.153 , pp. 2541-2543
    • Cahill, L.1
  • 53
    • 0029876218 scopus 로고    scopus 로고
    • Molecular aging of tubulin: Accumulation of isoaspartyl sites in vitro and in vivo
    • doi:10.1021/bi953063g. PubMed: 8611502
    • Najbauer J, Orpiszewski J, Aswad DW (1996) Molecular aging of tubulin: accumulation of isoaspartyl sites in vitro and in vivo. Biochemistry 35: 5183-5190. doi:10.1021/bi953063g. PubMed: 8611502.
    • (1996) Biochemistry , vol.35 , pp. 5183-5190
    • Najbauer, J.1    Orpiszewski, J.2    Aswad, D.W.3
  • 54
    • 0036667931 scopus 로고    scopus 로고
    • Inclusion of phosphatase inhibitors during Western blotting enhances signal detection with phospho-specific antibodies
    • doi:10.1016/S0003-2697(02)00008-8. PubMed: 12137799
    • Sharma SK, Carew TJ (2002) Inclusion of phosphatase inhibitors during Western blotting enhances signal detection with phospho-specific antibodies. Anal Biochem 307: 187-189. doi:10.1016/S0003-2697(02)00008-8. PubMed: 12137799.
    • (2002) Anal Biochem , vol.307 , pp. 187-189
    • Sharma, S.K.1    Carew, T.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.