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Volumn 33, Issue 11, 2010, Pages 493-502

Protein modifications involved in neurotransmitter and gasotransmitter signaling

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; CYCLIC AMP; CYSTEINE; HYDROGEN SULFIDE; LYSINE; MEMBRANE RECEPTOR; NEUROTRANSMITTER; NITRIC OXIDE;

EID: 77958158351     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tins.2010.07.004     Document Type: Review
Times cited : (48)

References (120)
  • 1
    • 75049085878 scopus 로고    scopus 로고
    • New insight into the functioning of nitric oxide-receptive guanylyl cyclase: physiological and pharmacological implications
    • Garthwaite J. New insight into the functioning of nitric oxide-receptive guanylyl cyclase: physiological and pharmacological implications. Mol. Cell Biochem. 2010, 334:221-232.
    • (2010) Mol. Cell Biochem. , vol.334 , pp. 221-232
    • Garthwaite, J.1
  • 2
    • 0031932281 scopus 로고    scopus 로고
    • CAPON: a protein associated with neuronal nitric oxide synthase that regulates its interactions with PSD95
    • Jaffrey S.R., et al. CAPON: a protein associated with neuronal nitric oxide synthase that regulates its interactions with PSD95. Neuron 1998, 20:115-124.
    • (1998) Neuron , vol.20 , pp. 115-124
    • Jaffrey, S.R.1
  • 3
    • 74949103637 scopus 로고    scopus 로고
    • H2S signals through protein S-sulfhydration
    • Mustafa A.K. H2S signals through protein S-sulfhydration. Sci. Signal. 2009, 2:ra72.
    • (2009) Sci. Signal. , vol.2
    • Mustafa, A.K.1
  • 4
    • 67651165474 scopus 로고    scopus 로고
    • Palmitoylation of the synaptic vesicle fusion machinery
    • Prescott G.R., et al. Palmitoylation of the synaptic vesicle fusion machinery. J. Neurochem. 2009, 110:1135-1149.
    • (2009) J. Neurochem. , vol.110 , pp. 1135-1149
    • Prescott, G.R.1
  • 5
    • 0034051227 scopus 로고    scopus 로고
    • Acetylation of histones and transcription-related factors
    • Sterner D.E., Berger S.L. Acetylation of histones and transcription-related factors. Microbiol. Mol. Biol. Rev. 2000, 64:435-459.
    • (2000) Microbiol. Mol. Biol. Rev. , vol.64 , pp. 435-459
    • Sterner, D.E.1    Berger, S.L.2
  • 6
    • 56049090769 scopus 로고    scopus 로고
    • Acetylation of non-histone proteins modulates cellular signalling at multiple levels
    • Spange S., et al. Acetylation of non-histone proteins modulates cellular signalling at multiple levels. Int. J. Biochem. Cell Biol. 2009, 41:185-198.
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 185-198
    • Spange, S.1
  • 7
    • 70350041309 scopus 로고    scopus 로고
    • Protein SUMOylation in neuropathological conditions
    • Anderson D.B., et al. Protein SUMOylation in neuropathological conditions. Drug News Perspect. 2009, 22:255-265.
    • (2009) Drug News Perspect. , vol.22 , pp. 255-265
    • Anderson, D.B.1
  • 8
    • 13444282230 scopus 로고    scopus 로고
    • Protein S-nitrosylation: purview and parameters
    • Hess D.T., et al. Protein S-nitrosylation: purview and parameters. Nat. Rev. Mol. Cell Biol. 2005, 6:150-166.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 150-166
    • Hess, D.T.1
  • 9
    • 0035147435 scopus 로고    scopus 로고
    • Protein S-nitrosylation: a physiological signal for neuronal nitric oxide
    • Jaffrey S.R., et al. Protein S-nitrosylation: a physiological signal for neuronal nitric oxide. Nat. Cell Biol. 2001, 3:193-197.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 193-197
    • Jaffrey, S.R.1
  • 10
    • 0033995950 scopus 로고    scopus 로고
    • Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation
    • Choi Y.B., et al. Molecular basis of NMDA receptor-coupled ion channel modulation by S-nitrosylation. Nat. Neurosci. 2000, 3:15-21.
    • (2000) Nat. Neurosci. , vol.3 , pp. 15-21
    • Choi, Y.B.1
  • 11
    • 13344277364 scopus 로고    scopus 로고
    • Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains
    • Brenman J.E., et al. Interaction of nitric oxide synthase with the postsynaptic density protein PSD-95 and alpha1-syntrophin mediated by PDZ domains. Cell 1996, 84:757-767.
    • (1996) Cell , vol.84 , pp. 757-767
    • Brenman, J.E.1
  • 12
    • 67349230279 scopus 로고    scopus 로고
    • Neuronal nitric oxide synthase: structure, subcellular localization, regulation, and clinical implications
    • Zhou L., Zhu D.Y. Neuronal nitric oxide synthase: structure, subcellular localization, regulation, and clinical implications. Nitric Oxide 2009, 20:223-230.
    • (2009) Nitric Oxide , vol.20 , pp. 223-230
    • Zhou, L.1    Zhu, D.Y.2
  • 13
    • 0036752945 scopus 로고    scopus 로고
    • Cysteine regulation of protein function - as exemplified by NMDA-receptor modulation
    • Lipton S.A., et al. Cysteine regulation of protein function - as exemplified by NMDA-receptor modulation. Trends Neurosci. 2002, 25:474-480.
    • (2002) Trends Neurosci. , vol.25 , pp. 474-480
    • Lipton, S.A.1
  • 14
    • 33846558995 scopus 로고    scopus 로고
    • Regulatory mechanisms of AMPA receptors in synaptic plasticity
    • Derkach V.A., et al. Regulatory mechanisms of AMPA receptors in synaptic plasticity. Nat. Rev. Neurosci. 2007, 8:101-113.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 101-113
    • Derkach, V.A.1
  • 15
    • 0030248099 scopus 로고    scopus 로고
    • LTP of AMPA and NMDA receptor-mediated signals: evidence for presynaptic expression and extrasynaptic glutamate spill-over
    • Kullmann D.M., et al. LTP of AMPA and NMDA receptor-mediated signals: evidence for presynaptic expression and extrasynaptic glutamate spill-over. Neuron 1996, 17:461-474.
    • (1996) Neuron , vol.17 , pp. 461-474
    • Kullmann, D.M.1
  • 16
    • 38149016966 scopus 로고    scopus 로고
    • The cell biology of synaptic plasticity: AMPA receptor trafficking
    • Shepherd J.D., Huganir R.L. The cell biology of synaptic plasticity: AMPA receptor trafficking. Annu. Rev. Cell Dev. Biol. 2007, 23:613-643.
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 613-643
    • Shepherd, J.D.1    Huganir, R.L.2
  • 17
    • 20444388020 scopus 로고    scopus 로고
    • S-nitrosylation of N-ethylmaleimide sensitive factor mediates surface expression of AMPA receptors
    • Huang Y., et al. S-nitrosylation of N-ethylmaleimide sensitive factor mediates surface expression of AMPA receptors. Neuron 2005, 46:533-540.
    • (2005) Neuron , vol.46 , pp. 533-540
    • Huang, Y.1
  • 18
    • 0034700490 scopus 로고    scopus 로고
    • Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms
    • Chen L., et al. Stargazin regulates synaptic targeting of AMPA receptors by two distinct mechanisms. Nature 2000, 408:936-943.
    • (2000) Nature , vol.408 , pp. 936-943
    • Chen, L.1
  • 19
    • 70350725088 scopus 로고    scopus 로고
    • S-nitrosylation of stargazin regulates surface expression of AMPA-glutamate neurotransmitter receptors
    • Selvakumar B., et al. S-nitrosylation of stargazin regulates surface expression of AMPA-glutamate neurotransmitter receptors. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:16440-16445.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 16440-16445
    • Selvakumar, B.1
  • 20
    • 33847253971 scopus 로고    scopus 로고
    • Nitric oxide S-nitrosylates serine racemase, mediating feedback inhibition of D-serine formation
    • Mustafa A.K., et al. Nitric oxide S-nitrosylates serine racemase, mediating feedback inhibition of D-serine formation. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:2950-2955.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 2950-2955
    • Mustafa, A.K.1
  • 21
    • 0032488810 scopus 로고    scopus 로고
    • Dexamethasone rapidly induces a novel ras superfamily member-related gene in AtT-20 cells
    • Kemppainen R.J., Behrend E.N. Dexamethasone rapidly induces a novel ras superfamily member-related gene in AtT-20 cells. J. Biol. Chem. 1998, 273:3129-3131.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3129-3131
    • Kemppainen, R.J.1    Behrend, E.N.2
  • 22
    • 0033634643 scopus 로고    scopus 로고
    • Dexras1: a G protein specifically coupled to neuronal nitric oxide synthase via CAPON
    • Fang M., et al. Dexras1: a G protein specifically coupled to neuronal nitric oxide synthase via CAPON. Neuron 2000, 28:183-193.
    • (2000) Neuron , vol.28 , pp. 183-193
    • Fang, M.1
  • 23
    • 33747047271 scopus 로고    scopus 로고
    • NMDA receptor-nitric oxide transmission mediates neuronal iron homeostasis via the GTPase Dexras1
    • Cheah J.H., et al. NMDA receptor-nitric oxide transmission mediates neuronal iron homeostasis via the GTPase Dexras1. Neuron 2006, 51:431-440.
    • (2006) Neuron , vol.51 , pp. 431-440
    • Cheah, J.H.1
  • 24
    • 3342877609 scopus 로고    scopus 로고
    • Nitric oxide and cerebral ischemic preconditioning
    • Huang P.L., et al. Nitric oxide and cerebral ischemic preconditioning. Cell Calcium 2004, 36:323-329.
    • (2004) Cell Calcium , vol.36 , pp. 323-329
    • Huang, P.L.1
  • 25
    • 22144477159 scopus 로고    scopus 로고
    • S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding
    • Hara M.R., et al. S-nitrosylated GAPDH initiates apoptotic cell death by nuclear translocation following Siah1 binding. Nat. Cell Biol. 2005, 7:665-674.
    • (2005) Nat. Cell Biol. , vol.7 , pp. 665-674
    • Hara, M.R.1
  • 26
    • 68349098976 scopus 로고    scopus 로고
    • GOSPEL: a neuroprotective protein that binds to GAPDH upon S-nitrosylation
    • Sen N., et al. GOSPEL: a neuroprotective protein that binds to GAPDH upon S-nitrosylation. Neuron 2009, 63:81-91.
    • (2009) Neuron , vol.63 , pp. 81-91
    • Sen, N.1
  • 27
    • 33644857006 scopus 로고    scopus 로고
    • Neuroprotection by pharmacologic blockade of the GAPDH death cascade
    • Hara M.R., et al. Neuroprotection by pharmacologic blockade of the GAPDH death cascade. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:3887-3889.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 3887-3889
    • Hara, M.R.1
  • 28
    • 2542534741 scopus 로고    scopus 로고
    • S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function
    • Chung K.K., et al. S-nitrosylation of parkin regulates ubiquitination and compromises parkin's protective function. Science 2004, 304:1328-1331.
    • (2004) Science , vol.304 , pp. 1328-1331
    • Chung, K.K.1
  • 29
    • 3242733689 scopus 로고    scopus 로고
    • Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity
    • Yao D., et al. Nitrosative stress linked to sporadic Parkinson's disease: S-nitrosylation of parkin regulates its E3 ubiquitin ligase activity. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:10810-10814.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 10810-10814
    • Yao, D.1
  • 30
    • 0033555133 scopus 로고    scopus 로고
    • Effect of superoxide dismutase on the stability of S-nitrosothiols
    • Jourd'heuil D., et al. Effect of superoxide dismutase on the stability of S-nitrosothiols. Arch. Biochem. Biophys. 1999, 361:323-330.
    • (1999) Arch. Biochem. Biophys. , vol.361 , pp. 323-330
    • Jourd'heuil, D.1
  • 31
    • 44449119080 scopus 로고    scopus 로고
    • Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins
    • Benhar M., et al. Regulated protein denitrosylation by cytosolic and mitochondrial thioredoxins. Science 2008, 320:1050-1054.
    • (2008) Science , vol.320 , pp. 1050-1054
    • Benhar, M.1
  • 32
    • 33745315287 scopus 로고    scopus 로고
    • S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration
    • Uehara T., et al. S-nitrosylated protein-disulphide isomerase links protein misfolding to neurodegeneration. Nature 2006, 441:513-517.
    • (2006) Nature , vol.441 , pp. 513-517
    • Uehara, T.1
  • 33
    • 64249133725 scopus 로고    scopus 로고
    • S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury
    • Cho D.H., et al. S-nitrosylation of Drp1 mediates beta-amyloid-related mitochondrial fission and neuronal injury. Science 2009, 324:102-105.
    • (2009) Science , vol.324 , pp. 102-105
    • Cho, D.H.1
  • 34
    • 29344465714 scopus 로고    scopus 로고
    • Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2
    • Kim S.F., et al. Inducible nitric oxide synthase binds, S-nitrosylates, and activates cyclooxygenase-2. Science 2005, 310:1966-1970.
    • (2005) Science , vol.310 , pp. 1966-1970
    • Kim, S.F.1
  • 35
    • 48749087958 scopus 로고    scopus 로고
    • S-nitrosylation/activation of COX-2 mediates NMDA neurotoxicity
    • Tian J., et al. S-nitrosylation/activation of COX-2 mediates NMDA neurotoxicity. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:10537-10540.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 10537-10540
    • Tian, J.1
  • 36
    • 11144249792 scopus 로고    scopus 로고
    • Physiological functions for brain NF-kappaB
    • Meffert M.K., Baltimore D. Physiological functions for brain NF-kappaB. Trends Neurosci. 2005, 28:37-43.
    • (2005) Trends Neurosci. , vol.28 , pp. 37-43
    • Meffert, M.K.1    Baltimore, D.2
  • 37
    • 0033570299 scopus 로고    scopus 로고
    • Lack of the p50 subunit of nuclear factor-kappaB increases the vulnerability of hippocampal neurons to excitotoxic injury
    • Yu Z., et al. Lack of the p50 subunit of nuclear factor-kappaB increases the vulnerability of hippocampal neurons to excitotoxic injury. J. Neurosci. 1999, 19:8856-8865.
    • (1999) J. Neurosci. , vol.19 , pp. 8856-8865
    • Yu, Z.1
  • 38
    • 0141653866 scopus 로고    scopus 로고
    • NF-kappa B functions in synaptic signaling and behavior
    • Meffert M.K., et al. NF-kappa B functions in synaptic signaling and behavior. Nat. Neurosci. 2003, 6:1072-1078.
    • (2003) Nat. Neurosci. , vol.6 , pp. 1072-1078
    • Meffert, M.K.1
  • 39
    • 0028981287 scopus 로고
    • Synaptic activation of NF-kappa B by glutamate in cerebellar granule neurons in vitro
    • Guerrini L., et al. Synaptic activation of NF-kappa B by glutamate in cerebellar granule neurons in vitro. Proc. Natl. Acad. Sci. U. S. A. 1995, 92:9077-9081.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 9077-9081
    • Guerrini, L.1
  • 40
    • 2942682649 scopus 로고    scopus 로고
    • S-nitrosylation: physiological regulation of NF-kappaB
    • Marshall H.E., et al. S-nitrosylation: physiological regulation of NF-kappaB. Proc. Natl. Acad. Sci. U. S. A. 2004, 101:8841-8842.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 8841-8842
    • Marshall, H.E.1
  • 41
    • 17644405803 scopus 로고    scopus 로고
    • Physiological roles of hydrogen sulfide: synaptic modulation, neuroprotection, and smooth muscle relaxation
    • Kimura H., et al. Physiological roles of hydrogen sulfide: synaptic modulation, neuroprotection, and smooth muscle relaxation. Antioxid. Redox Signal. 2005, 7:795-803.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 795-803
    • Kimura, H.1
  • 42
    • 43049086657 scopus 로고    scopus 로고
    • Nuclear factor-kappaB1: regulation and function
    • Pereira S.G., Oakley F. Nuclear factor-kappaB1: regulation and function. Int. J. Biochem. Cell Biol. 2008, 40:1425-1430.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 1425-1430
    • Pereira, S.G.1    Oakley, F.2
  • 43
    • 35748959038 scopus 로고    scopus 로고
    • Hydrogen sulphide and its therapeutic potential
    • Szabó C. Hydrogen sulphide and its therapeutic potential. Nat. Rev. Drug Discov. 2007, 6:917-935.
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 917-935
    • Szabó, C.1
  • 44
    • 70349205750 scopus 로고    scopus 로고
    • Hydrogen sulfide: a new EDRF
    • Wang R. Hydrogen sulfide: a new EDRF. Kidney Int. 2009, 76:700-704.
    • (2009) Kidney Int. , vol.76 , pp. 700-704
    • Wang, R.1
  • 45
    • 34047142764 scopus 로고    scopus 로고
    • 2S) - the third gas of interest for pharmacologists
    • 2S) - the third gas of interest for pharmacologists. Pharmacol. Rep. 2007, 59:4-24.
    • (2007) Pharmacol. Rep. , vol.59 , pp. 4-24
    • Łowicka, E.1    Bełtowski, J.2
  • 46
    • 67649289870 scopus 로고    scopus 로고
    • Physiological and pharmacological features of the novel gasotransmitter: hydrogen sulfide
    • Mancardi D., et al. Physiological and pharmacological features of the novel gasotransmitter: hydrogen sulfide. Biochim. Biophys. Acta 2009, 1787:864-872.
    • (2009) Biochim. Biophys. Acta , vol.1787 , pp. 864-872
    • Mancardi, D.1
  • 47
    • 54949084607 scopus 로고    scopus 로고
    • H2S as a physiologic vasorelaxant: hypertension in mice with deletion of cystathionine gamma-lyase
    • Yang G., et al. H2S as a physiologic vasorelaxant: hypertension in mice with deletion of cystathionine gamma-lyase. Science 2008, 322:587-590.
    • (2008) Science , vol.322 , pp. 587-590
    • Yang, G.1
  • 48
    • 0029876402 scopus 로고    scopus 로고
    • The possible role of hydrogen sulfide as an endogenous neuromodulator
    • Abe K., Kimura H. The possible role of hydrogen sulfide as an endogenous neuromodulator. J. Neurosci. 1996, 16:1066-1071.
    • (1996) J. Neurosci. , vol.16 , pp. 1066-1071
    • Abe, K.1    Kimura, H.2
  • 49
    • 17644405803 scopus 로고    scopus 로고
    • Physiological roles of hydrogen sulfide: synaptic modulation, neuroprotection, and smooth muscle relaxation
    • Kimura H., et al. Physiological roles of hydrogen sulfide: synaptic modulation, neuroprotection, and smooth muscle relaxation. Antioxid. Redox Signal. 2005, 7:795-803.
    • (2005) Antioxid. Redox Signal. , vol.7 , pp. 795-803
    • Kimura, H.1
  • 50
    • 2442655642 scopus 로고    scopus 로고
    • Hydrogen sulfide induces calcium waves in astrocytes
    • Nagai Y., et al. Hydrogen sulfide induces calcium waves in astrocytes. FASEB J. 2004, 18:557-559.
    • (2004) FASEB J. , vol.18 , pp. 557-559
    • Nagai, Y.1
  • 51
    • 9444263079 scopus 로고    scopus 로고
    • Hydrogen sulfide protects neurons from oxidative stress
    • Kimura Y., Kimura H. Hydrogen sulfide protects neurons from oxidative stress. FASEB J. 2004, 18:1165-1167.
    • (2004) FASEB J. , vol.18 , pp. 1165-1167
    • Kimura, Y.1    Kimura, H.2
  • 52
    • 0024536043 scopus 로고
    • Monoamine oxidase inhibition as a sequel of hydrogen sulfide intoxication: increases in brain catecholamine and 5-hydroxytryptamine levels
    • Warenycia M.W. Monoamine oxidase inhibition as a sequel of hydrogen sulfide intoxication: increases in brain catecholamine and 5-hydroxytryptamine levels. Arch. Toxicol. 1989, 63:131-136.
    • (1989) Arch. Toxicol. , vol.63 , pp. 131-136
    • Warenycia, M.W.1
  • 53
    • 11144304027 scopus 로고    scopus 로고
    • Hydrogen sulfide may improve the hippocampal damage induced by recurrent febrile seizures in rats
    • Han Y., et al. Hydrogen sulfide may improve the hippocampal damage induced by recurrent febrile seizures in rats. Biochem. Biophys. Res. Commun. 2005, 327:431-436.
    • (2005) Biochem. Biophys. Res. Commun. , vol.327 , pp. 431-436
    • Han, Y.1
  • 54
    • 77953262917 scopus 로고    scopus 로고
    • Neuroprotective effects of hydrogen sulfide on Parkinson's disease rat models
    • Hu L.F., et al. Neuroprotective effects of hydrogen sulfide on Parkinson's disease rat models. Aging Cell 2010, 9:135-146.
    • (2010) Aging Cell , vol.9 , pp. 135-146
    • Hu, L.F.1
  • 55
    • 66449084646 scopus 로고    scopus 로고
    • Signaling by gasotransmitters
    • Mustafa A.K., et al. Signaling by gasotransmitters. Sci. Signal. 2009, 2:re2.
    • (2009) Sci. Signal. , vol.2
    • Mustafa, A.K.1
  • 56
    • 0029898894 scopus 로고    scopus 로고
    • Protein prenylation: molecular mechanisms and functional consequences
    • Zhang F.L., Casey P.J. Protein prenylation: molecular mechanisms and functional consequences. Annu. Rev. Biochem. 1996, 65:241-269.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 241-269
    • Zhang, F.L.1    Casey, P.J.2
  • 57
    • 0028306245 scopus 로고
    • Genetic and biochemical studies of protein N-myristoylation
    • Johnson D.R., et al. Genetic and biochemical studies of protein N-myristoylation. Annu. Rev. Biochem. 1994, 63:869-914.
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 869-914
    • Johnson, D.R.1
  • 58
    • 50549089448 scopus 로고    scopus 로고
    • Molecular form follows function: (un)snaring the SNAREs
    • Parpura V., Mohideen U. Molecular form follows function: (un)snaring the SNAREs. Trends Neurosci. 2008, 31:435-443.
    • (2008) Trends Neurosci. , vol.31 , pp. 435-443
    • Parpura, V.1    Mohideen, U.2
  • 59
    • 0026471991 scopus 로고
    • The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS
    • Hess D.T., et al. The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS. J. Neurosci. 1992, 12:4634-4641.
    • (1992) J. Neurosci. , vol.12 , pp. 4634-4641
    • Hess, D.T.1
  • 60
    • 57749183941 scopus 로고    scopus 로고
    • Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation
    • Kang R., et al. Neural palmitoyl-proteomics reveals dynamic synaptic palmitoylation. Nature 2008, 456:904-909.
    • (2008) Nature , vol.456 , pp. 904-909
    • Kang, R.1
  • 61
    • 0038356721 scopus 로고    scopus 로고
    • Palmitoylation sites and processing of synaptotagmin I, the putative calcium sensor for neurosecretion
    • Heindel U., et al. Palmitoylation sites and processing of synaptotagmin I, the putative calcium sensor for neurosecretion. FEBS Lett. 2003, 544:57-62.
    • (2003) FEBS Lett. , vol.544 , pp. 57-62
    • Heindel, U.1
  • 62
    • 59349119386 scopus 로고    scopus 로고
    • Large-scale profiling of protein palmitoylation in mammalian cells
    • Martin B.R., Cravatt B.F. Large-scale profiling of protein palmitoylation in mammalian cells. Nat. Methods 2009, 6:135-138.
    • (2009) Nat. Methods , vol.6 , pp. 135-138
    • Martin, B.R.1    Cravatt, B.F.2
  • 63
    • 34247590130 scopus 로고    scopus 로고
    • Palmitoylation of ligands, receptors, and intracellular signaling molecules
    • Resh M.D. Palmitoylation of ligands, receptors, and intracellular signaling molecules. Sci. STKE 2006, 2006:re14.
    • (2006) Sci. STKE , vol.2006
    • Resh, M.D.1
  • 64
    • 0027340389 scopus 로고
    • Increased palmitoylation of the Gs protein alpha subunit after activation by the beta-adrenergic receptor or cholera toxin
    • Degtyarev M.Y., et al. Increased palmitoylation of the Gs protein alpha subunit after activation by the beta-adrenergic receptor or cholera toxin. J. Biol. Chem. 1993, 268:23769-23772.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23769-23772
    • Degtyarev, M.Y.1
  • 65
    • 0027522372 scopus 로고
    • Lipid modifications of G proteins: alpha subunits are palmitoylated
    • Linder M.E., et al. Lipid modifications of G proteins: alpha subunits are palmitoylated. Proc. Natl. Acad. Sci. U. S. A. 1993, 90:3675-3679.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 3675-3679
    • Linder, M.E.1
  • 66
    • 0024544232 scopus 로고
    • Palmitoylation of the human beta 2-adrenergic receptor. Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor
    • O'Dowd B.F., et al. Palmitoylation of the human beta 2-adrenergic receptor. Mutation of Cys341 in the carboxyl tail leads to an uncoupled nonpalmitoylated form of the receptor. J. Biol. Chem. 1989, 264:7564-7569.
    • (1989) J. Biol. Chem. , vol.264 , pp. 7564-7569
    • O'Dowd, B.F.1
  • 67
    • 0032747133 scopus 로고    scopus 로고
    • Activation of the beta(2)-adrenergic receptor-Galpha(s) complex leads to rapid depalmitoylation and inhibition of repalmitoylation of both the receptor and Galpha(s)
    • Loisel T.P., et al. Activation of the beta(2)-adrenergic receptor-Galpha(s) complex leads to rapid depalmitoylation and inhibition of repalmitoylation of both the receptor and Galpha(s). J. Biol. Chem. 1999, 274:31014-31019.
    • (1999) J. Biol. Chem. , vol.274 , pp. 31014-31019
    • Loisel, T.P.1
  • 68
    • 70350207200 scopus 로고    scopus 로고
    • Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking
    • Hayashi T., et al. Dual palmitoylation of NR2 subunits regulates NMDA receptor trafficking. Neuron 2009, 64:213-226.
    • (2009) Neuron , vol.64 , pp. 213-226
    • Hayashi, T.1
  • 69
    • 23944433700 scopus 로고    scopus 로고
    • Differential regulation of AMPA receptor subunit trafficking by palmitoylation of two distinct sites
    • Hayashi T., et al. Differential regulation of AMPA receptor subunit trafficking by palmitoylation of two distinct sites. Neuron 2005, 47:709-723.
    • (2005) Neuron , vol.47 , pp. 709-723
    • Hayashi, T.1
  • 70
    • 10444253304 scopus 로고    scopus 로고
    • Identification of PSD-95 palmitoylating enzymes
    • Fukata M. Identification of PSD-95 palmitoylating enzymes. Neuron 2004, 44:987-996.
    • (2004) Neuron , vol.44 , pp. 987-996
    • Fukata, M.1
  • 71
    • 0031932282 scopus 로고    scopus 로고
    • N-terminal palmitoylation of PSD-95 regulates association with cell membranes and interaction with K+ channel Kv1.4
    • Topinka J.R., Bredt D.S. N-terminal palmitoylation of PSD-95 regulates association with cell membranes and interaction with K+ channel Kv1.4. Neuron 1998, 20:125-134.
    • (1998) Neuron , vol.20 , pp. 125-134
    • Topinka, J.R.1    Bredt, D.S.2
  • 72
    • 18344396972 scopus 로고    scopus 로고
    • Synaptic strength regulated by palmitate cycling on PSD-95
    • El-Husseini A., et al. Synaptic strength regulated by palmitate cycling on PSD-95. Cell 2002, 108:849-863.
    • (2002) Cell , vol.108 , pp. 849-863
    • El-Husseini, A.1
  • 73
    • 9644302439 scopus 로고    scopus 로고
    • Presynaptic trafficking of synaptotagmin I is regulated by protein palmitoylation
    • Kang R., et al. Presynaptic trafficking of synaptotagmin I is regulated by protein palmitoylation. J. Biol. Chem. 2004, 279:50524-50536.
    • (2004) J. Biol. Chem. , vol.279 , pp. 50524-50536
    • Kang, R.1
  • 74
    • 67650475440 scopus 로고    scopus 로고
    • Mobile DHHC palmitoylating enzyme mediates activity-sensitive synaptic targeting of PSD-95
    • Noritake J., et al. Mobile DHHC palmitoylating enzyme mediates activity-sensitive synaptic targeting of PSD-95. J. Cell Biol. 2009, 186:147-160.
    • (2009) J. Cell Biol. , vol.186 , pp. 147-160
    • Noritake, J.1
  • 75
    • 77249134163 scopus 로고    scopus 로고
    • Protein palmitoylation in neuronal development and synaptic plasticity
    • Fukata Y., Fukata M. Protein palmitoylation in neuronal development and synaptic plasticity. Nat. Rev. Neurosci. 2010, 11:161-175.
    • (2010) Nat. Rev. Neurosci. , vol.11 , pp. 161-175
    • Fukata, Y.1    Fukata, M.2
  • 76
    • 33845451067 scopus 로고    scopus 로고
    • GODZ-mediated palmitoylation of GABA(A) receptors is required for normal assembly and function of GABAergic inhibitory synapses
    • Fang C., et al. GODZ-mediated palmitoylation of GABA(A) receptors is required for normal assembly and function of GABAergic inhibitory synapses. J. Neurosci. 2006, 26:12758-12768.
    • (2006) J. Neurosci. , vol.26 , pp. 12758-12768
    • Fang, C.1
  • 77
    • 0037213362 scopus 로고    scopus 로고
    • The on-off story of protein palmitoylation
    • Biljmakers M.J., Marsh M. The on-off story of protein palmitoylation. Trends Cell Biol. 2003, 13:32-42.
    • (2003) Trends Cell Biol. , vol.13 , pp. 32-42
    • Biljmakers, M.J.1    Marsh, M.2
  • 78
    • 33748895740 scopus 로고    scopus 로고
    • Neurocognitive profile in 22q11 deletion syndrome and schizophrenia
    • Chow E.W., et al. Neurocognitive profile in 22q11 deletion syndrome and schizophrenia. Schizophr. Res. 2006, 87:270-278.
    • (2006) Schizophr. Res. , vol.87 , pp. 270-278
    • Chow, E.W.1
  • 79
    • 0027989917 scopus 로고
    • Psychotic illness in patients diagnosed with velo-cardio-facial syndrome and their relatives
    • Pulver A.E., et al. Psychotic illness in patients diagnosed with velo-cardio-facial syndrome and their relatives. J. Nerv. Ment. Dis. 1994, 182:476-478.
    • (1994) J. Nerv. Ment. Dis. , vol.182 , pp. 476-478
    • Pulver, A.E.1
  • 80
    • 0033358588 scopus 로고    scopus 로고
    • Low-copy repeats mediate the common 3-Mb deletion in patients with velo-cardio-facial syndrome
    • Edelmann L., et al. Low-copy repeats mediate the common 3-Mb deletion in patients with velo-cardio-facial syndrome. Am. J. Hum. Genet. 1999, 64:1076-1086.
    • (1999) Am. J. Hum. Genet. , vol.64 , pp. 1076-1086
    • Edelmann, L.1
  • 81
    • 54949150182 scopus 로고    scopus 로고
    • Palmitoylation-dependent neurodevelopmental deficits in a mouse model of 22q11 microdeletion
    • Mukai J., et al. Palmitoylation-dependent neurodevelopmental deficits in a mouse model of 22q11 microdeletion. Nat. Neurosci. 2008, 11:1302-1310.
    • (2008) Nat. Neurosci. , vol.11 , pp. 1302-1310
    • Mukai, J.1
  • 82
    • 68849113445 scopus 로고    scopus 로고
    • Neuronal palmitoyl acyl transferases exhibit distinct substrate specificity
    • Huang K., et al. Neuronal palmitoyl acyl transferases exhibit distinct substrate specificity. FASEB J. 2009, 23:2605-2615.
    • (2009) FASEB J. , vol.23 , pp. 2605-2615
    • Huang, K.1
  • 83
    • 33745627659 scopus 로고    scopus 로고
    • Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function
    • Yanai A., et al. Palmitoylation of huntingtin by HIP14 is essential for its trafficking and function. Nat. Neurosci. 2006, 9:824-831.
    • (2006) Nat. Neurosci. , vol.9 , pp. 824-831
    • Yanai, A.1
  • 84
    • 0032403433 scopus 로고    scopus 로고
    • Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin
    • Halpain S., et al. Regulation of F-actin stability in dendritic spines by glutamate receptors and calcineurin. J. Neurosci. 1998, 18:9835-9844.
    • (1998) J. Neurosci. , vol.18 , pp. 9835-9844
    • Halpain, S.1
  • 85
    • 34250214907 scopus 로고    scopus 로고
    • SUMOrganization of the nucleus
    • Heun P. SUMOrganization of the nucleus. Curr. Opin. Cell Biol. 2007, 19:350-355.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 350-355
    • Heun, P.1
  • 87
    • 38549181148 scopus 로고    scopus 로고
    • Sumoylation regulates diverse biological processes
    • Zhao J. Sumoylation regulates diverse biological processes. Cell. Mol. Life Sci. 2007, 64:3017-3033.
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 3017-3033
    • Zhao, J.1
  • 88
    • 34249880519 scopus 로고    scopus 로고
    • Modification in reverse: the SUMO proteases
    • Mukhopadhyay D., Dasso M. Modification in reverse: the SUMO proteases. Trends Biochem. Sci. 2007, 32:286-295.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 286-295
    • Mukhopadhyay, D.1    Dasso, M.2
  • 89
    • 0034789730 scopus 로고    scopus 로고
    • Involvement of PIAS1 in the sumoylation of tumor suppressor p53
    • Kahyo T., et al. Involvement of PIAS1 in the sumoylation of tumor suppressor p53. Mol. Cell 2001, 8:713-718.
    • (2001) Mol. Cell , vol.8 , pp. 713-718
    • Kahyo, T.1
  • 90
    • 0037059619 scopus 로고    scopus 로고
    • The nucleoporin RanBP2 has SUMO1 E3 ligase activity
    • Pichler A., et al. The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 2002, 108:109-120.
    • (2002) Cell , vol.108 , pp. 109-120
    • Pichler, A.1
  • 91
    • 0037418829 scopus 로고    scopus 로고
    • The polycomb protein Pc2 is a SUMO E3
    • Kagey M.H., et al. The polycomb protein Pc2 is a SUMO E3. Cell 2003, 113:127-137.
    • (2003) Cell , vol.113 , pp. 127-137
    • Kagey, M.H.1
  • 92
    • 36349022018 scopus 로고    scopus 로고
    • Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction
    • Martin S., et al. Emerging extranuclear roles of protein SUMOylation in neuronal function and dysfunction. Nat. Rev. Neurosci. 2007, 8:948-959.
    • (2007) Nat. Rev. Neurosci. , vol.8 , pp. 948-959
    • Martin, S.1
  • 93
    • 33144462154 scopus 로고    scopus 로고
    • Brawn for brains: the role of MEF2 proteins in the developing nervous system
    • Shalizi A.K., Bonni A. brawn for brains: the role of MEF2 proteins in the developing nervous system. Curr. Top. Dev. Biol. 2005, 69:239-266.
    • (2005) Curr. Top. Dev. Biol. , vol.69 , pp. 239-266
    • Shalizi, A.K.1    Bonni, A.2
  • 94
    • 33144473786 scopus 로고    scopus 로고
    • A calcium-regulated MEF2 sumoylation switch controls postsynaptic differentiation
    • Shalizi A., et al. A calcium-regulated MEF2 sumoylation switch controls postsynaptic differentiation. Science 2006, 311:1012-1017.
    • (2006) Science , vol.311 , pp. 1012-1017
    • Shalizi, A.1
  • 95
    • 33645801010 scopus 로고    scopus 로고
    • Wrestling with SUMO in a new arena
    • Wilson V.G., Rosas-Acosta G. Wrestling with SUMO in a new arena. Sci. STKE 2005, 2005:pe32.
    • (2005) Sci. STKE , vol.2005
    • Wilson, V.G.1    Rosas-Acosta, G.2
  • 96
    • 20444381721 scopus 로고    scopus 로고
    • K2P channels and their protein partners
    • Plant L.D., et al. K2P channels and their protein partners. Curr. Opin. Neurobiol. 2005, 15:326-333.
    • (2005) Curr. Opin. Neurobiol. , vol.15 , pp. 326-333
    • Plant, L.D.1
  • 97
    • 33751440647 scopus 로고    scopus 로고
    • The potassium channels Kv1.5 and Kv1.3 modulate distinct functions of microglia
    • Pannasch U., et al. The potassium channels Kv1.5 and Kv1.3 modulate distinct functions of microglia. Mol. Cell. Neurosci. 2006, 33:401-411.
    • (2006) Mol. Cell. Neurosci. , vol.33 , pp. 401-411
    • Pannasch, U.1
  • 98
    • 33846914818 scopus 로고    scopus 로고
    • SUMO modification regulates inactivation of the voltage-gated potassium channel Kv1.5
    • Benson M.D., et al. SUMO modification regulates inactivation of the voltage-gated potassium channel Kv1.5. Proc. Natl. Acad. Sci. U. S. A. 2007, 104:1805-1810.
    • (2007) Proc. Natl. Acad. Sci. U. S. A. , vol.104 , pp. 1805-1810
    • Benson, M.D.1
  • 99
    • 34249046463 scopus 로고    scopus 로고
    • SUMOylation regulates kainate-receptor-mediated synaptic transmission
    • Martin S., et al. SUMOylation regulates kainate-receptor-mediated synaptic transmission. Nature 2007, 447:321-325.
    • (2007) Nature , vol.447 , pp. 321-325
    • Martin, S.1
  • 100
    • 57649198470 scopus 로고    scopus 로고
    • Complexity and heterogeneity: what drives the ever-changing brain in Huntington's disease?
    • Rosas H.D., et al. Complexity and heterogeneity: what drives the ever-changing brain in Huntington's disease?. Ann. N. Y. Acad. Sci. 2008, 1147:196-205.
    • (2008) Ann. N. Y. Acad. Sci. , vol.1147 , pp. 196-205
    • Rosas, H.D.1
  • 101
    • 11144353613 scopus 로고    scopus 로고
    • SUMO modification of Huntingtin and Huntington's disease pathology
    • Steffan J.S., et al. SUMO modification of Huntingtin and Huntington's disease pathology. Science 2004, 304:100-104.
    • (2004) Science , vol.304 , pp. 100-104
    • Steffan, J.S.1
  • 102
    • 66749167799 scopus 로고    scopus 로고
    • Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity
    • Subramaniam S., et al. Rhes, a striatal specific protein, mediates mutant-huntingtin cytotoxicity. Science 2009, 324:1327-1330.
    • (2009) Science , vol.324 , pp. 1327-1330
    • Subramaniam, S.1
  • 103
    • 77954240133 scopus 로고    scopus 로고
    • Rhes, a physiologic regulator of sumoylation, enhances cross-sumoylation between e1 and ubc9
    • Subramaniam S., et al. Rhes, a physiologic regulator of sumoylation, enhances cross-sumoylation between e1 and ubc9. J. Biol. Chem. 2010, 285:20428-20432.
    • (2010) J. Biol. Chem. , vol.285 , pp. 20428-20432
    • Subramaniam, S.1
  • 104
    • 71549143207 scopus 로고    scopus 로고
    • Balance between synaptic versus extrasynaptic NMDA receptor activity influences inclusions and neurotoxicity of mutant huntingtin
    • Okamoto S., et al. Balance between synaptic versus extrasynaptic NMDA receptor activity influences inclusions and neurotoxicity of mutant huntingtin. Nat. Med. 2009, 15:1407-1413.
    • (2009) Nat. Med. , vol.15 , pp. 1407-1413
    • Okamoto, S.1
  • 105
    • 20444467297 scopus 로고    scopus 로고
    • SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal
    • Riley B.E., et al. SUMOylation of the polyglutamine repeat protein, ataxin-1, is dependent on a functional nuclear localization signal. J. Biol. Chem. 2005, 280:21942-21948.
    • (2005) J. Biol. Chem. , vol.280 , pp. 21942-21948
    • Riley, B.E.1
  • 106
    • 0034094873 scopus 로고    scopus 로고
    • Glutamine repeats and neurodegeneration
    • Zoghbi H.Y., Orr H.T. Glutamine repeats and neurodegeneration. Annu. Rev. Neurosci. 2000, 23:217-247.
    • (2000) Annu. Rev. Neurosci. , vol.23 , pp. 217-247
    • Zoghbi, H.Y.1    Orr, H.T.2
  • 107
    • 33744544785 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) modification of natively unfolded proteins tau and alpha-synuclein
    • Dorval V., Fraser P.E. Small ubiquitin-like modifier (SUMO) modification of natively unfolded proteins tau and alpha-synuclein. J. Biol. Chem. 2006, 281:9919-9924.
    • (2006) J. Biol. Chem. , vol.281 , pp. 9919-9924
    • Dorval, V.1    Fraser, P.E.2
  • 108
    • 33750604073 scopus 로고    scopus 로고
    • Functional modulation of parkin through physical interaction with SUMO-1
    • Um J.W., Chung K.C. Functional modulation of parkin through physical interaction with SUMO-1. J. Neurosci. Res. 2006, 84:1543-1554.
    • (2006) J. Neurosci. Res. , vol.84 , pp. 1543-1554
    • Um, J.W.1    Chung, K.C.2
  • 109
    • 33645640622 scopus 로고    scopus 로고
    • Parkin ubiquitinates and promotes the degradation of RanBP2
    • Um J.W., et al. Parkin ubiquitinates and promotes the degradation of RanBP2. J. Biol. Chem. 2006, 281:3595-3603.
    • (2006) J. Biol. Chem. , vol.281 , pp. 3595-3603
    • Um, J.W.1
  • 110
    • 33644543761 scopus 로고    scopus 로고
    • Expanding insights of mitochondrial dysfunction in Parkinson's disease
    • Abou-Sleiman P.M., et al. Expanding insights of mitochondrial dysfunction in Parkinson's disease. Nat. Rev. Neurosci. 2006, 7:207-219.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 207-219
    • Abou-Sleiman, P.M.1
  • 111
    • 33645002036 scopus 로고    scopus 로고
    • Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities
    • Shinbo Y., et al. Proper SUMO-1 conjugation is essential to DJ-1 to exert its full activities. Cell Death Differ. 2006, 13:96-108.
    • (2006) Cell Death Differ. , vol.13 , pp. 96-108
    • Shinbo, Y.1
  • 112
    • 70349085803 scopus 로고    scopus 로고
    • Antidepressant actions of histone deacetylase inhibitors
    • 3rdet al.
    • Covington H.E., 3rd, et al. Antidepressant actions of histone deacetylase inhibitors. J. Neurosci. 2009, 29:11451-11460.
    • (2009) J. Neurosci. , vol.29 , pp. 11451-11460
    • Covington, H.E.1
  • 113
    • 33748928786 scopus 로고    scopus 로고
    • Histone deacetylase inhibitors as therapeutics for polyglutamine disorders
    • Butler R., Bates G.P. Histone deacetylase inhibitors as therapeutics for polyglutamine disorders. Nat. Rev. Neurosci. 2006, 7:784-796.
    • (2006) Nat. Rev. Neurosci. , vol.7 , pp. 784-796
    • Butler, R.1    Bates, G.P.2
  • 114
    • 58149389397 scopus 로고    scopus 로고
    • HDAC4 regulates neuronal survival in normal and diseased retinas
    • Chen B., Cepko C.L. HDAC4 regulates neuronal survival in normal and diseased retinas. Science 2009, 323:256-259.
    • (2009) Science , vol.323 , pp. 256-259
    • Chen, B.1    Cepko, C.L.2
  • 115
    • 0034927081 scopus 로고    scopus 로고
    • Neurotrophins: roles in neuronal development and function
    • Huang E., Reichardt L. Neurotrophins: roles in neuronal development and function. Annu. Rev. Neurosci. 2001, 24:677-736.
    • (2001) Annu. Rev. Neurosci. , vol.24 , pp. 677-736
    • Huang, E.1    Reichardt, L.2
  • 116
    • 52149108919 scopus 로고    scopus 로고
    • S-Nitrosylation of histone deacetylase 2 induces chromatin remodelling in neurons
    • Nott A., et al. S-Nitrosylation of histone deacetylase 2 induces chromatin remodelling in neurons. Nature 2008, 455:411-415.
    • (2008) Nature , vol.455 , pp. 411-415
    • Nott, A.1
  • 117
    • 68949212379 scopus 로고    scopus 로고
    • Lysine acetylation targets protein complexes and co-regulates major cellular functions
    • Choudhary C., et al. Lysine acetylation targets protein complexes and co-regulates major cellular functions. Science 2009, 325:834-840.
    • (2009) Science , vol.325 , pp. 834-840
    • Choudhary, C.1
  • 118
    • 46649101876 scopus 로고    scopus 로고
    • Nitric oxide-induced nuclear GAPDH activates p300/CBP and mediates apoptosis
    • Sen N., et al. Nitric oxide-induced nuclear GAPDH activates p300/CBP and mediates apoptosis. Nat. Cell Biol. 2008, 10:866-873.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 866-873
    • Sen, N.1
  • 119
    • 63049132756 scopus 로고    scopus 로고
    • Acetylation targets mutant huntingtin to autophagosomes for degradation
    • Jeong H., et al. Acetylation targets mutant huntingtin to autophagosomes for degradation. Cell 2009, 137:60-72.
    • (2009) Cell , vol.137 , pp. 60-72
    • Jeong, H.1
  • 120
    • 0037160106 scopus 로고    scopus 로고
    • Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities
    • Li F., et al. Ataxin-3 is a histone-binding protein with two independent transcriptional corepressor activities. J. Biol. Chem. 2002, 277:45004-45012.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45004-45012
    • Li, F.1


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