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Volumn 7, Issue JAN, 2015, Pages 1-20

Neuroinflammation and J2 prostaglandins: Linking impairment of the ubiquitin-proteasome pathway and mitochondria to neurodegeneration

Author keywords

J2 prostaglandins; Mitochondria; Neurodegeneration; Neuroinflammation; UPP

Indexed keywords

15 HYDROXYPROSTAGLANDIN DEHYDROGENASE; ADENOSINE TRIPHOSPHATE; ALPHA SYNUCLEIN; ARACHIDONIC ACID; CALCIUM; CELL NUCLEUS RECEPTOR; CYCLIC AMP; CYCLOOXYGENASE 1; CYCLOOXYGENASE 2; DYNAMIN RELATED PROTEIN 1; G PROTEIN COUPLED RECEPTOR; INDUCIBLE NITRIC OXIDE SYNTHASE; INTERLEUKIN 1BETA; INTERLEUKIN 8; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; MULTIDRUG RESISTANCE PROTEIN; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA; PHOSPHOLIPASE A2; PHOSPHOLIPASE D2; PROSTAGLANDIN J2; PROSTAGLANDIN TRANSPORTER; PROSTANOID; PROTEASOME; RAS PROTEIN; REACTIVE OXYGEN METABOLITE; TUMOR NECROSIS FACTOR ALPHA; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; UNINDEXED DRUG;

EID: 84920983279     PISSN: 16625099     EISSN: None     Source Type: Journal    
DOI: 10.3389/fnmol.2014.00104     Document Type: Review
Times cited : (89)

References (237)
  • 1
    • 0017625640 scopus 로고
    • Identification of prostaglandin D2 as a major prostaglandin in homogenates of rat brain
    • Abdel-Halim, M. S., Hamberg, M., Sjoquist, B., and Anggard, E. (1977). Identification of prostaglandin D2 as a major prostaglandin in homogenates of rat brain. Prostaglandins 14, 633-643. doi: 10.1016/0090-6980(77)90190-3
    • (1977) Prostaglandins , vol.14 , pp. 633-643
    • Abdel-Halim, M.S.1    Hamberg, M.2    Sjoquist, B.3    Anggard, E.4
  • 2
    • 77956183759 scopus 로고    scopus 로고
    • Prostaglandin D2 DP1 receptor is beneficial in ischemic stroke and in acute exicitotoxicity in young and old mice
    • Ahmad, A. S., Ahmad, M., Maruyama, T., Narumiya, S., and Dore, S. (2010). Prostaglandin D2 DP1 receptor is beneficial in ischemic stroke and in acute exicitotoxicity in young and old mice. Age (Dordr.) 32, 271-282. doi: 10.1007/s11357-010-9135-y
    • (2010) Age (Dordr.) , vol.32 , pp. 271-282
    • Ahmad, A.S.1    Ahmad, M.2    Maruyama, T.3    Narumiya, S.4    Dore, S.5
  • 3
    • 78650510200 scopus 로고    scopus 로고
    • Targeting cyclooxygenases-1 and -2 in neuroinflammation: Therapeutic implications
    • Aid, S., and Bosetti, F. (2011). Targeting cyclooxygenases-1 and -2 in neuroinflammation: therapeutic implications.Biochimie 93, 46-51. doi: 10.1016/j.biochi.2010.09.009
    • (2011) Biochimie , vol.93 , pp. 46-51
    • Aid, S.1    Bosetti, F.2
  • 4
    • 79955757695 scopus 로고    scopus 로고
    • Oxidative stress-mediated regulation of proteasome complexes
    • Aiken, C. T., Kaake, R. M., Wang, X., and Huang, L. (2011). Oxidative stress-mediated regulation of proteasome complexes. Mol. Cell Proteomics 10, R110. doi: 10.1074/mcp.M110.006924
    • (2011) Mol. Cell Proteomics , vol.10 , pp. R110
    • Aiken, C.T.1    Kaake, R.M.2    Wang, X.3    Huang, L.4
  • 5
    • 84861875788 scopus 로고    scopus 로고
    • Prostaglandins and chronic inflammation
    • Aoki, T., and Narumiya, S. (2012). Prostaglandins and chronic inflammation. Trends Pharmacol. Sci. 33, 304-311. doi: 10.1016/j.tips.2012.02.004
    • (2012) Trends Pharmacol. Sci , vol.33 , pp. 304-311
    • Aoki, T.1    Narumiya, S.2
  • 6
    • 0037083896 scopus 로고    scopus 로고
    • Cross-talk unfolded: MARCKS proteins
    • Arbuzova, A., Schmitz, A. A., and Vergeres, G. (2002). Cross-talk unfolded: MARCKS proteins. Biochem. J. 362, 1-12. doi: 10.1042/0264-6021:3620001
    • (2002) Biochem. J , vol.362 , pp. 1-12
    • Arbuzova, A.1    Schmitz, A.A.2    Vergeres, G.3
  • 7
    • 67449127077 scopus 로고    scopus 로고
    • Proteasome-caspase-cathepsin sequence leading to tau pathology induced by prostaglandin J2 in neuronal cells
    • Arnaud, L. T., Myeku, N., and Figueiredo-Pereira, M. E. (2009). Proteasome-caspase-cathepsin sequence leading to tau pathology induced by prostaglandin J2 in neuronal cells. J. Neurochem. 110, 328-342. doi: 10.1111/j.1471-4159.2009.06142.x
    • (2009) J. Neurochem , vol.110 , pp. 328-342
    • Arnaud, L.T.1    Myeku, N.2    Figueiredo-Pereira, M.E.3
  • 8
    • 83455203613 scopus 로고    scopus 로고
    • Dynamics of arachidonic acid mobilization by inflammatory cells
    • Astudillo, A. M., Balgoma, D., Balboa, M. A., and Balsinde, J. (2012). Dynamics of arachidonic acid mobilization by inflammatory cells. Biochim. Biophys. Acta 1821, 249-256. doi: 10.1016/j.bbalip.2011.11.006
    • (2012) Biochim. Biophys. Acta , vol.1821 , pp. 249-256
    • Astudillo, A.M.1    Balgoma, D.2    Balboa, M.A.3    Balsinde, J.4
  • 9
    • 74449086851 scopus 로고    scopus 로고
    • Evaluation of the protective effects of PACAP with cell-specific markers in ischemia-induced retinal degeneration
    • Atlasz, T., Szabadfi, K., Kiss, P., Tamas, A., Toth, G., Reglodi, D., et al. (2010). Evaluation of the protective effects of PACAP with cell-specific markers in ischemia-induced retinal degeneration. Brain Res. Bull. 81, 497-504. doi: 10.1016/j.brainresbull.2009.09.004
    • (2010) Brain Res. Bull , vol.81 , pp. 497-504
    • Atlasz, T.1    Szabadfi, K.2    Kiss, P.3    Tamas, A.4    Toth, G.5    Reglodi, D.6
  • 10
    • 0036850086 scopus 로고    scopus 로고
    • Visualising microglial activation in vivo
    • Banati, R. B. (2002). Visualising microglial activation in vivo. Glia 40, 206-217. doi: 10.1002/glia.10144
    • (2002) Glia , vol.40 , pp. 206-217
    • Banati, R.B.1
  • 11
    • 0141482019 scopus 로고    scopus 로고
    • Molecular cloning and spatio-temporal expression of the prostaglandin transporter: A basis for the action of prostaglandins in the bovine reproductive system
    • Banu, S. K., Arosh, J. A., Chapdelaine, P., and Fortier, M. A. (2003). Molecular cloning and spatio-temporal expression of the prostaglandin transporter: a basis for the action of prostaglandins in the bovine reproductive system. Proc. Natl. Acad. Sci. U.S.A. 100, 11747-11752. doi: 10.1073/pnas.1833330100
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 11747-11752
    • Banu, S.K.1    Arosh, J.A.2    Chapdelaine, P.3    Fortier, M.A.4
  • 12
    • 77950249229 scopus 로고    scopus 로고
    • Cyclooxygenase and neuroinflammation in Parkinson's disease neurodegeneration
    • Bartels, A. L., and Leenders, K. L. (2010). Cyclooxygenase and neuroinflammation in Parkinson's disease neurodegeneration. Curr. Neuropharmacol. 8, 62-68. doi: 10.2174/157015910790909485
    • (2010) Curr. Neuropharmacol , vol.8 , pp. 62-68
    • Bartels, A.L.1    Leenders, K.L.2
  • 13
    • 74149090924 scopus 로고    scopus 로고
    • Risk of stroke in patients with idiopathic Parkinson disease
    • Becker, C., Jick, S. S., and Meier, C. R. (2010). Risk of stroke in patients with idiopathic Parkinson disease.Parkinsonism. Relat. Disord. 16, 31-35. doi: 10.1016/j.parkreldis.2009.06.005
    • (2010) Parkinsonism. Relat. Disord , vol.16 , pp. 31-35
    • Becker, C.1    Jick, S.S.2    Meier, C.R.3
  • 14
    • 84866426167 scopus 로고    scopus 로고
    • Exosomes: Vehicles for the transfer of toxic proteins associated with neurodegenerative diseases?
    • Bellingham, S. A., Guo, B. B., Coleman, B. M., and Hill, A. F. (2012). Exosomes: vehicles for the transfer of toxic proteins associated with neurodegenerative diseases? Front. Physiol. 3:124. doi: 10.3389/fphys.2012.00124
    • (2012) Front. Physiol , vol.3 , pp. 124
    • Bellingham, S.A.1    Guo, B.B.2    Coleman, B.M.3    Hill, A.F.4
  • 15
    • 0142210300 scopus 로고    scopus 로고
    • 15-Deoxy-delta12,14-prostaglandin J2 regulates the functional state and the survival of microglial cells through multiple molecular mechanisms
    • Bernardo, A., Ajmone-Cat, M. A., Levi, G., and Minghetti, L. (2003). 15-Deoxy-delta12,14-prostaglandin J2 regulates the functional state and the survival of microglial cells through multiple molecular mechanisms. J. Neurochem. 87, 742-751. doi: 10.1046/j.1471-4159.2003.02045.x
    • (2003) J. Neurochem , vol.87 , pp. 742-751
    • Bernardo, A.1    Ajmone-Cat, M.A.2    Levi, G.3    Minghetti, L.4
  • 17
    • 84861569658 scopus 로고    scopus 로고
    • Inhibition of 26S protease regulatory subunit 7 (MSS1) suppresses neuroinflammation
    • Bi, W., Jing, X., Zhu, L., Liang, Y., Liu, J., Yang, L., et al. (2012). Inhibition of 26S protease regulatory subunit 7 (MSS1) suppresses neuroinflammation. PLoS ONE 7:e36142. doi: 10.1371/journal.pone.0036142
    • (2012) PLoS ONE , vol.7
    • Bi, W.1    Jing, X.2    Zhu, L.3    Liang, Y.4    Liu, J.5    Yang, L.6
  • 18
    • 84906936127 scopus 로고    scopus 로고
    • Investigations into the role of 26S proteasome non-ATPase regulatory subunit 13 in neuroinflammation
    • Bi, W., Zhu, L., Zeng, Z., Jing, X., Liang, Y., Guo, L., et al. (2014). Investigations into the role of 26S proteasome non-ATPase regulatory subunit 13 in neuroinflammation. Neuroimmunomodulation 21, 331-337. doi: 10.1159/000357811
    • (2014) Neuroimmunomodulation , vol.21 , pp. 331-337
    • Bi, W.1    Zhu, L.2    Zeng, Z.3    Jing, X.4    Liang, Y.5    Guo, L.6
  • 19
    • 84903179483 scopus 로고    scopus 로고
    • The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy
    • Bingol, B., Tea, J. S., Phu, L., Reichelt, M., Bakalarski, C. E., Song, Q., et al. (2014). The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy. Nature 510, 370-375. doi: 10.1038/nature13418
    • (2014) Nature , vol.510 , pp. 370-375
    • Bingol, B.1    Tea, J.S.2    Phu, L.3    Reichelt, M.4    Bakalarski, C.E.5    Song, Q.6
  • 20
    • 20444363048 scopus 로고    scopus 로고
    • Increased plasma levels of 15-deoxyDelta prostaglandin J2 are associated with good outcome in acute atherothrombotic ischemic stroke
    • Blanco, M., Moro, M. A., Davalos, A., Leira, R., Castellanos, M., Serena, J., et al. (2005). Increased plasma levels of 15-deoxyDelta prostaglandin J2 are associated with good outcome in acute atherothrombotic ischemic stroke.Stroke 36, 1189-1194. doi: 10.1161/01.STR.0000166054.55993.e5
    • (2005) Stroke , vol.36 , pp. 1189-1194
    • Blanco, M.1    Moro, M.A.2    Davalos, A.3    Leira, R.4    Castellanos, M.5    Serena, J.6
  • 21
    • 34250624816 scopus 로고    scopus 로고
    • Arachidonic acid metabolism in brain physiology and pathology: Lessons from genetically altered mouse models
    • Bosetti, F. (2007). Arachidonic acid metabolism in brain physiology and pathology: lessons from genetically altered mouse models. J. Neurochem. 102, 577-586. doi: 10.1111/j.1471-4159.2007.04558.x
    • (2007) J. Neurochem , vol.102 , pp. 577-586
    • Bosetti, F.1
  • 22
    • 25644436461 scopus 로고    scopus 로고
    • Essential role for the PKC target MARCKS in maintaining dendritic spine morphology
    • Calabrese, B., and Halpain, S. (2005). Essential role for the PKC target MARCKS in maintaining dendritic spine morphology. Neuron 48, 77-90. doi: 10.1016/j.neuron.2005.08.027
    • (2005) Neuron , vol.48 , pp. 77-90
    • Calabrese, B.1    Halpain, S.2
  • 23
    • 84890805926 scopus 로고    scopus 로고
    • Role of the ubiquitin-proteasome system in brain ischemia: Friend or foe?
    • Caldeira, M. V., Salazar, I. L., Curcio, M., Canzoniero, L. M., and Duarte, C. B. (2014). Role of the ubiquitin-proteasome system in brain ischemia: friend or foe? Prog. Neurobiol. 112, 50-69. doi: 10.1016/j.pneurobio.2013.10.003
    • (2014) Prog. Neurobiol , vol.112 , pp. 50-69
    • Caldeira, M.V.1    Salazar, I.L.2    Curcio, M.3    Canzoniero, L.M.4    Duarte, C.B.5
  • 24
    • 20444362984 scopus 로고    scopus 로고
    • Fatty acid incorporation is decreased in astrocytes cultured from alpha-synuclein gene-ablated mice
    • Castagnet, P. I., Golovko, M. Y., Barcelo-Coblijn, G. C., Nussbaum, R. L., and Murphy, E. J. (2005). Fatty acid incorporation is decreased in astrocytes cultured from alpha-synuclein gene-ablated mice. J. Neurochem. 94, 839-849. doi: 10.1111/j.1471-4159.2005.03247.x
    • (2005) J. Neurochem , vol.94 , pp. 839-849
    • Castagnet, P.I.1    Golovko, M.Y.2    Barcelo-Coblijn, G.C.3    Nussbaum, R.L.4    Murphy, E.J.5
  • 25
    • 10744223324 scopus 로고    scopus 로고
    • Mechanisms of signal transduction mediated by oxidized lipids: The role of the electrophile-responsive proteome
    • Ceaser, E. K., Moellering, D. R., Shiva, S., Ramachandran, A., Landar, A., Venkartraman, A., et al. (2004). Mechanisms of signal transduction mediated by oxidized lipids: the role of the electrophile-responsive proteome.Biochem. Soc. Trans. 32, 151-155. doi: 10.1042/BST0320151
    • (2004) Biochem. Soc. Trans , vol.32 , pp. 151-155
    • Ceaser, E.K.1    Moellering, D.R.2    Shiva, S.3    Ramachandran, A.4    Landar, A.5    Venkartraman, A.6
  • 26
    • 0035929592 scopus 로고    scopus 로고
    • 15-Deoxy-Delta 12,14-prostaglandin J2 inhibition of NF-kappaB-DNA binding through covalent modification of the p50 subunit
    • Cernuda-Morollon, E., Pineda-Molina, E., Canada, F. J., and Perez-Sala, D. (2001). 15-Deoxy-Delta 12,14-prostaglandin J2 inhibition of NF-kappaB-DNA binding through covalent modification of the p50 subunit. J. Biol. Chem. 276, 35530-35536. doi: 10.1074/jbc.M104518200
    • (2001) J. Biol. Chem , vol.276 , pp. 35530-35536
    • Cernuda-Morollon, E.1    Pineda-Molina, E.2    Canada, F.J.3    Perez-Sala, D.4
  • 27
    • 0036080578 scopus 로고    scopus 로고
    • Identification of lactate as a driving force for prostanoid transport by prostaglandin transporter PGT
    • Chan, B. S., Endo, S., Kanai, N., and Schuster, V. L. (2002). Identification of lactate as a driving force for prostanoid transport by prostaglandin transporter PGT. Am. J. Physiol. Renal. Physiol. 282, F1097-F1102. doi: 10.1152/ajprenal.00151.2001
    • (2002) Am. J. Physiol. Renal. Physiol , vol.282 , pp. F1097-F1102
    • Chan, B.S.1    Endo, S.2    Kanai, N.3    Schuster, V.L.4
  • 28
    • 84885430485 scopus 로고    scopus 로고
    • Multiple sclerosis is primarily a neurodegenerative disease
    • Chaudhuri, A. (2013). Multiple sclerosis is primarily a neurodegenerative disease. J. Neural Transm. 120, 1463-1466. doi: 10.1007/s00702-013-1080-3
    • (2013) J. Neural Transm , vol.120 , pp. 1463-1466
    • Chaudhuri, A.1
  • 29
    • 33644782816 scopus 로고    scopus 로고
    • Identification of a new class of prostaglandin transporter inhibitors and characterization of their biological effects on prostaglandin E2 transport
    • Chi, Y., Khersonsky, S. M., Chang, Y. T., and Schuster, V. L. (2006). Identification of a new class of prostaglandin transporter inhibitors and characterization of their biological effects on prostaglandin E2 transport. J. Pharmacol. Exp. Ther. 316, 1346-1350. doi: 10.1124/jpet.105.091975
    • (2006) J. Pharmacol. Exp. Ther , vol.316 , pp. 1346-1350
    • Chi, Y.1    Khersonsky, S.M.2    Chang, Y.T.3    Schuster, V.L.4
  • 30
    • 80054775987 scopus 로고    scopus 로고
    • Development of a high-affinity inhibitor of the prostaglandin transporter
    • Chi, Y., Min, J., Jasmin, J. F., Lisanti, M. P., Chang, Y. T., and Schuster, V. L. (2011). Development of a high-affinity inhibitor of the prostaglandin transporter. J. Pharmacol. Exp. Ther. 339, 633-641. doi: 10.1124/jpet.111.181354
    • (2011) J. Pharmacol. Exp. Ther , vol.339 , pp. 633-641
    • Chi, Y.1    Min, J.2    Jasmin, J.F.3    Lisanti, M.P.4    Chang, Y.T.5    Schuster, V.L.6
  • 31
    • 77951620812 scopus 로고    scopus 로고
    • The prostaglandin transporter PGT transports PGH(2)
    • Chi, Y., and Schuster, V. L. (2010). The prostaglandin transporter PGT transports PGH(2). Biochem. Biophys. Res. Commun. 395, 168-172. doi: 10.1016/j.bbrc.2010.03.108
    • (2010) Biochem. Biophys. Res. Commun , vol.395 , pp. 168-172
    • Chi, Y.1    Schuster, V.L.2
  • 32
    • 84938558801 scopus 로고    scopus 로고
    • Regulation of prostaglandin EP1 and EP4 receptor signaling by carrier-meditaed ligand reuptake
    • Chi, Y., Suadicani, S., and Schuster, V. L. (2014). Regulation of prostaglandin EP1 and EP4 receptor signaling by carrier-meditaed ligand reuptake. Pharma Res. Per. 2:e00051. doi: 10.1002/prp2.51
    • (2014) Pharma Res. Per , vol.2
    • Chi, Y.1    Suadicani, S.2    Schuster, V.L.3
  • 34
    • 1842581669 scopus 로고    scopus 로고
    • Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases
    • Choi, J., Levey, A. I., Weintraub, S. T., Rees, H. D., Gearing, M., Chin, L. S., et al. (2004). Oxidative modifications and down-regulation of ubiquitin carboxyl-terminal hydrolase L1 associated with idiopathic Parkinson's and Alzheimer's diseases. J. Biol. Chem. 279, 13256-13264. doi: 10.1074/jbc.M314124200
    • (2004) J. Biol. Chem , vol.279 , pp. 13256-13264
    • Choi, J.1    Levey, A.I.2    Weintraub, S.T.3    Rees, H.D.4    Gearing, M.5    Chin, L.S.6
  • 35
    • 41949138921 scopus 로고    scopus 로고
    • Expression and localization of prostaglandin transporter in Alzheimer disease brains and age-matched controls
    • Choi, K., Zhuang, H., Crain, B., and Dore, S. (2008). Expression and localization of prostaglandin transporter in Alzheimer disease brains and age-matched controls. J. Neuroimmunol. 195, 81-87. doi: 10.1016/j.jneuroim.2008.01.014
    • (2008) J. Neuroimmunol , vol.195 , pp. 81-87
    • Choi, K.1    Zhuang, H.2    Crain, B.3    Dore, S.4
  • 36
    • 62949176283 scopus 로고    scopus 로고
    • The distinct roles of cyclooxygenase-1 and -2 in neuroinflammation: Implications for translational research
    • Choi, S. H., Aid, S., and Bosetti, F. (2009). The distinct roles of cyclooxygenase-1 and -2 in neuroinflammation: implications for translational research. Trends Pharmacol. Sci. 30, 174-181. doi: 10.1016/j.tips.2009.01.002
    • (2009) Trends Pharmacol. Sci , vol.30 , pp. 174-181
    • Choi, S.H.1    Aid, S.2    Bosetti, F.3
  • 38
    • 0032884254 scopus 로고    scopus 로고
    • Influence of J series prostaglandins on apoptosis and tumorigenesis of breast cancer cells
    • Clay, C. E., Namen, A. M., Atsumi, G., Willingham, M. C., High, K. P., Kute, T. E., et al. (1999). Influence of J series prostaglandins on apoptosis and tumorigenesis of breast cancer cells. Carcinogenesis 20, 1905-1911. doi: 10.1093/carcin/20.10.1905
    • (1999) Carcinogenesis , vol.20 , pp. 1905-1911
    • Clay, C.E.1    Namen, A.M.2    Atsumi, G.3    Willingham, M.C.4    High, K.P.5    Kute, T.E.6
  • 39
    • 0034651101 scopus 로고    scopus 로고
    • Inflammatory mechanisms in Alzheimer's disease: Inhibition of beta-amyloid-stimulated proinflammatory responses and neurotoxicity by PPARgamma agonists
    • Combs, C. K., Johnson, D. E., Karlo, J. C., Cannady, S. B., and Landreth, G. E. (2000). Inflammatory mechanisms in Alzheimer's disease: inhibition of beta-amyloid-stimulated proinflammatory responses and neurotoxicity by PPARgamma agonists. J. Neurosci. 20, 558-567.
    • (2000) J. Neurosci , vol.20 , pp. 558-567
    • Combs, C.K.1    Johnson, D.E.2    Karlo, J.C.3    Cannady, S.B.4    Landreth, G.E.5
  • 40
    • 1842714301 scopus 로고    scopus 로고
    • Neuroinflammation, COX-2, and ALS-a dual role?
    • Consilvio, C., Vincent, A. M., and Feldman, E. L. (2004). Neuroinflammation, COX-2, and ALS-a dual role? Exp. Neurol. 187, 1-10. doi: 10.1016/j.expneurol.2003.12.009
    • (2004) Exp. Neurol , vol.187 , pp. 1-10
    • Consilvio, C.1    Vincent, A.M.2    Feldman, E.L.3
  • 41
    • 84907328599 scopus 로고    scopus 로고
    • Deubiquitinating enzyme inhibitors and their potential in cancer therapy
    • Crosas, B. (2014). Deubiquitinating enzyme inhibitors and their potential in cancer therapy. Curr. Cancer Drug Targets 14, 506-516. doi: 10.2174/1568009614666140725090620
    • (2014) Curr. Cancer Drug Targets , vol.14 , pp. 506-516
    • Crosas, B.1
  • 42
    • 84897954152 scopus 로고    scopus 로고
    • Therapeutic implications of the prostaglandin pathway in Alzheimer's disease
    • Cudaback, E., Jorstad, N. L., Yang, Y., Montine, T. J., and Keene, C. D. (2014). Therapeutic implications of the prostaglandin pathway in Alzheimer's disease. Biochem. Pharmacol. 88, 565-572. doi: 10.1016/j.bcp.2013.12.014
    • (2014) Biochem. Pharmacol , vol.88 , pp. 565-572
    • Cudaback, E.1    Jorstad, N.L.2    Yang, Y.3    Montine, T.J.4    Keene, C.D.5
  • 45
    • 79957989551 scopus 로고    scopus 로고
    • PACAP and a novel stable analog protect rat brain from ischemia: Insight into the mechanisms of action
    • Dejda, A., Seaborn, T., Bourgault, S., Touzani, O., Fournier, A., Vaudry, H., et al. (2011). PACAP and a novel stable analog protect rat brain from ischemia: insight into the mechanisms of action. Peptides 32, 1207-1216. doi: 10.1016/j.peptides.2011.04.003
    • (2011) Peptides , vol.32 , pp. 1207-1216
    • Dejda, A.1    Seaborn, T.2    Bourgault, S.3    Touzani, O.4    Fournier, A.5    Vaudry, H.6
  • 46
    • 0036499074 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma agonist 15-deoxy-Delta(12,14)-prostaglandin J(2) ameliorates experimental autoimmune encephalomyelitis
    • Diab, A., Deng, C., Smith, J. D., Hussain, R. Z., Phanavanh, B., Lovett-Racke, A. E., et al. (2002). Peroxisome proliferator-activated receptor-gamma agonist 15-deoxy-Delta(12,14)-prostaglandin J(2) ameliorates experimental autoimmune encephalomyelitis. J. Immunol. 168, 2508-2515. doi: 10.4049/jimmunol.168.5.2508
    • (2002) J. Immunol , vol.168 , pp. 2508-2515
    • Diab, A.1    Deng, C.2    Smith, J.D.3    Hussain, R.Z.4    Phanavanh, B.5    Lovett-Racke, A.E.6
  • 47
    • 76549096602 scopus 로고    scopus 로고
    • Mitochondrial targeting of the electrophilic lipid 15-deoxy-Delta12,14-prostaglandin J2 increases apoptotic efficacy via redox cell signalling mechanisms
    • Diers, A. R., Higdon, A. N., Ricart, K. C., Johnson, M. S., Agarwal, A., Kalyanaraman, B., et al. (2010). Mitochondrial targeting of the electrophilic lipid 15-deoxy-Delta12,14-prostaglandin J2 increases apoptotic efficacy via redox cell signalling mechanisms. Biochem. J. 426, 31-41. doi: 10.1042/BJ20091293
    • (2010) Biochem. J , vol.426 , pp. 31-41
    • Diers, A.R.1    Higdon, A.N.2    Ricart, K.C.3    Johnson, M.S.4    Agarwal, A.5    Kalyanaraman, B.6
  • 48
    • 56549096129 scopus 로고    scopus 로고
    • Human embryonic stem cell-derived motor neurons are sensitive to the toxic effect of glial cells carrying an ALS-causing mutation
    • Di Giorgio, F. P., Boulting, G. L., Bobrowicz, S., and Eggan, K. C. (2008). Human embryonic stem cell-derived motor neurons are sensitive to the toxic effect of glial cells carrying an ALS-causing mutation. Cell Stem Cell 3, 637-648. doi: 10.1016/j.stem.2008.09.017
    • (2008) Cell Stem Cell , vol.3 , pp. 637-648
    • Di Giorgio, F.P.1    Boulting, G.L.2    Bobrowicz, S.3    Eggan, K.C.4
  • 49
    • 0018966157 scopus 로고
    • Hereditary leucodystrophy in the mouse: The new mutant twitcher
    • Duchen, L. W., Eicher, E. M., Jacobs, J. M., Scaravilli, F., and Teixeira, F. (1980). Hereditary leucodystrophy in the mouse: the new mutant twitcher. Brain 103, 695-710. doi: 10.1093/brain/103.3.695
    • (1980) Brain , vol.103 , pp. 695-710
    • Duchen, L.W.1    Eicher, E.M.2    Jacobs, J.M.3    Scaravilli, F.4    Teixeira, F.5
  • 50
    • 84857085837 scopus 로고    scopus 로고
    • Pharmacological targets in the ubiquitin system offer new ways of treating cancer, neurodegenerative disorders and infectious diseases
    • Edelmann, M. J., Nicholson, B., and Kessler, B. M. (2011). Pharmacological targets in the ubiquitin system offer new ways of treating cancer, neurodegenerative disorders and infectious diseases. Expert Rev. Mol. Med. 13, e35. doi: 10.1017/S1462399411002031
    • (2011) Expert Rev. Mol. Med , vol.13 , pp. e35
    • Edelmann, M.J.1    Nicholson, B.2    Kessler, B.M.3
  • 51
    • 84890190983 scopus 로고    scopus 로고
    • Regulation of proteolysis by human deubiquitinating enzymes
    • Eletr, Z. M., and Wilkinson, K. D. (2014). Regulation of proteolysis by human deubiquitinating enzymes. Biochim. Biophys. Acta 1843, 114-128. doi: 10.1016/j.bbamcr.2013.06.027
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 114-128
    • Eletr, Z.M.1    Wilkinson, K.D.2
  • 52
    • 9344263462 scopus 로고    scopus 로고
    • Ligands of peroxisome proliferator-activated receptor gamma induce apoptosis in multiple myeloma
    • Eucker, J., Bangeroth, K., Zavrski, I., Krebbel, H., Zang, C., Heider, U., et al. (2004). Ligands of peroxisome proliferator-activated receptor gamma induce apoptosis in multiple myeloma. Anticancer Drugs 15, 955-960. doi: 10.1097/00001813-200411000-00004
    • (2004) Anticancer Drugs , vol.15 , pp. 955-960
    • Eucker, J.1    Bangeroth, K.2    Zavrski, I.3    Krebbel, H.4    Zang, C.5    Heider, U.6
  • 53
    • 84864150600 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Parkinson's disease: Molecular mechanisms and pathophysiological consequences
    • Exner, N., Lutz, A. K., Haass, C., and Winklhofer, K. F. (2012). Mitochondrial dysfunction in Parkinson's disease: molecular mechanisms and pathophysiological consequences. EMBO J. 31, 3038-3062. doi: 10.1038/emboj.2012.170
    • (2012) EMBO J , vol.31 , pp. 3038-3062
    • Exner, N.1    Lutz, A.K.2    Haass, C.3    Winklhofer, K.F.4
  • 54
    • 0642339281 scopus 로고    scopus 로고
    • COX-2-deficient mice are less prone to MPTP-neurotoxicity than wild-type mice
    • Feng, Z., Li, D., Fung, P. C., Pei, Z., Ramsden, D. B., and Ho, S. L. (2003). COX-2-deficient mice are less prone to MPTP-neurotoxicity than wild-type mice. Neuroreport 14, 1927-1929. doi: 10.1097/00001756-200310270-00009
    • (2003) Neuroreport , vol.14 , pp. 1927-1929
    • Feng, Z.1    Li, D.2    Fung, P.C.3    Pei, Z.4    Ramsden, D.B.5    Ho, S.L.6
  • 55
    • 0035976575 scopus 로고    scopus 로고
    • Prostaglandins and leukotrienes: Advances in eicosanoid biology
    • Funk, C. D. (2001). Prostaglandins and leukotrienes: advances in eicosanoid biology. Science 294, 1871-1875. doi: 10.1126/science.294.5548.1871
    • (2001) Science , vol.294 , pp. 1871-1875
    • Funk, C.D.1
  • 56
    • 0041689948 scopus 로고    scopus 로고
    • Caspase cleavage of tau: Linking amyloid and neurofibrillary tangles in Alzheimer's disease
    • Gamblin, T. C., Chen, F., Zambrano, A., Abraha, A., Lagalwar, S., Guillozet, A. L., et al. (2003). Caspase cleavage of tau: linking amyloid and neurofibrillary tangles in Alzheimer's disease. Proc. Natl. Acad. Sci. U.S.A. 100, 10032-10037. doi: 10.1073/pnas.1630428100
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 10032-10037
    • Gamblin, T.C.1    Chen, F.2    Zambrano, A.3    Abraha, A.4    Lagalwar, S.5    Guillozet, A.L.6
  • 57
    • 77649185235 scopus 로고    scopus 로고
    • Eicosanoids and the endogenous control of acute inflammatory resolution
    • Gilroy, D. W. (2010). Eicosanoids and the endogenous control of acute inflammatory resolution. Int. J. Biochem. Cell Biol. 42, 524-528. doi: 10.1016/j.biocel.2009.12.013
    • (2010) Int. J. Biochem. Cell Biol , vol.42 , pp. 524-528
    • Gilroy, D.W.1
  • 58
    • 6344278016 scopus 로고    scopus 로고
    • The 15-deoxy-delta12,14-prostaglandin J2 inhibits the inflammatory response in primary rat astrocytes via down-regulating multiple steps in phosphatidylinositol 3-kinase-Akt-NF-kappaB-p300 pathway independent of peroxisome proliferator-activated receptor gamma
    • Giri, S., Rattan, R., Singh, A. K., and Singh, I. (2004). The 15-deoxy-delta12,14-prostaglandin J2 inhibits the inflammatory response in primary rat astrocytes via down-regulating multiple steps in phosphatidylinositol 3-kinase-Akt-NF-kappaB-p300 pathway independent of peroxisome proliferator-activated receptor gamma. J. Immunol. 173, 5196-5208. doi: 10.4049/jimmunol.173.8.5196
    • (2004) J. Immunol , vol.173 , pp. 5196-5208
    • Giri, S.1    Rattan, R.2    Singh, A.K.3    Singh, I.4
  • 59
    • 77950363010 scopus 로고    scopus 로고
    • Mechanisms underlying inflammation in neurodegeneration
    • Glass, C. K., Saijo, K., Winner, B., Marchetto, M. C., and Gage, F. H. (2010). Mechanisms underlying inflammation in neurodegeneration. Cell 140, 918-934. doi: 10.1016/j.cell.2010.02.016
    • (2010) Cell , vol.140 , pp. 918-934
    • Glass, C.K.1    Saijo, K.2    Winner, B.3    Marchetto, M.C.4    Gage, F.H.5
  • 60
    • 39149105267 scopus 로고    scopus 로고
    • Brain prostaglandin formation is increased by alpha-synuclein gene-ablation during global ischemia
    • Golovko, M. Y., and Murphy, E. J. (2008). Brain prostaglandin formation is increased by alpha-synuclein gene-ablation during global ischemia. Neurosci. Lett. 432, 243-247. doi: 10.1016/j.neulet.2007.12.031
    • (2008) Neurosci. Lett , vol.432 , pp. 243-247
    • Golovko, M.Y.1    Murphy, E.J.2
  • 61
    • 33744949939 scopus 로고    scopus 로고
    • Acyl-CoA synthetase activity links wild-type but not mutant alpha-synuclein to brain arachidonate metabolism
    • Golovko, M. Y., Rosenberger, T. A., Faergeman, N. J., Feddersen, S., Cole, N. B., Pribill, I., et al. (2006). Acyl-CoA synthetase activity links wild-type but not mutant alpha-synuclein to brain arachidonate metabolism.Biochemistry 45, 6956-6966. doi: 10.1021/bi0600289
    • (2006) Biochemistry , vol.45 , pp. 6956-6966
    • Golovko, M.Y.1    Rosenberger, T.A.2    Faergeman, N.J.3    Feddersen, S.4    Cole, N.B.5    Pribill, I.6
  • 62
    • 33750475625 scopus 로고    scopus 로고
    • Free radicals, mitochondria, and oxidized lipids: The emerging role in signal transduction in vascular cells
    • Gutierrez, J., Ballinger, S. W., Darley-Usmar, V. M., and Landar, A. (2006). Free radicals, mitochondria, and oxidized lipids: the emerging role in signal transduction in vascular cells. Circ. Res. 99, 924-932. doi: 10.1161/01.RES.0000248212.86638.e9
    • (2006) Circ. Res , vol.99 , pp. 924-932
    • Gutierrez, J.1    Ballinger, S.W.2    Darley-Usmar, V.M.3    Landar, A.4
  • 63
    • 0020478717 scopus 로고
    • Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation
    • Haas, A. L., Warms, J. V., Hershko, A., and Rose, I. A. (1982). Ubiquitin-activating enzyme. Mechanism and role in protein-ubiquitin conjugation. J. Biol. Chem. 257, 2543-2548.
    • (1982) J. Biol. Chem , vol.257 , pp. 2543-2548
    • Haas, A.L.1    Warms, J.V.2    Hershko, A.3    Rose, I.A.4
  • 64
    • 84861220041 scopus 로고    scopus 로고
    • Prostaglandin EP1 receptor down-regulates expression of cyclooxygenase-2 by facilitating its proteasomal degradation
    • Haddad, A., Flint-Ashtamker, G., Minzel, W., Sood, R., Rimon, G., and Barki-Harrington, L. (2012). Prostaglandin EP1 receptor down-regulates expression of cyclooxygenase-2 by facilitating its proteasomal degradation. J. Biol. Chem. 287, 17214-17223. doi: 10.1074/jbc.M111.304220
    • (2012) J. Biol. Chem , vol.287 , pp. 17214-17223
    • Haddad, A.1    Flint-Ashtamker, G.2    Minzel, W.3    Sood, R.4    Rimon, G.5    Barki-Harrington, L.6
  • 65
    • 78650919059 scopus 로고    scopus 로고
    • Nonenzymatic free radical-catalyzed generation of 15-deoxy-Delta(12,14)-prostaglandin J(2)-like compounds (deoxy-J(2)-isoprostanes) in vivo
    • Hardy, K. D., Cox, B. E., Milne, G. L., Yin, H., and Roberts, L. J. (2011). Nonenzymatic free radical-catalyzed generation of 15-deoxy-Delta(12,14)-prostaglandin J(2)-like compounds (deoxy-J(2)-isoprostanes) in vivo. J. Lipid Res. 52, 113-124. doi: 10.1194/jlr.M010264
    • (2011) J. Lipid Res , vol.52 , pp. 113-124
    • Hardy, K.D.1    Cox, B.E.2    Milne, G.L.3    Yin, H.4    Roberts, L.J.5
  • 66
    • 29244452165 scopus 로고    scopus 로고
    • Prostaglandin D synthase isoforms from cerebrospinal fluid vary with brain pathology
    • Harrington, M. G., Fonteh, A. N., Biringer, R. G., AF, R. H., and Cowan, R. P. (2006). Prostaglandin D synthase isoforms from cerebrospinal fluid vary with brain pathology. Dis. Markers 22, 73-81. doi: 10.1155/2006/241817
    • (2006) Dis. Markers , vol.22 , pp. 73-81
    • Harrington, M.G.1    Fonteh, A.N.2    Biringer, R.G.A.F.R.H.3    Cowan, R.P.4
  • 67
    • 0036499224 scopus 로고    scopus 로고
    • Prostaglandins as modulators of immunity
    • Harris, S. G., Padilla, J., Koumas, L., Ray, D., and Phipps, R. P. (2002). Prostaglandins as modulators of immunity.Trends Immunol. 23, 144-150. doi: 10.1016/S1471-4906(01)02154-8
    • (2002) Trends Immunol , vol.23 , pp. 144-150
    • Harris, S.G.1    Padilla, J.2    Koumas, L.3    Ray, D.4    Phipps, R.P.5
  • 68
    • 84873308914 scopus 로고    scopus 로고
    • 15-Deoxy-Delta12,14-prostaglandin J2 (15d-PGJ2) protects neurons from oxidative death via an Nrf2 astrocyte-specific mechanism independent of PPARgamma
    • Haskew-Layton, R. E., Payappilly, J. B., Xu, H., Bennett, S. A., and Ratan, R. R. (2013). 15-Deoxy-Delta12,14-prostaglandin J2 (15d-PGJ2) protects neurons from oxidative death via an Nrf2 astrocyte-specific mechanism independent of PPARgamma. J. Neurochem. 124, 536-547. doi: 10.1111/jnc.12107
    • (2013) J. Neurochem , vol.124 , pp. 536-547
    • Haskew-Layton, R.E.1    Payappilly, J.B.2    Xu, H.3    Bennett, S.A.4    Ratan, R.R.5
  • 69
    • 4444262310 scopus 로고    scopus 로고
    • Pharmacology and signaling of prostaglandin receptors: Multiple roles in inflammation and immune modulation
    • Hata, A. N., and Breyer, R. M. (2004). Pharmacology and signaling of prostaglandin receptors: multiple roles in inflammation and immune modulation. Pharmacol. Ther. 103, 147-166. doi: 10.1016/j.pharmthera.2004.06.003
    • (2004) Pharmacol. Ther , vol.103 , pp. 147-166
    • Hata, A.N.1    Breyer, R.M.2
  • 70
    • 78650403081 scopus 로고    scopus 로고
    • Reimagining Alzheimer's disease-an age-based hypothesis
    • Herrup, K. (2010). Reimagining Alzheimer's disease-an age-based hypothesis. J. Neurosci. 30, 16755-16762. doi: 10.1523/JNEUROSCI.4521-10.2010
    • (2010) J. Neurosci , vol.30 , pp. 16755-16762
    • Herrup, K.1
  • 71
    • 0024434811 scopus 로고
    • Formation and function of eicosanoids in the central nervous system
    • Hertting, G., and Seregi, A. (1989). Formation and function of eicosanoids in the central nervous system. Ann. N. Y. Acad. Sci. 559, 84-99. doi: 10.1111/j.1749-6632.1989.tb22600.x
    • (1989) Ann. N. Y. Acad. Sci , vol.559 , pp. 84-99
    • Hertting, G.1    Seregi, A.2
  • 72
    • 34548136578 scopus 로고    scopus 로고
    • Cyclooxygenase-2 activity following traumatic brain injury in the developing rat
    • Hickey, R. W., Adelson, P. D., Johnnides, M. J., Davis, D. S., Yu, Z., Rose, M. E., et al. (2007). Cyclooxygenase-2 activity following traumatic brain injury in the developing rat. Pediatr. Res. 62, 271-276. doi: 10.1203/PDR.0b013e3180db2902
    • (2007) Pediatr. Res , vol.62 , pp. 271-276
    • Hickey, R.W.1    Adelson, P.D.2    Johnnides, M.J.3    Davis, D.S.4    Yu, Z.5    Rose, M.E.6
  • 73
    • 84857833776 scopus 로고    scopus 로고
    • Cell signalling by reactive lipid species: New concepts and molecular mechanisms
    • Higdon, A., Diers, A. R., Oh, J. Y., Landar, A., and Darley-Usmar, V. M. (2012a). Cell signalling by reactive lipid species: new concepts and molecular mechanisms. Biochem. J. 442, 453-464.
    • (2012) Biochem. J , vol.442 , pp. 453-464
    • Higdon, A.1    Diers, A.R.2    Oh, J.Y.3    Landar, A.4    Darley-Usmar, V.M.5
  • 74
    • 84864393985 scopus 로고    scopus 로고
    • The electrophile responsive proteome: Integrating proteomics and lipidomics with cellular function
    • Higdon, A. N., Landar, A., Barnes, S., and Darley-Usmar, V. M. (2012b). The electrophile responsive proteome: integrating proteomics and lipidomics with cellular function. Antioxid. Redox. Signal. 17, 1580-1589. doi: 10.1089/ars.2012.4523
    • (2012) Antioxid. Redox. Signal , vol.17 , pp. 1580-1589
    • Higdon, A.N.1    Landar, A.2    Barnes, S.3    Darley-Usmar, V.M.4
  • 75
    • 0023796962 scopus 로고
    • Occurrence of 9-deoxy-delta 9,delta 12-13,14-dihydroprostaglandin D2 in human urine
    • Hirata, Y., Hayashi, H., Ito, S., Kikawa, Y., Ishibashi, M., Sudo, M., et al. (1988). Occurrence of 9-deoxy-delta 9,delta 12-13,14-dihydroprostaglandin D2 in human urine. J. Biol. Chem. 263, 16619-16625.
    • (1988) J. Biol. Chem , vol.263 , pp. 16619-16625
    • Hirata, Y.1    Hayashi, H.2    Ito, S.3    Kikawa, Y.4    Ishibashi, M.5    Sudo, M.6
  • 76
    • 34347262128 scopus 로고    scopus 로고
    • LipoCardium: Endothelium-directed cyclopentenone prostaglandin-based liposome formulation that completely reverses atherosclerotic lesions
    • Homem de Bittencourt, P. I. Jr., Lagranha, D. J., Maslinkiewicz, A., Senna, S. M., Tavares, A. M., Baldissera, L. P., et al. (2007). LipoCardium: endothelium-directed cyclopentenone prostaglandin-based liposome formulation that completely reverses atherosclerotic lesions. Atherosclerosis 193, 245-258. doi: 10.1016/j.atherosclerosis.2006.08.049
    • (2007) Atherosclerosis , vol.193 , pp. 245-258
    • Homem de Bittencourt, P.I.1    Lagranha, D.J.2    Maslinkiewicz, A.3    Senna, S.M.4    Tavares, A.M.5    Baldissera, L.P.6
  • 77
    • 0029742199 scopus 로고    scopus 로고
    • Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice [see comments]
    • Hsiao, K., Chapman, P., Nilsen, S., Eckman, C., Harigaya, Y., Younkin, S., et al. (1996). Correlative memory deficits, Abeta elevation, and amyloid plaques in transgenic mice [see comments]. Science 274, 99-102. doi: 10.1126/science.274.5284.99
    • (1996) Science , vol.274 , pp. 99-102
    • Hsiao, K.1    Chapman, P.2    Nilsen, S.3    Eckman, C.4    Harigaya, Y.5    Younkin, S.6
  • 78
    • 84876903554 scopus 로고    scopus 로고
    • Negative regulation of 26S proteasome stability via calpain-mediated cleavage of Rpn10 subunit upon mitochondrial dysfunction in neurons
    • Huang, Q., Wang, H., Perry, S. W., and Figueiredo-Pereira, M. E. (2013). Negative regulation of 26S proteasome stability via calpain-mediated cleavage of Rpn10 subunit upon mitochondrial dysfunction in neurons. J. Biol. Chem. 288, 12161-12174. doi: 10.1074/jbc.M113.464552
    • (2013) J. Biol. Chem , vol.288 , pp. 12161-12174
    • Huang, Q.1    Wang, H.2    Perry, S.W.3    Figueiredo-Pereira, M.E.4
  • 79
    • 12844282180 scopus 로고    scopus 로고
    • The Janus face of cyclooxygenase-2 in ischemic stroke: Shifting toward downstream targets
    • Iadecola, C., and Gorelick, P. B. (2005). The Janus face of cyclooxygenase-2 in ischemic stroke: shifting toward downstream targets. Stroke 36, 182-185. doi: 10.1161/01.STR.0000153797.33611.d8
    • (2005) Stroke , vol.36 , pp. 182-185
    • Iadecola, C.1    Gorelick, P.B.2
  • 80
    • 27144441722 scopus 로고    scopus 로고
    • Oxidative modification of proteasome: Identification of an oxidation-sensitive subunit in 26 s proteasome
    • Ishii, T., Sakurai, T., Usami, H., and Uchida, K. (2005). Oxidative modification of proteasome: identification of an oxidation-sensitive subunit in 26 s proteasome. Biochemistry 44, 13893-13901. doi: 10.1021/bi051336u
    • (2005) Biochemistry , vol.44 , pp. 13893-13901
    • Ishii, T.1    Sakurai, T.2    Usami, H.3    Uchida, K.4
  • 81
    • 6344238985 scopus 로고    scopus 로고
    • Induction of reversible cysteine-targeted protein oxidation by an endogenous electrophile 15-deoxy-delta12,14-prostaglandin J2
    • Ishii, T., and Uchida, K. (2004). Induction of reversible cysteine-targeted protein oxidation by an endogenous electrophile 15-deoxy-delta12,14-prostaglandin J2. Chem. Res. Toxicol. 17, 1313-1322. doi: 10.1021/tx049860+
    • (2004) Chem. Res. Toxicol , vol.17 , pp. 1313-1322
    • Ishii, T.1    Uchida, K.2
  • 82
    • 10744230015 scopus 로고    scopus 로고
    • Transcription factor Nrf2 regulates inflammation by mediating the effect of 15-deoxy-Delta(12,14)-prostaglandin j(2)
    • Itoh, K., Mochizuki, M., Ishii, Y., Ishii, T., Shibata, T., Kawamoto, Y., et al. (2004). Transcription factor Nrf2 regulates inflammation by mediating the effect of 15-deoxy-Delta(12,14)-prostaglandin j(2). Mol. Cell Biol. 24, 36-45. doi: 10.1128/MCB.24.1.36-45.2004
    • (2004) Mol. Cell Biol , vol.24 , pp. 36-45
    • Itoh, K.1    Mochizuki, M.2    Ishii, Y.3    Ishii, T.4    Shibata, T.5    Kawamoto, Y.6
  • 83
    • 0030265669 scopus 로고    scopus 로고
    • Structural determinants of substrates for the prostaglandin transporter PGT
    • Itoh, S., Lu, R., Bao, Y., Morrow, J. D., Roberts, L. J., and Schuster, V. L. (1996). Structural determinants of substrates for the prostaglandin transporter PGT. Mol. Pharmacol. 50, 738-742.
    • (1996) Mol. Pharmacol , vol.50 , pp. 738-742
    • Itoh, S.1    Lu, R.2    Bao, Y.3    Morrow, J.D.4    Roberts, L.J.5    Schuster, V.L.6
  • 84
    • 0024515832 scopus 로고
    • The formation of prostaglandins in the postmortem cerebral cortex of Alzheimer-type dementia patients
    • Iwamoto, N., Kobayashi, K., and Kosaka, K. (1989). The formation of prostaglandins in the postmortem cerebral cortex of Alzheimer-type dementia patients. J. Neurol. 236, 80-84. doi: 10.1007/BF00314401
    • (1989) J. Neurol , vol.236 , pp. 80-84
    • Iwamoto, N.1    Kobayashi, K.2    Kosaka, K.3
  • 85
    • 69249211014 scopus 로고    scopus 로고
    • Prostanoid receptor antagonists: Development strategies and therapeutic applications
    • Jones, R. L., Giembycz, M. A., and Woodward, D. F. (2009). Prostanoid receptor antagonists: development strategies and therapeutic applications. Br. J. Pharmacol. 158, 104-145. doi: 10.1111/j.1476-5381.2009.00317.x
    • (2009) Br. J. Pharmacol , vol.158 , pp. 104-145
    • Jones, R.L.1    Giembycz, M.A.2    Woodward, D.F.3
  • 86
    • 0029078231 scopus 로고
    • Identification and characterization of a prostaglandin transporter
    • Kanai, N., Lu, R., Satriano, J. A., Bao, Y., Wolkoff, A. W., and Schuster, V. L. (1995). Identification and characterization of a prostaglandin transporter. Science 268, 866-869. doi: 10.1126/science.7754369
    • (1995) Science , vol.268 , pp. 866-869
    • Kanai, N.1    Lu, R.2    Satriano, J.A.3    Bao, Y.4    Wolkoff, A.W.5    Schuster, V.L.6
  • 88
    • 34250854262 scopus 로고    scopus 로고
    • Lipocalin-type prostaglandin D synthase/beta-trace is a major amyloid beta-chaperone in human cerebrospinal fluid
    • Kanekiyo, T., Ban, T., Aritake, K., Huang, Z. L., Qu, W. M., Okazaki, I., et al. (2007). Lipocalin-type prostaglandin D synthase/beta-trace is a major amyloid beta-chaperone in human cerebrospinal fluid. Proc. Natl. Acad. Sci. U.S.A. 104, 6412-6417. doi: 10.1073/pnas.0701585104
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 6412-6417
    • Kanekiyo, T.1    Ban, T.2    Aritake, K.3    Huang, Z.L.4    Qu, W.M.5    Okazaki, I.6
  • 89
    • 38449085356 scopus 로고    scopus 로고
    • Mechanisms of anti-inflammatory and neuroprotective actions of PPAR-gamma agonists
    • Kapadia, R., Yi, J. H., and Vemuganti, R. (2008). Mechanisms of anti-inflammatory and neuroprotective actions of PPAR-gamma agonists. Front. Biosci. 13:1813-1826. doi: 10.2741/2802
    • (2008) Front. Biosci , vol.13 , pp. 1813-1826
    • Kapadia, R.1    Yi, J.H.2    Vemuganti, R.3
  • 90
    • 70349843323 scopus 로고    scopus 로고
    • Nrf2:INrf2 (Keap1) signaling in oxidative stress
    • Kaspar, J. W., Niture, S. K., and Jaiswal, A. K. (2009). Nrf2:INrf2 (Keap1) signaling in oxidative stress. Free Radic. Biol. Med. 47, 1304-1309. doi: 10.1016/j.freeradbiomed.2009.07.035
    • (2009) Free Radic. Biol. Med , vol.47 , pp. 1304-1309
    • Kaspar, J.W.1    Niture, S.K.2    Jaiswal, A.K.3
  • 91
    • 77950272320 scopus 로고    scopus 로고
    • 15-Deoxy-delta 12,14-prostaglandin J2 biphasically regulates the proliferation of mouse hippocampal neural progenitor cells by modulating the redox state
    • Katura, T., Moriya, T., and Nakahata, N. (2010). 15-Deoxy-delta 12,14-prostaglandin J2 biphasically regulates the proliferation of mouse hippocampal neural progenitor cells by modulating the redox state. Mol. Pharmacol. 77, 601-611. doi: 10.1124/mol.109.061010
    • (2010) Mol. Pharmacol , vol.77 , pp. 601-611
    • Katura, T.1    Moriya, T.2    Nakahata, N.3
  • 92
    • 44049091481 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor-gamma in amyotrophic lateral sclerosis and Huntington's disease
    • Kiaei, M. (2008). Peroxisome proliferator-activated receptor-gamma in amyotrophic lateral sclerosis and Huntington's disease. PPAR. Res. 2008, 418765. doi: 10.1155/2008/418765
    • (2008) PPAR. Res , vol.2008
    • Kiaei, M.1
  • 93
    • 41849150053 scopus 로고    scopus 로고
    • 15-Deoxy-Delta12,14-prostaglandin J2 induces COX-2 expression through Akt-driven AP-1 activation in human breast cancer cells: A potential role of ROS
    • Kim, E. H., Na, H. K., Kim, D. H., Park, S. A., Kim, H. N., Song, N. Y., et al. (2008). 15-Deoxy-Delta12,14-prostaglandin J2 induces COX-2 expression through Akt-driven AP-1 activation in human breast cancer cells: a potential role of ROS. Carcinogenesis 29, 688-695. doi: 10.1093/carcin/bgm299
    • (2008) Carcinogenesis , vol.29 , pp. 688-695
    • Kim, E.H.1    Na, H.K.2    Kim, D.H.3    Park, S.A.4    Kim, H.N.5    Song, N.Y.6
  • 94
    • 79952038944 scopus 로고    scopus 로고
    • 15-Deoxy-Delta12,14-prostaglandin J2 induces Cox-2 expression in human osteosarcoma cells through MAPK and EGFR activation involving reactive oxygen species
    • Kitz, K., Windischhofer, W., Leis, H. J., Huber, E., Kollroser, M., and Malle, E. (2011). 15-Deoxy-Delta12,14-prostaglandin J2 induces Cox-2 expression in human osteosarcoma cells through MAPK and EGFR activation involving reactive oxygen species. Free Radic. Biol. Med. 50, 854-865. doi: 10.1016/j.freeradbiomed.2010.12.039
    • (2011) Free Radic. Biol. Med , vol.50 , pp. 854-865
    • Kitz, K.1    Windischhofer, W.2    Leis, H.J.3    Huber, E.4    Kollroser, M.5    Malle, E.6
  • 95
    • 34248400478 scopus 로고    scopus 로고
    • Therapeutic approaches to inflammation in neurodegenerative disease
    • Klegeris, A., McGeer, E. G., and McGeer, P. L. (2007). Therapeutic approaches to inflammation in neurodegenerative disease. Curr. Opin. Neurol. 20, 351-357. doi: 10.1097/WCO.0b013e3280adc943
    • (2007) Curr. Opin. Neurol , vol.20 , pp. 351-357
    • Klegeris, A.1    McGeer, E.G.2    McGeer, P.L.3
  • 96
    • 4344680646 scopus 로고    scopus 로고
    • Additive neuroprotective effects of creatine and a cyclooxygenase 2 inhibitor against dopamine depletion in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mouse model of Parkinson's disease
    • Klivenyi, P., Gardian, G., Calingasan, N. Y., Yang, L., and Beal, M. F. (2003). Additive neuroprotective effects of creatine and a cyclooxygenase 2 inhibitor against dopamine depletion in the 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP) mouse model of Parkinson's disease. J. Mol. Neurosci. 21, 191-198. doi: 10.1385/JMN:21:3:191
    • (2003) J. Mol. Neurosci , vol.21 , pp. 191-198
    • Klivenyi, P.1    Gardian, G.2    Calingasan, N.Y.3    Yang, L.4    Beal, M.F.5
  • 97
    • 0019274883 scopus 로고
    • The Twitcher mouse: An enzymatically authentic model of human globoid cell leukodystrophy (Krabbe disease)
    • Kobayashi, T., Yamanaka, T., Jacobs, J. M., Teixeira, F., and Suzuki, K. (1980). The Twitcher mouse: an enzymatically authentic model of human globoid cell leukodystrophy (Krabbe disease). Brain Res. 202, 479-483. doi: 10.1016/0006-8993(80)90159-6
    • (1980) Brain Res , vol.202 , pp. 479-483
    • Kobayashi, T.1    Yamanaka, T.2    Jacobs, J.M.3    Teixeira, F.4    Suzuki, K.5
  • 98
    • 77951069130 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandin-induced unfolding and aggregation of the Parkinson disease-associated UCH-L1
    • Koharudin, L. M., Liu, H., Di, M. R., Kodali, R. B., Graham, S. H., and Gronenborn, A. M. (2010). Cyclopentenone prostaglandin-induced unfolding and aggregation of the Parkinson disease-associated UCH-L1. Proc. Natl. Acad. Sci. U.S.A. 107, 6835-6840. doi: 10.1073/pnas.1002295107
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 6835-6840
    • Koharudin, L.M.1    Liu, H.2    Di, M.R.3    Kodali, R.B.4    Graham, S.H.5    Gronenborn, A.M.6
  • 99
    • 0035853707 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandins as potential inducers of intracellular oxidative stress
    • Kondo, M., Oya-Ito, T., Kumagai, T., Osawa, T., and Uchida, K. (2001). Cyclopentenone prostaglandins as potential inducers of intracellular oxidative stress. J. Biol. Chem. 276, 12076-12083. doi: 10.1074/jbc.M009630200
    • (2001) J. Biol. Chem , vol.276 , pp. 12076-12083
    • Kondo, M.1    Oya-Ito, T.2    Kumagai, T.3    Osawa, T.4    Uchida, K.5
  • 100
    • 0012954726 scopus 로고    scopus 로고
    • 15-Deoxy-Delta(12,14)-prostaglandin J(2): The endogenous electrophile that induces neuronal apoptosis
    • Kondo, M., Shibata, T., Kumagai, T., Osawa, T., Shibata, N., Kobayashi, M., et al. (2002). 15-Deoxy-Delta(12,14)-prostaglandin J(2): the endogenous electrophile that induces neuronal apoptosis. Proc. Natl. Acad. Sci. U.S.A. 99, 7367-7372. doi: 10.1073/pnas.112212599
    • (2002) Proc. Natl. Acad. Sci. U.S.A , vol.99 , pp. 7367-7372
    • Kondo, M.1    Shibata, T.2    Kumagai, T.3    Osawa, T.4    Shibata, N.5    Kobayashi, M.6
  • 101
    • 0033843309 scopus 로고    scopus 로고
    • Cyclooxygenase isoenzymes and newer therapeutic potential for selective COX-2 inhibitors
    • Kulkarni, S. K., Jain, N. K., and Singh, A. (2000). Cyclooxygenase isoenzymes and newer therapeutic potential for selective COX-2 inhibitors. Methods Find. Exp. Clin. Pharmacol. 22, 291-298. doi: 10.1358/mf.2000.22.5.796648
    • (2000) Methods Find. Exp. Clin. Pharmacol , vol.22 , pp. 291-298
    • Kulkarni, S.K.1    Jain, N.K.2    Singh, A.3
  • 102
    • 0036737399 scopus 로고    scopus 로고
    • Cyclooxygenase-2, prostaglandin synthases, and prostaglandin H2 metabolism in traumatic brain injury in the rat
    • Kunz, T., Marklund, N., Hillered, L., and Oliw, E. H. (2002). Cyclooxygenase-2, prostaglandin synthases, and prostaglandin H2 metabolism in traumatic brain injury in the rat. J. Neurotrauma 19, 1051-1064. doi: 10.1089/089771502760341965
    • (2002) J. Neurotrauma , vol.19 , pp. 1051-1064
    • Kunz, T.1    Marklund, N.2    Hillered, L.3    Oliw, E.H.4
  • 103
    • 78751703517 scopus 로고    scopus 로고
    • Release of exosomes from differentiated neurons and its regulation by synaptic glutamatergic activity
    • Lachenal, G., Pernet-Gallay, K., Chivet, M., Hemming, F. J., Belly, A., Bodon, G., et al. (2011). Release of exosomes from differentiated neurons and its regulation by synaptic glutamatergic activity. Mol. Cell Neurosci. 46, 409-418. doi: 10.1016/j.mcn.2010.11.004
    • (2011) Mol. Cell Neurosci , vol.46 , pp. 409-418
    • Lachenal, G.1    Pernet-Gallay, K.2    Chivet, M.3    Hemming, F.J.4    Belly, A.5    Bodon, G.6
  • 104
    • 77956527159 scopus 로고    scopus 로고
    • Enhancement of proteasome activity by a small-molecule inhibitor of USP14
    • Lee, B. H., Lee, M. J., Park, S., Oh, D. C., Elsasser, S., Chen, P. C., et al. (2010). Enhancement of proteasome activity by a small-molecule inhibitor of USP14. Nature 467, 179-184. doi: 10.1038/nature09299
    • (2010) Nature , vol.467 , pp. 179-184
    • Lee, B.H.1    Lee, M.J.2    Park, S.3    Oh, D.C.4    Elsasser, S.5    Chen, P.C.6
  • 105
    • 60249095867 scopus 로고    scopus 로고
    • 15-Deoxy-Delta(12,14)-prostaglandin J(2) induces mitochondrial-dependent apoptosis through inhibition of PKA/NF-kappaB in renal proximal epithelial cells
    • Lee, D. R., Kwon, C. H., Park, J. Y., Kim, Y. K., and Woo, J. S. (2009). 15-Deoxy-Delta(12,14)-prostaglandin J(2) induces mitochondrial-dependent apoptosis through inhibition of PKA/NF-kappaB in renal proximal epithelial cells. Toxicology 258, 17-24. doi: 10.1016/j.tox.2009.01.001
    • (2009) Toxicology , vol.258 , pp. 17-24
    • Lee, D.R.1    Kwon, C.H.2    Park, J.Y.3    Kim, Y.K.4    Woo, J.S.5
  • 106
    • 84863341420 scopus 로고    scopus 로고
    • Lipocalin-type prostaglandin D2 synthase protein regulates glial cell migration and morphology through myristoylated alanine-rich C-kinase substrate: Prostaglandin D2-independent effects
    • Lee, S., Jang, E., Kim, J. H., Kim, J. H., Lee, W. H., and Suk, K. (2012). Lipocalin-type prostaglandin D2 synthase protein regulates glial cell migration and morphology through myristoylated alanine-rich C-kinase substrate: prostaglandin D2-independent effects. J. Biol. Chem. 287, 9414-9428. doi: 10.1074/jbc.M111.330662
    • (2012) J. Biol. Chem , vol.287 , pp. 9414-9428
    • Lee, S.1    Jang, E.2    Kim, J.H.3    Kim, J.H.4    Lee, W.H.5    Suk, K.6
  • 107
    • 82455164113 scopus 로고    scopus 로고
    • Neurodegenerative diseases: An alternative path to reduce neuroinflammation
    • Legg, K. (2011). Neurodegenerative diseases: an alternative path to reduce neuroinflammation. Nat. Rev. Drug Discov. 10:901. doi: 10.1038/nrd3607
    • (2011) Nat. Rev. Drug Discov , vol.10 , pp. 901
    • Legg, K.1
  • 108
    • 10644230914 scopus 로고    scopus 로고
    • Neurotoxic prostaglandin J2 enhances cyclooxygenase-2 expression in neuronal cells through the p38MAPK pathway: A death wish?
    • Li, Z., Jansen, M., Ogburn, K., Salvatierra, L., Hunter, L., Mathew, S., et al. (2004a). Neurotoxic prostaglandin J2 enhances cyclooxygenase-2 expression in neuronal cells through the p38MAPK pathway: a death wish? J. Neurosci. Res. 78, 824-836. doi: 10.1002/jnr.20346
    • (2004) J. Neurosci. Res , vol.78 , pp. 824-836
    • Li, Z.1    Jansen, M.2    Ogburn, K.3    Salvatierra, L.4    Hunter, L.5    Mathew, S.6
  • 109
    • 2942575072 scopus 로고    scopus 로고
    • Delta12-Prostaglandin J2 inhibits the ubiquitin hydrolase UCH-L1 and elicits ubiquitin-protein aggregation without proteasome inhibition
    • Li, Z., Melandri, F., Berdo, I., Jansen, M., Hunter, L., Wright, S., et al. (2004b). Delta12-Prostaglandin J2 inhibits the ubiquitin hydrolase UCH-L1 and elicits ubiquitin-protein aggregation without proteasome inhibition. Biochem. Biophys. Res. Commun. 319, 1171-1180. doi: 10.1016/j.bbrc.2004.05.098
    • (2004) Biochem. Biophys. Res. Commun , vol.319 , pp. 1171-1180
    • Li, Z.1    Melandri, F.2    Berdo, I.3    Jansen, M.4    Hunter, L.5    Wright, S.6
  • 110
    • 13244262806 scopus 로고    scopus 로고
    • Prostaglandin D2 mediates neuronal protection via the DP1 receptor
    • Liang, X., Wu, L., Hand, T., and Andreasson, K. (2005). Prostaglandin D2 mediates neuronal protection via the DP1 receptor. J. Neurochem. 92, 477-486. doi: 10.1111/j.1471-4159.2004.02870.x
    • (2005) J. Neurochem , vol.92 , pp. 477-486
    • Liang, X.1    Wu, L.2    Hand, T.3    Andreasson, K.4
  • 111
    • 35348873104 scopus 로고    scopus 로고
    • Function of COX-2 and prostaglandins in neurological disease
    • Liang, X., Wu, L., Wang, Q., Hand, T., Bilak, M., McCullough, L., et al. (2007). Function of COX-2 and prostaglandins in neurological disease. J. Mol. Neurosci. 33, 94-99. doi: 10.1007/s12031-007-0058-8
    • (2007) J. Mol. Neurosci , vol.33 , pp. 94-99
    • Liang, X.1    Wu, L.2    Wang, Q.3    Hand, T.4    Bilak, M.5    McCullough, L.6
  • 113
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin, M. T., and Beal, M. F. (2006). Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases.Nature 443, 787-795. doi: 10.1038/nature05292
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 114
    • 0037677549 scopus 로고    scopus 로고
    • Parkinson's disease and exposure to infectious agents and pesticides and the occurrence of brain injuries: Role of neuroinflammation
    • Liu, B., Gao, H. M., and Hong, J. S. (2003). Parkinson's disease and exposure to infectious agents and pesticides and the occurrence of brain injuries: role of neuroinflammation. Environ. Health Perspect. 111, 1065-1073. doi: 10.1289/ehp.6361
    • (2003) Environ. Health Perspect , vol.111 , pp. 1065-1073
    • Liu, B.1    Gao, H.M.2    Hong, J.S.3
  • 115
    • 0037215645 scopus 로고    scopus 로고
    • Role of microglia in inflammation-mediated neurodegenerative diseases: Mechanisms and strategies for therapeutic intervention
    • Liu, B., and Hong, J. S. (2003). Role of microglia in inflammation-mediated neurodegenerative diseases: mechanisms and strategies for therapeutic intervention. J. Pharmacol. Exp. Ther. 304, 1-7. doi: 10.1124/jpet.102.035048
    • (2003) J. Pharmacol. Exp. Ther , vol.304 , pp. 1-7
    • Liu, B.1    Hong, J.S.2
  • 116
    • 33749069075 scopus 로고    scopus 로고
    • ATP binding and ATP hydrolysis play distinct roles in the function of 26S proteasome
    • Liu, C. W., Li, X., Thompson, D., Wooding, K., Chang, T. L., Tang, Z., et al. (2006). ATP binding and ATP hydrolysis play distinct roles in the function of 26S proteasome. Mol. Cell 24, 39-50. doi: 10.1016/j.molcel.2006.08.025
    • (2006) Mol. Cell , vol.24 , pp. 39-50
    • Liu, C.W.1    Li, X.2    Thompson, D.3    Wooding, K.4    Chang, T.L.5    Tang, Z.6
  • 117
    • 78650598280 scopus 로고    scopus 로고
    • Modification of ubiquitin-C-terminal hydrolase-L1 by cyclopentenone prostaglandins exacerbates hypoxic injury
    • Liu, H., Li, W., Ahmad, M., Miller, T. M., Rose, M. E., Poloyac, S. M., et al. (2011). Modification of ubiquitin-C-terminal hydrolase-L1 by cyclopentenone prostaglandins exacerbates hypoxic injury. Neurobiol. Dis. 41, 318-328. doi: 10.1016/j.nbd.2010.09.020
    • (2011) Neurobiol. Dis , vol.41 , pp. 318-328
    • Liu, H.1    Li, W.2    Ahmad, M.3    Miller, T.M.4    Rose, M.E.5    Poloyac, S.M.6
  • 118
    • 84879795343 scopus 로고    scopus 로고
    • Increased generation of cyclopentenone prostaglandins after brain ischemia and their role in aggregation of ubiquitinated proteins in neurons
    • Liu, H., Li, W., Ahmad, M., Rose, M. E., Miller, T. M., Yu, M., et al. (2013a). Increased generation of cyclopentenone prostaglandins after brain ischemia and their role in aggregation of ubiquitinated proteins in neurons. Neurotox. Res. 24, 191-204. doi: 10.1007/s12640-013-9377-4
    • (2013) Neurotox. Res , vol.24 , pp. 191-204
    • Liu, H.1    Li, W.2    Ahmad, M.3    Rose, M.E.4    Miller, T.M.5    Yu, M.6
  • 119
    • 84883660064 scopus 로고    scopus 로고
    • Prostaglandin D toxicity in primary neurons is mediated through its bioactive cyclopentenone metabolites
    • Liu, H., Li, W., Rose, M. E., Pascoe, J. L., Miller, T. M., Ahmad, M., et al. (2013b). Prostaglandin D toxicity in primary neurons is mediated through its bioactive cyclopentenone metabolites. Neurotoxicology 39C, 35-44. doi: 10.1016/j.neuro.2013.08.001
    • (2013) Neurotoxicology , vol.39 C , pp. 35-44
    • Liu, H.1    Li, W.2    Rose, M.E.3    Pascoe, J.L.4    Miller, T.M.5    Ahmad, M.6
  • 120
    • 84878759705 scopus 로고    scopus 로고
    • COX2-derived primary and cyclopentenone prostaglandins are increased after asphyxial cardiac arrest
    • Liu, H., Rose, M. E., Miller, T. M., Li, W., Shinde, S. N., Pickrell, A. M., et al. (2013c). COX2-derived primary and cyclopentenone prostaglandins are increased after asphyxial cardiac arrest. Brain Res. 1519, 71-77. doi: 10.1016/j.brainres.2013.04.029
    • (2013) Brain Res , vol.1519 , pp. 71-77
    • Liu, H.1    Rose, M.E.2    Miller, T.M.3    Li, W.4    Shinde, S.N.5    Pickrell, A.M.6
  • 121
    • 79151480727 scopus 로고    scopus 로고
    • Ubiquitin-proteasome system and mitochondria - reciprocity
    • Livnat-Levanon, N., and Glickman, M. H. (2011). Ubiquitin-proteasome system and mitochondria - reciprocity.Biochim. Biophys. Acta 1809, 80-87. doi: 10.1016/j.bbagrm.2010.07.005
    • (2011) Biochim. Biophys. Acta , vol.1809 , pp. 80-87
    • Livnat-Levanon, N.1    Glickman, M.H.2
  • 122
    • 0029739973 scopus 로고    scopus 로고
    • Cloning, in vitro expression, and tissue distribution of a human prostaglandin transporter cDNA(hPGT)
    • Lu, R., Kanai, N., Bao, Y., and Schuster, V. L. (1996). Cloning, in vitro expression, and tissue distribution of a human prostaglandin transporter cDNA(hPGT). J. Clin. Invest. 98, 1142-1149. doi: 10.1172/JCI118897
    • (1996) J. Clin. Invest , vol.98 , pp. 1142-1149
    • Lu, R.1    Kanai, N.2    Bao, Y.3    Schuster, V.L.4
  • 123
    • 70349807619 scopus 로고    scopus 로고
    • Immune activation in brain aging and neurodegeneration: Too much or too little?
    • Lucin, K. M., and Wyss-Coray, T. (2009). Immune activation in brain aging and neurodegeneration: too much or too little? Neuron 64, 110-122. doi: 10.1016/j.neuron.2009.08.039
    • (2009) Neuron , vol.64 , pp. 110-122
    • Lucin, K.M.1    Wyss-Coray, T.2
  • 124
    • 84863798933 scopus 로고    scopus 로고
    • Exogenous administration of PACAP alleviates traumatic brain injury in rats through a mechanism involving the TLR4/MyD88/NF-kappaB pathway
    • Mao, S. S., Hua, R., Zhao, X. P., Qin, X., Sun, Z. Q., Zhang, Y., et al. (2012). Exogenous administration of PACAP alleviates traumatic brain injury in rats through a mechanism involving the TLR4/MyD88/NF-kappaB pathway. J. Neurotrauma 29, 1941-1959. doi: 10.1089/neu.2011.2244
    • (2012) J. Neurotrauma , vol.29 , pp. 1941-1959
    • Mao, S.S.1    Hua, R.2    Zhao, X.P.3    Qin, X.4    Sun, Z.Q.5    Zhang, Y.6
  • 125
    • 84880601792 scopus 로고    scopus 로고
    • Proteomic identification of the candidate target proteins of 15-deoxy-delta12,14-prostaglandin J2
    • Marcone, S., and Fitzgerald, D. J. (2013). Proteomic identification of the candidate target proteins of 15-deoxy-delta12,14-prostaglandin J2. Proteomics 13, 2135-2139. doi: 10.1002/pmic.201200289
    • (2013) Proteomics , vol.13 , pp. 2135-2139
    • Marcone, S.1    Fitzgerald, D.J.2
  • 126
    • 21744455741 scopus 로고    scopus 로고
    • The mitochondrial respiratory complex I is a target for 15-deoxy-delta12,14-prostaglandin J2 action
    • Martinez, B., Perez-Castillo, A., and Santos, A. (2005). The mitochondrial respiratory complex I is a target for 15-deoxy-delta12,14-prostaglandin J2 action. J. Lipid Res. 46, 736-743. doi: 10.1194/jlr.M400392-JLR200
    • (2005) J. Lipid Res , vol.46 , pp. 736-743
    • Martinez, B.1    Perez-Castillo, A.2    Santos, A.3
  • 127
    • 33845991203 scopus 로고    scopus 로고
    • The 19-amino acid cassette of cyclooxygenase-2 mediates entry of the protein into the endoplasmic reticulum-associated degradation system
    • Mbonye, U. R., Wada, M., Rieke, C. J., Tang, H. Y., DeWitt, D. L., and Smith, W. L. (2006). The 19-amino acid cassette of cyclooxygenase-2 mediates entry of the protein into the endoplasmic reticulum-associated degradation system. J. Biol. Chem. 281, 35770-35778. doi: 10.1074/jbc.M608281200
    • (2006) J. Biol. Chem , vol.281 , pp. 35770-35778
    • Mbonye, U.R.1    Wada, M.2    Rieke, C.J.3    Tang, H.Y.4    DeWitt, D.L.5    Smith, W.L.6
  • 129
    • 0033583029 scopus 로고    scopus 로고
    • Peroxisome proliferators enhance cyclooxygenase-2 expression in epithelial cells
    • Meade, E. A., McIntyre, T. M., Zimmerman, G. A., and Prescott, S. M. (1999). Peroxisome proliferators enhance cyclooxygenase-2 expression in epithelial cells. J. Biol. Chem. 274, 8328-8334. doi: 10.1074/jbc.274.12.8328
    • (1999) J. Biol. Chem , vol.274 , pp. 8328-8334
    • Meade, E.A.1    McIntyre, T.M.2    Zimmerman, G.A.3    Prescott, S.M.4
  • 130
    • 84863431427 scopus 로고    scopus 로고
    • Coordination between proteasome impairment and caspase activation leading to TAU pathology: Neuroprotection by cAMP
    • Metcalfe, M. J., Huang, Q., and Figueiredo-Pereira, M. E. (2012). Coordination between proteasome impairment and caspase activation leading to TAU pathology: neuroprotection by cAMP. Cell Death Dis. 3, e326. doi: 10.1038/cddis.2012.70
    • (2012) Cell Death Dis , vol.3 , pp. e326
    • Metcalfe, M.J.1    Huang, Q.2    Figueiredo-Pereira, M.E.3
  • 131
    • 84890176335 scopus 로고    scopus 로고
    • RING-type E3 ligases: Master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination
    • Metzger, M. B., Pruneda, J. N., Klevit, R. E., and Weissman, A. M. (2014). RING-type E3 ligases: master manipulators of E2 ubiquitin-conjugating enzymes and ubiquitination. Biochim. Biophys. Acta 1843, 47-60. doi: 10.1016/j.bbamcr.2013.05.026
    • (2014) Biochim. Biophys. Acta , vol.1843 , pp. 47-60
    • Metzger, M.B.1    Pruneda, J.N.2    Klevit, R.E.3    Weissman, A.M.4
  • 132
    • 77951905953 scopus 로고    scopus 로고
    • Inhibition of mitochondrial division through covalent modification of Drp1 protein by 15 deoxy-Delta(12,14)-prostaglandin J2
    • Mishra, N., Kar, R., Singha, P. K., Venkatachalam, M. A., McEwen, D. G., and Saikumar, P. (2010). Inhibition of mitochondrial division through covalent modification of Drp1 protein by 15 deoxy-Delta(12,14)-prostaglandin J2.Biochem. Biophys. Res. Commun. 395, 17-24. doi: 10.1016/j.bbrc.2010.03.093
    • (2010) Biochem. Biophys. Res. Commun , vol.395 , pp. 17-24
    • Mishra, N.1    Kar, R.2    Singha, P.K.3    Venkatachalam, M.A.4    McEwen, D.G.5    Saikumar, P.6
  • 133
    • 34249903093 scopus 로고    scopus 로고
    • Hematopoietic prostaglandin D synthase and DP1 receptor are selectively upregulated in microglia and astrocytes within senile plaques from human patients and in a mouse model of Alzheimer disease
    • Mohri, I., Kadoyama, K., Kanekiyo, T., Sato, Y., Kagitani-Shimono, K., Saito, Y., et al. (2007). Hematopoietic prostaglandin D synthase and DP1 receptor are selectively upregulated in microglia and astrocytes within senile plaques from human patients and in a mouse model of Alzheimer disease. J. Neuropathol. Exp. Neurol. 66, 469-480. doi: 10.1097/01.jnen.0000240472.43038.27
    • (2007) J. Neuropathol. Exp. Neurol , vol.66 , pp. 469-480
    • Mohri, I.1    Kadoyama, K.2    Kanekiyo, T.3    Sato, Y.4    Kagitani-Shimono, K.5    Saito, Y.6
  • 134
    • 33646438843 scopus 로고    scopus 로고
    • Prostaglandin D2-mediated microglia/astrocyte interaction enhances astrogliosis and demyelination in twitcher
    • Mohri, I., Taniike, M., Taniguchi, H., Kanekiyo, T., Aritake, K., Inui, T., et al. (2006). Prostaglandin D2-mediated microglia/astrocyte interaction enhances astrogliosis and demyelination in twitcher. J. Neurosci. 26, 4383-4393. doi: 10.1523/JNEUROSCI.4531-05.2006
    • (2006) J. Neurosci , vol.26 , pp. 4383-4393
    • Mohri, I.1    Taniike, M.2    Taniguchi, H.3    Kanekiyo, T.4    Aritake, K.5    Inui, T.6
  • 135
    • 0036533485 scopus 로고    scopus 로고
    • 15-Deoxy-delta 12,14-prostaglandins D2 and J2 are potent activators of human eosinophils
    • Monneret, G., Li, H., Vasilescu, J., Rokach, J., and Powell, W. S. (2002). 15-Deoxy-delta 12,14-prostaglandins D2 and J2 are potent activators of human eosinophils. J. Immunol. 168, 3563-3569. doi: 10.4049/jimmunol.168.7.3563
    • (2002) J. Immunol , vol.168 , pp. 3563-3569
    • Monneret, G.1    Li, H.2    Vasilescu, J.3    Rokach, J.4    Powell, W.S.5
  • 136
    • 78650835129 scopus 로고    scopus 로고
    • VIP and PACAP: Recent insights into their functions/roles in physiology and disease from molecular and genetic studies
    • Moody, T. W., Ito, T., Osefo, N., and Jensen, R. T. (2011). VIP and PACAP: recent insights into their functions/roles in physiology and disease from molecular and genetic studies. Curr. Opin. Endocrinol. Diabetes Obes. 18, 61-67. doi: 10.1097/MED.0b013e328342568a
    • (2011) Curr. Opin. Endocrinol. Diabetes Obes , vol.18 , pp. 61-67
    • Moody, T.W.1    Ito, T.2    Osefo, N.3    Jensen, R.T.4
  • 137
    • 0037428454 scopus 로고    scopus 로고
    • Electrophilic prostaglandins and lipid aldehydes repress redox-sensitive transcription factors p53 and hypoxia-inducible factor by impairing the selenoprotein thioredoxin reductase
    • Moos, P. J., Edes, K., Cassidy, P., Massuda, E., and Fitzpatrick, F. A. (2003). Electrophilic prostaglandins and lipid aldehydes repress redox-sensitive transcription factors p53 and hypoxia-inducible factor by impairing the selenoprotein thioredoxin reductase. J. Biol. Chem. 278, 745-750. doi: 10.1074/jbc.M211134200
    • (2003) J. Biol. Chem , vol.278 , pp. 745-750
    • Moos, P.J.1    Edes, K.2    Cassidy, P.3    Massuda, E.4    Fitzpatrick, F.A.5
  • 138
    • 84874833693 scopus 로고    scopus 로고
    • Neuronal exosomal miRNA-dependent translational regulation of astroglial glutamate transporter GLT1
    • Morel, L., Regan, M., Higashimori, H., Ng, S. K., Esau, C., Vidensky, S., et al. (2013). Neuronal exosomal miRNA-dependent translational regulation of astroglial glutamate transporter GLT1. J. Biol. Chem. 288, 7105-7116. doi: 10.1074/jbc.M112.410944
    • (2013) J. Biol. Chem , vol.288 , pp. 7105-7116
    • Morel, L.1    Regan, M.2    Higashimori, H.3    Ng, S.K.4    Esau, C.5    Vidensky, S.6
  • 139
    • 84897954445 scopus 로고    scopus 로고
    • Microglial dysfunction in brain aging and Alzheimer's disease
    • Mosher, K. I., and Wyss-Coray, T. (2014). Microglial dysfunction in brain aging and Alzheimer's disease. Biochem. Pharmacol. 88, 594-604. doi: 10.1016/j.bcp.2014.01.008
    • (2014) Biochem. Pharmacol , vol.88 , pp. 594-604
    • Mosher, K.I.1    Wyss-Coray, T.2
  • 140
    • 4344575026 scopus 로고    scopus 로고
    • PPARgamma, neuroinflammation, and disease
    • Mrak, R. E., and Landreth, G. E. (2004). PPARgamma, neuroinflammation, and disease. J. Neuroinflammation 1:5. doi: 10.1186/1742-2094-1-5
    • (2004) J. Neuroinflammation , vol.1 , pp. 5
    • Mrak, R.E.1    Landreth, G.E.2
  • 141
    • 0035839603 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandins of the J series inhibit the ubiquitin isopeptidase activity of the proteasome pathway
    • Mullally, J. E., Moos, P. J., Edes, K., and Fitzpatrick, F. A. (2001). Cyclopentenone prostaglandins of the J series inhibit the ubiquitin isopeptidase activity of the proteasome pathway. J. Biol. Chem. 276, 30366-30373. doi: 10.1074/jbc.M102198200
    • (2001) J. Biol. Chem , vol.276 , pp. 30366-30373
    • Mullally, J.E.1    Moos, P.J.2    Edes, K.3    Fitzpatrick, F.A.4
  • 142
    • 0022557575 scopus 로고
    • Release of prostaglandin D2 into human airways during acute antigen challenge
    • Murray, J. J., Tonnel, A. B., Brash, A. R., Roberts, L. J., Gosset, P., Workman, R., et al. (1986). Release of prostaglandin D2 into human airways during acute antigen challenge. N. Engl. J. Med. 315, 800-804. doi: 10.1056/NEJM198609253151304
    • (1986) N. Engl. J. Med , vol.315 , pp. 800-804
    • Murray, J.J.1    Tonnel, A.B.2    Brash, A.R.3    Roberts, L.J.4    Gosset, P.5    Workman, R.6
  • 143
    • 17444386729 scopus 로고    scopus 로고
    • Cyclopentenone eicosanoids as mediators of neurodegeneration: A pathogenic mechanism of oxidative stress-mediated and cyclooxygenase-mediated neurotoxicity
    • Musiek, E. S., Milne, G. L., McLaughlin, B., and Morrow, J. D. (2005). Cyclopentenone eicosanoids as mediators of neurodegeneration: a pathogenic mechanism of oxidative stress-mediated and cyclooxygenase-mediated neurotoxicity. Brain Pathol. 15, 149-158. doi: 10.1111/j.1750-3639.2005.tb00512.x
    • (2005) Brain Pathol , vol.15 , pp. 149-158
    • Musiek, E.S.1    Milne, G.L.2    McLaughlin, B.3    Morrow, J.D.4
  • 144
    • 0142144332 scopus 로고    scopus 로고
    • Peroxisome proliferator-activated receptor gamma (PPARgamma) ligands as bifunctional regulators of cell proliferation
    • Na, H. K., and Surh, Y. J. (2003). Peroxisome proliferator-activated receptor gamma (PPARgamma) ligands as bifunctional regulators of cell proliferation. Biochem. Pharmacol. 66, 1381-1391. doi: 10.1016/S0006-2952(03)00488-X
    • (2003) Biochem. Pharmacol , vol.66 , pp. 1381-1391
    • Na, H.K.1    Surh, Y.J.2
  • 145
    • 33748323449 scopus 로고    scopus 로고
    • 15-Deoxy-Delta12,14-prostaglandin J(2) induces death receptor 5 expression through mRNA stabilization independently of PPARgamma and potentiates TRAIL-induced apoptosis
    • Nakata, S., Yoshida, T., Shiraishi, T., Horinaka, M., Kouhara, J., Wakada, M., et al. (2006). 15-Deoxy-Delta12,14-prostaglandin J(2) induces death receptor 5 expression through mRNA stabilization independently of PPARgamma and potentiates TRAIL-induced apoptosis. Mol. Cancer Ther. 5, 1827-1835. doi: 10.1158/1535-7163.MCT-06-0023
    • (2006) Mol. Cancer Ther , vol.5 , pp. 1827-1835
    • Nakata, S.1    Yoshida, T.2    Shiraishi, T.3    Horinaka, M.4    Kouhara, J.5    Wakada, M.6
  • 146
    • 79954577302 scopus 로고    scopus 로고
    • Targeting mitochondrial dysfunction: Role for PINK1 and Parkin in mitochondrial quality control
    • Narendra, D. P., and Youle, R. J. (2011). Targeting mitochondrial dysfunction: role for PINK1 and Parkin in mitochondrial quality control. Antioxid. Redox. Signal. 14, 1929-1938. doi: 10.1089/ars.2010.3799
    • (2011) Antioxid. Redox. Signal , vol.14 , pp. 1929-1938
    • Narendra, D.P.1    Youle, R.J.2
  • 147
    • 0020333851 scopus 로고
    • Prostaglandin D2 in rat brain, spinal cord and pituitary: Basal level and regional distribution
    • Narumiya, S., Ogorochi, T., Nakao, K., and Hayaishi, O. (1982). Prostaglandin D2 in rat brain, spinal cord and pituitary: basal level and regional distribution. Life Sci. 31, 2093-2103. doi: 10.1016/0024-3205(82)90101-1
    • (1982) Life Sci , vol.31 , pp. 2093-2103
    • Narumiya, S.1    Ogorochi, T.2    Nakao, K.3    Hayaishi, O.4
  • 148
    • 77958484639 scopus 로고    scopus 로고
    • NSAID-induced gastrointestinal and cardiovascular injury
    • Ng, S. C., and Chan, F. K. (2010). NSAID-induced gastrointestinal and cardiovascular injury. Curr. Opin. Gastroenterol. 26, 611-617. doi: 10.1097/MOG.0b013e32833e91eb
    • (2010) Curr. Opin. Gastroenterol , vol.26 , pp. 611-617
    • Ng, S.C.1    Chan, F.K.2
  • 149
    • 57649178442 scopus 로고    scopus 로고
    • Oxidative stress and energy crises in neuronal dysfunction
    • Nicholls, D. G. (2008). Oxidative stress and energy crises in neuronal dysfunction. Ann. N. Y. Acad. Sci. 1147, 53-60. doi: 10.1196/annals.1427.002
    • (2008) Ann. N. Y. Acad. Sci , vol.1147 , pp. 53-60
    • Nicholls, D.G.1
  • 150
    • 84875243183 scopus 로고    scopus 로고
    • Parkinson's disease in the nuclear age of neuroinflammation
    • Nolan, Y. M., Sullivan, A. M., and Toulouse, A. (2013). Parkinson's disease in the nuclear age of neuroinflammation.Trends Mol. Med. 19, 187-196. doi: 10.1016/j.molmed.2012.12.003
    • (2013) Trends Mol. Med , vol.19 , pp. 187-196
    • Nolan, Y.M.1    Sullivan, A.M.2    Toulouse, A.3
  • 151
    • 81055156684 scopus 로고    scopus 로고
    • Endocannabinoid hydrolysis generates brain prostaglandins that promote neuroinflammation
    • Nomura, D. K., Morrison, B. E., Blankman, J. L., Long, J. Z., Kinsey, S. G., Marcondes, M. C., et al. (2011). Endocannabinoid hydrolysis generates brain prostaglandins that promote neuroinflammation. Science 334, 809-813. doi: 10.1126/science.1209200
    • (2011) Science , vol.334 , pp. 809-813
    • Nomura, D.K.1    Morrison, B.E.2    Blankman, J.L.3    Long, J.Z.4    Kinsey, S.G.5    Marcondes, M.C.6
  • 152
    • 1842532964 scopus 로고    scopus 로고
    • The two-step model of prostaglandin signal termination: in vitro reconstitution with the prostaglandin transporter and prostaglandin 15 dehydrogenase
    • Nomura, T., Lu, R., Pucci, M. L., and Schuster, V. L. (2004). The two-step model of prostaglandin signal termination: in vitro reconstitution with the prostaglandin transporter and prostaglandin 15 dehydrogenase. Mol. Pharmacol. 65, 973-978. doi: 10.1124/mol.65.4.973
    • (2004) Mol. Pharmacol , vol.65 , pp. 973-978
    • Nomura, T.1    Lu, R.2    Pucci, M.L.3    Schuster, V.L.4
  • 153
    • 84889841360 scopus 로고    scopus 로고
    • Update on the status of DP2 receptor antagonists; from proof of concept through clinical failures to promising new drugs
    • Norman, P. (2014). Update on the status of DP2 receptor antagonists; from proof of concept through clinical failures to promising new drugs. Expert Opin. Investig. Drugs 23, 55-66. doi: 10.1517/13543784.2013.839658
    • (2014) Expert Opin. Investig. Drugs , vol.23 , pp. 55-66
    • Norman, P.1
  • 154
    • 42349089604 scopus 로고    scopus 로고
    • The ubiquitin-proteasome system in Alzheimer's disease
    • Oddo, S. (2008). The ubiquitin-proteasome system in Alzheimer's disease. J. Cell Mol. Med. 12, 363-373. doi: 10.1111/j.1582-4934.2008.00276.x
    • (2008) J. Cell Mol. Med , vol.12 , pp. 363-373
    • Oddo, S.1
  • 155
    • 84893766780 scopus 로고    scopus 로고
    • Modification of cysteine residues by cyclopentenone prostaglandins: Interplay with redox regulation of protein function
    • Oeste, C. L., and Perez-Sala, D. (2014). Modification of cysteine residues by cyclopentenone prostaglandins: interplay with redox regulation of protein function. Mass Spectrom. Rev. 33, 110-125. doi: 10.1002/mas.21383
    • (2014) Mass Spectrom. Rev , vol.33 , pp. 110-125
    • Oeste, C.L.1    Perez-Sala, D.2
  • 156
    • 0022602693 scopus 로고
    • The use of crevicular fluid prostaglandin E2 levels as a predictor of periodontal attachment loss
    • Offenbacher, S., Odle, B. M., and Van Dyke, T. E. (1986). The use of crevicular fluid prostaglandin E2 levels as a predictor of periodontal attachment loss. J. Periodontal. Res. 21, 101-112. doi: 10.1111/j.1600-0765.1986.tb01443.x
    • (1986) J. Periodontal. Res , vol.21 , pp. 101-112
    • Offenbacher, S.1    Odle, B.M.2    Van Dyke, T.E.3
  • 157
    • 33747368700 scopus 로고    scopus 로고
    • Cytoskeleton/endoplasmic reticulum collapse induced by prostaglandin J2 parallels centrosomal deposition of ubiquitinated protein aggregates
    • Ogburn, K. D., and Figueiredo-Pereira, M. E. (2006). Cytoskeleton/endoplasmic reticulum collapse induced by prostaglandin J2 parallels centrosomal deposition of ubiquitinated protein aggregates. J. Biol. Chem. 281, 23274-23284. doi: 10.1074/jbc.M600635200
    • (2006) J. Biol. Chem , vol.281 , pp. 23274-23284
    • Ogburn, K.D.1    Figueiredo-Pereira, M.E.2
  • 158
    • 0021269319 scopus 로고
    • Regional distribution of prostaglandins D2, E2, and F2 alpha and related enzymes in postmortem human brain
    • Ogorochi, T., Narumiya, S., Mizuno, N., Yamashita, K., Miyazaki, H., and Hayaishi, O. (1984). Regional distribution of prostaglandins D2, E2, and F2 alpha and related enzymes in postmortem human brain. J. Neurochem. 43, 71-82. doi: 10.1111/j.1471-4159.1984.tb06680.x
    • (1984) J. Neurochem , vol.43 , pp. 71-82
    • Ogorochi, T.1    Narumiya, S.2    Mizuno, N.3    Yamashita, K.4    Miyazaki, H.5    Hayaishi, O.6
  • 159
    • 84905240283 scopus 로고    scopus 로고
    • Prostaglandin transporting protein-mediated prostaglandin E2 transport in lipopolysaccharide-inflamed rat dental pulp
    • Ohkura, N., Shigetani, Y., Yoshiba, N., Yoshiba, K., and Okiji, T. (2014). Prostaglandin transporting protein-mediated prostaglandin E2 transport in lipopolysaccharide-inflamed rat dental pulp. J. Endod. 40, 1112-1117. doi: 10.1016/j.joen.2013.12.024
    • (2014) J. Endod , vol.40 , pp. 1112-1117
    • Ohkura, N.1    Shigetani, Y.2    Yoshiba, N.3    Yoshiba, K.4    Okiji, T.5
  • 160
    • 78349307902 scopus 로고    scopus 로고
    • Regulation of oxidative stress by pituitary adenylate cyclase-activating polypeptide (PACAP) mediated by PACAP receptor
    • Ohtaki, H., Satoh, A., Nakamachi, T., Yofu, S., Dohi, K., Mori, H., et al. (2010). Regulation of oxidative stress by pituitary adenylate cyclase-activating polypeptide (PACAP) mediated by PACAP receptor. J. Mol. Neurosci. 42, 397-403. doi: 10.1007/s12031-010-9350-0
    • (2010) J. Mol. Neurosci , vol.42 , pp. 397-403
    • Ohtaki, H.1    Satoh, A.2    Nakamachi, T.3    Yofu, S.4    Dohi, K.5    Mori, H.6
  • 161
    • 0344987879 scopus 로고    scopus 로고
    • The cyclopentenone 15-deoxy-delta 12,14-prostaglandin J2 binds to and activates H-Ras
    • Oliva, J. L., Perez-Sala, D., Castrillo, A., Martinez, N., Canada, F. J., Bosca, L., et al. (2003). The cyclopentenone 15-deoxy-delta 12,14-prostaglandin J2 binds to and activates H-Ras. Proc. Natl. Acad. Sci. U.S.A. 100, 4772-4777. doi: 10.1073/pnas.0735842100
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 4772-4777
    • Oliva, J.L.1    Perez-Sala, D.2    Castrillo, A.3    Martinez, N.4    Canada, F.J.5    Bosca, L.6
  • 162
    • 84886948548 scopus 로고    scopus 로고
    • Alterations of brain eicosanoid synthetic pathway in multiple sclerosis and in animal models of demyelination: Role of cyclooxygenase-2
    • Palumbo, S., and Bosetti, F. (2013). Alterations of brain eicosanoid synthetic pathway in multiple sclerosis and in animal models of demyelination: role of cyclooxygenase-2. Prostaglandins Leukot. Essent. Fatty Acids 89, 273-278. doi: 10.1016/j.plefa.2013.08.008
    • (2013) Prostaglandins Leukot. Essent. Fatty Acids , vol.89 , pp. 273-278
    • Palumbo, S.1    Bosetti, F.2
  • 163
    • 58149159907 scopus 로고    scopus 로고
    • Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: Therapeutic approaches
    • Paul, S. (2008). Dysfunction of the ubiquitin-proteasome system in multiple disease conditions: therapeutic approaches. Bioessays 30, 1172-1184. doi: 10.1002/bies.20852
    • (2008) Bioessays , vol.30 , pp. 1172-1184
    • Paul, S.1
  • 164
    • 84866702312 scopus 로고    scopus 로고
    • Proteome analysis identified the PPARgamma ligand 15d-PGJ2 as a novel drug inhibiting melanoma progression and interfering with tumor-stroma interaction
    • Paulitschke, V., Gruber, S., Hofstatter, E., Haudek-Prinz, V., Klepeisz, P., Schicher, N., et al. (2012). Proteome analysis identified the PPARgamma ligand 15d-PGJ2 as a novel drug inhibiting melanoma progression and interfering with tumor-stroma interaction. PLoS ONE 7:e46103. doi: 10.1371/journal.pone.0046103
    • (2012) PLoS ONE , vol.7
    • Paulitschke, V.1    Gruber, S.2    Hofstatter, E.3    Haudek-Prinz, V.4    Klepeisz, P.5    Schicher, N.6
  • 165
    • 84871118236 scopus 로고    scopus 로고
    • The exosome secretory pathway transports amyloid precursor protein carboxyl-terminal fragments from the cell into the brain extracellular space
    • Perez-Gonzalez, R., Gauthier, S. A., Kumar, A., and Levy, E. (2012). The exosome secretory pathway transports amyloid precursor protein carboxyl-terminal fragments from the cell into the brain extracellular space. J. Biol. Chem. 287, 43108-43115. doi: 10.1074/jbc.M112.404467
    • (2012) J. Biol. Chem , vol.287 , pp. 43108-43115
    • Perez-Gonzalez, R.1    Gauthier, S.A.2    Kumar, A.3    Levy, E.4
  • 166
    • 33947726053 scopus 로고    scopus 로고
    • Antagonism of the prostaglandin D2 receptors DP1 and CRTH2 as an approach to treat allergic diseases
    • Pettipher, R., Hansel, T. T., and Armer, R. (2007). Antagonism of the prostaglandin D2 receptors DP1 and CRTH2 as an approach to treat allergic diseases. Nat. Rev. Drug Discov. 6, 313-325. doi: 10.1038/nrd2266
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 313-325
    • Pettipher, R.1    Hansel, T.T.2    Armer, R.3
  • 167
    • 68949213095 scopus 로고    scopus 로고
    • Subchronic infusion of the product of inflammation prostaglandin J2 models sporadic Parkinson's disease in mice
    • Pierre, S. R., Lemmens, M. A., and Figueiredo-Pereira, M. E. (2009). Subchronic infusion of the product of inflammation prostaglandin J2 models sporadic Parkinson's disease in mice. J. Neuroinflammation 6:18. doi: 10.1186/1742-2094-6-18
    • (2009) J. Neuroinflammation , vol.6 , pp. 18
    • Pierre, S.R.1    Lemmens, M.A.2    Figueiredo-Pereira, M.E.3
  • 168
    • 13444292545 scopus 로고    scopus 로고
    • 15-Deoxy-{Delta}-12,14-prostaglandin J2 induces programmed cell death of breast cancer cells by a pleiotropic mechanism
    • Pignatelli, M., Sanchez-Rodriguez, J., Santos, A., and Perez-Castillo, A. (2005). 15-Deoxy-{Delta}-12,14-prostaglandin J2 induces programmed cell death of breast cancer cells by a pleiotropic mechanism. Carcinogenesis26, 81-92. doi: 10.1093/carcin/bgh308
    • (2005) Carcinogenesis , vol.26 , pp. 81-92
    • Pignatelli, M.1    Sanchez-Rodriguez, J.2    Santos, A.3    Perez-Castillo, A.4
  • 169
    • 84863103124 scopus 로고    scopus 로고
    • A dysregulated endocannabinoid-eicosanoid network supports pathogenesis in a mouse model of Alzheimer's disease
    • Piro, J. R., Benjamin, D. I., Duerr, J. M., Pi, Y., Gonzales, C., Wood, K. M., et al. (2012). A dysregulated endocannabinoid-eicosanoid network supports pathogenesis in a mouse model of Alzheimer's disease. Cell Rep. 1, 617-623. doi: 10.1016/j.celrep.2012.05.001
    • (2012) Cell Rep , vol.1 , pp. 617-623
    • Piro, J.R.1    Benjamin, D.I.2    Duerr, J.M.3    Pi, Y.4    Gonzales, C.5    Wood, K.M.6
  • 170
    • 78649738973 scopus 로고    scopus 로고
    • Peroxisome proliferator activated receptor-gamma and traumatic brain injury
    • Qi, L., Jacob, A., Wang, P., and Wu, R. (2010). Peroxisome proliferator activated receptor-gamma and traumatic brain injury. Int. J. Clin. Exp. Med. 3, 283-292.
    • (2010) Int. J. Clin. Exp. Med , vol.3 , pp. 283-292
    • Qi, L.1    Jacob, A.2    Wang, P.3    Wu, R.4
  • 171
    • 34547598278 scopus 로고    scopus 로고
    • Anti-inflammatory drugs in the 21st century
    • Rainsford, K. D. (2007). Anti-inflammatory drugs in the 21st century. Subcell. Biochem. 42, 3-27. doi: 10.1007/1-4020-5688-5_1
    • (2007) Subcell. Biochem , vol.42 , pp. 3-27
    • Rainsford, K.D.1
  • 172
    • 38049181031 scopus 로고    scopus 로고
    • Hematopoietic prostaglandin D2 synthase controls the onset and resolution of acute inflammation through PGD2 and 15-deoxyDelta12 14 PGJ2
    • Rajakariar, R., Hilliard, M., Lawrence, T., Trivedi, S., Colville-Nash, P., Bellingan, G., et al. (2007). Hematopoietic prostaglandin D2 synthase controls the onset and resolution of acute inflammation through PGD2 and 15-deoxyDelta12 14 PGJ2. Proc. Natl. Acad. Sci. U.S.A. 104, 20979-20984. doi: 10.1073/pnas.0707394104
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 20979-20984
    • Rajakariar, R.1    Hilliard, M.2    Lawrence, T.3    Trivedi, S.4    Colville-Nash, P.5    Bellingan, G.6
  • 173
    • 4444355926 scopus 로고    scopus 로고
    • Pituitary adenylate cyclase activating polypeptide protects dopaminergic neurons and improves behavioral deficits in a rat model of Parkinson's disease
    • Reglodi, D., Lubics, A., Tamas, A., Szalontay, L., and Lengvari, I. (2004). Pituitary adenylate cyclase activating polypeptide protects dopaminergic neurons and improves behavioral deficits in a rat model of Parkinson's disease.Behav. Brain Res. 151, 303-312. doi: 10.1016/j.bbr.2003.09.007
    • (2004) Behav. Brain Res , vol.151 , pp. 303-312
    • Reglodi, D.1    Lubics, A.2    Tamas, A.3    Szalontay, L.4    Lengvari, I.5
  • 175
    • 3242749074 scopus 로고    scopus 로고
    • Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology
    • Rissman, R. A., Poon, W. W., Blurton-Jones, M., Oddo, S., Torp, R., Vitek, M. P., et al. (2004). Caspase-cleavage of tau is an early event in Alzheimer disease tangle pathology. J. Clin. Invest. 114, 121-130. doi: 10.1172/JCI200420640
    • (2004) J. Clin. Invest , vol.114 , pp. 121-130
    • Rissman, R.A.1    Poon, W.W.2    Blurton-Jones, M.3    Oddo, S.4    Torp, R.5    Vitek, M.P.6
  • 176
    • 84920999733 scopus 로고    scopus 로고
    • An optimal ubiquitin-proteasome pathway in the nervous system: The role of deubiquitinating enzymes
    • Ristic, G., Tsou, W. L., and Todi, S. V. (2014). An optimal ubiquitin-proteasome pathway in the nervous system: the role of deubiquitinating enzymes. Front. Mol. Neurosci. 7:72. doi: 10.3389/fnmol.2014.00072
    • (2014) Front. Mol. Neurosci , vol.7 , pp. 72
    • Ristic, G.1    Tsou, W.L.2    Todi, S.V.3
  • 177
    • 0034652238 scopus 로고    scopus 로고
    • Proteasome inhibition in neuronal cells induces a proinflammatory response manifested by upregulation of cyclooxygenase-2, its accumulation as ubiquitin conjugates, and production of the prostaglandin PGE2
    • Rockwell, P., Yuan, H. M., Magnusson, R., and Figueiredo-Pereira, M. E. (2000). Proteasome inhibition in neuronal cells induces a proinflammatory response manifested by upregulation of cyclooxygenase-2, its accumulation as ubiquitin conjugates, and production of the prostaglandin PGE2. Arch. Biochem. Biophys. 374, 325-333. doi: 10.1006/abbi.1999.1646
    • (2000) Arch. Biochem. Biophys , vol.374 , pp. 325-333
    • Rockwell, P.1    Yuan, H.M.2    Magnusson, R.3    Figueiredo-Pereira, M.E.4
  • 178
    • 84873420568 scopus 로고    scopus 로고
    • Loss of substance P and inflammation precede delayed neurodegeneration in the substantia nigra after cerebral ischemia
    • Rodriguez-Grande, B., Blackabey, V., Gittens, B., Pinteaux, E., and Denes, A. (2013). Loss of substance P and inflammation precede delayed neurodegeneration in the substantia nigra after cerebral ischemia. Brain Behav. Immun. 29, 51-61. doi: 10.1016/j.bbi.2012.11.017
    • (2013) Brain Behav. Immun , vol.29 , pp. 51-61
    • Rodriguez-Grande, B.1    Blackabey, V.2    Gittens, B.3    Pinteaux, E.4    Denes, A.5
  • 179
    • 0034610759 scopus 로고    scopus 로고
    • Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase
    • Rossi, A., Kapahi, P., Natoli, G., Takahashi, T., Chen, Y., Karin, M., et al. (2000). Anti-inflammatory cyclopentenone prostaglandins are direct inhibitors of IkappaB kinase. Nature 403, 103-108. doi: 10.1038/47520
    • (2000) Nature , vol.403 , pp. 103-108
    • Rossi, A.1    Kapahi, P.2    Natoli, G.3    Takahashi, T.4    Chen, Y.5    Karin, M.6
  • 180
    • 33846687384 scopus 로고    scopus 로고
    • Contrary prostaglandins: The opposing roles of PGD2 and its metabolites in leukocyte function
    • Sandig, H., Pease, J. E., and Sabroe, I. (2007). Contrary prostaglandins: the opposing roles of PGD2 and its metabolites in leukocyte function. J. Leukoc. Biol. 81, 372-382. doi: 10.1189/jlb.0706424
    • (2007) J. Leukoc. Biol , vol.81 , pp. 372-382
    • Sandig, H.1    Pease, J.E.2    Sabroe, I.3
  • 181
    • 33845648094 scopus 로고    scopus 로고
    • Redox regulation of neuronal survival mediated by electrophilic compounds
    • Satoh, T., and Lipton, S. A. (2007). Redox regulation of neuronal survival mediated by electrophilic compounds.Trends Neurosci. 30, 37-45. doi: 10.1016/j.tins.2006.11.004
    • (2007) Trends Neurosci , vol.30 , pp. 37-45
    • Satoh, T.1    Lipton, S.A.2
  • 182
    • 11444261543 scopus 로고    scopus 로고
    • 15d-PGJ2: The anti-inflammatory prostaglandin?
    • Scher, J. U., and Pillinger, M. H. (2005). 15d-PGJ2: the anti-inflammatory prostaglandin? Clin. Immunol. 114, 100-109. doi: 10.1016/j.clim.2004.09.008
    • (2005) Clin. Immunol , vol.114 , pp. 100-109
    • Scher, J.U.1    Pillinger, M.H.2
  • 183
    • 70349263442 scopus 로고    scopus 로고
    • The anti-inflammatory effects of prostaglandins
    • Scher, J. U., and Pillinger, M. H. (2009). The anti-inflammatory effects of prostaglandins. J. Investig. Med. 57, 703-708. doi: 10.231/JIM.0b013e31819aaa76
    • (2009) J. Investig. Med , vol.57 , pp. 703-708
    • Scher, J.U.1    Pillinger, M.H.2
  • 184
    • 84875234646 scopus 로고    scopus 로고
    • Exosomes: Vesicular carriers for intercellular communication in neurodegenerative disorders
    • Schneider, A., and Simons, M. (2013). Exosomes: vesicular carriers for intercellular communication in neurodegenerative disorders. Cell Tissue Res. 352, 33-47. doi: 10.1007/s00441-012-1428-2
    • (2013) Cell Tissue Res , vol.352 , pp. 33-47
    • Schneider, A.1    Simons, M.2
  • 185
    • 67349256160 scopus 로고    scopus 로고
    • Ubiquitin-like protein activation by E1 enzymes: The apex for downstream signalling pathways
    • Schulman, B. A., and Harper, J. W. (2009). Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways. Nat. Rev. Mol. Cell Biol. 10, 319-331. doi: 10.1038/nrm2673
    • (2009) Nat. Rev. Mol. Cell Biol , vol.10 , pp. 319-331
    • Schulman, B.A.1    Harper, J.W.2
  • 186
    • 0031919154 scopus 로고    scopus 로고
    • Molecular mechanisms of prostaglandin transport
    • Schuster, V. L. (1998). Molecular mechanisms of prostaglandin transport. Annu. Rev. Physiol. 60, 221-242. doi: 10.1146/annurev.physiol.60.1.221
    • (1998) Annu. Rev. Physiol , vol.60 , pp. 221-242
    • Schuster, V.L.1
  • 187
    • 0036669441 scopus 로고    scopus 로고
    • Prostaglandin transport
    • Schuster, V. L. (2002). Prostaglandin transport. Prostaglandins Other Lipid Mediat. 68-69, 633-647. doi: 10.1016/S0090-6980(02)00061-8
    • (2002) Prostaglandins Other Lipid Mediat , vol.69-69 , pp. 633-647
    • Schuster, V.L.1
  • 188
    • 47849127085 scopus 로고    scopus 로고
    • Inflammatory aspects of Alzheimer disease and other neurodegenerative disorders
    • Schwab, C., and McGeer, P. L. (2008). Inflammatory aspects of Alzheimer disease and other neurodegenerative disorders. J. Alzheimers. Dis. 13, 359-369.
    • (2008) J. Alzheimers. Dis , vol.13 , pp. 359-369
    • Schwab, C.1    McGeer, P.L.2
  • 189
    • 7944233158 scopus 로고    scopus 로고
    • Cell biology of protein misfolding: The examples of Alzheimer's and Parkinson's diseases
    • Selkoe, D. J. (2004). Cell biology of protein misfolding: the examples of Alzheimer's and Parkinson's diseases. Nat. Cell Biol. 6, 1054-1061. doi: 10.1038/ncb1104-1054
    • (2004) Nat. Cell Biol , vol.6 , pp. 1054-1061
    • Selkoe, D.J.1
  • 190
    • 4043127497 scopus 로고    scopus 로고
    • The cellular response to PPARgamma ligands is related to the phenotype of neuroblastoma cell lines
    • Servidei, T., Morosetti, R., Ferlini, C., Cusano, G., Scambia, G., Mastrangelo, R., et al. (2004). The cellular response to PPARgamma ligands is related to the phenotype of neuroblastoma cell lines. Oncol. Res. 14, 345-354.
    • (2004) Oncol. Res , vol.14 , pp. 345-354
    • Servidei, T.1    Morosetti, R.2    Ferlini, C.3    Cusano, G.4    Scambia, G.5    Mastrangelo, R.6
  • 192
    • 84862297456 scopus 로고    scopus 로고
    • The emerging role of proteolysis in mitochondrial quality control and the etiology of Parkinson's disease
    • Shanbhag, R., Shi, G., Rujiviphat, J., and McQuibban, G. A. (2012). The emerging role of proteolysis in mitochondrial quality control and the etiology of Parkinson's disease. Parkinsons Dis. 2012, 382175. doi: 10.1155/2012/382175
    • (2012) Parkinsons Dis , vol.2012
    • Shanbhag, R.1    Shi, G.2    Rujiviphat, J.3    McQuibban, G.A.4
  • 193
    • 33947729229 scopus 로고    scopus 로고
    • Biomarkers of neurodegeneration for diagnosis and monitoring therapeutics
    • Shaw, L. M., Korecka, M., Clark, C. M., Lee, V. M., and Trojanowski, J. Q. (2007). Biomarkers of neurodegeneration for diagnosis and monitoring therapeutics. Nat. Rev. Drug Discov. 6, 295-303. doi: 10.1038/nrd2176
    • (2007) Nat. Rev. Drug Discov , vol.6 , pp. 295-303
    • Shaw, L.M.1    Korecka, M.2    Clark, C.M.3    Lee, V.M.4    Trojanowski, J.Q.5
  • 194
    • 0037155868 scopus 로고    scopus 로고
    • 15-deoxy-delta 12,14-prostaglandin J2. A prostaglandin D2 metabolite generated during inflammatory processes
    • Shibata, T., Kondo, M., Osawa, T., Shibata, N., Kobayashi, M., and Uchida, K. (2002). 15-deoxy-delta 12,14-prostaglandin J2. A prostaglandin D2 metabolite generated during inflammatory processes. J. Biol. Chem. 277, 10459-10466. doi: 10.1074/jbc.M110314200
    • (2002) J. Biol. Chem , vol.277 , pp. 10459-10466
    • Shibata, T.1    Kondo, M.2    Osawa, T.3    Shibata, N.4    Kobayashi, M.5    Uchida, K.6
  • 195
    • 0345707597 scopus 로고    scopus 로고
    • An endogenous electrophile that modulates the regulatory mechanism of protein turnover: Inhibitory effects of 15-deoxy-delta(12,14)-prostaglandin J2 on proteasome
    • Shibata, T., Yamada, T., Kondo, M., Tanahashi, N., Tanaka, K., Nakamura, H., et al. (2003). An endogenous electrophile that modulates the regulatory mechanism of protein turnover: inhibitory effects of 15-deoxy-delta(12,14)-prostaglandin J2 on proteasome. Biochemistry 42, 13960-13968. doi: 10.1021/bi035215a
    • (2003) Biochemistry , vol.42 , pp. 13960-13968
    • Shibata, T.1    Yamada, T.2    Kondo, M.3    Tanahashi, N.4    Tanaka, K.5    Nakamura, H.6
  • 196
    • 39849109063 scopus 로고    scopus 로고
    • Ser515 phosphorylation-independent regulation of cytosolic phospholipase A2alpha (cPLA2alpha) by calmodulin-dependent protein kinase: Possible interaction with catalytic domain A of cPLA2alpha
    • Shimizu, M., Nakamura, H., Hirabayashi, T., Suganami, A., Tamura, Y., and Murayama, T. (2008). Ser515 phosphorylation-independent regulation of cytosolic phospholipase A2alpha (cPLA2alpha) by calmodulin-dependent protein kinase: possible interaction with catalytic domain A of cPLA2alpha. Cell Signal. 20, 815-824. doi: 10.1016/j.cellsig.2007.12.016
    • (2008) Cell Signal , vol.20 , pp. 815-824
    • Shimizu, M.1    Nakamura, H.2    Hirabayashi, T.3    Suganami, A.4    Tamura, Y.5    Murayama, T.6
  • 197
    • 84904089007 scopus 로고    scopus 로고
    • PACAP27 prevents Parkinson-like neuronal loss and motor deficits but not microglia activation induced by prostaglandin J2
    • Shivers, K. Y., Nikolopoulou, A., Machlovi, S. I., Vallabhajosula, S., and Figueiredo-Pereira, M. E. (2014). PACAP27 prevents Parkinson-like neuronal loss and motor deficits but not microglia activation induced by prostaglandin J2.Biochim. Biophys. Acta 1842, 1707-1719. doi: 10.1016/j.bbadis.2014.06.020
    • (2014) Biochim. Biophys. Acta , vol.1842 , pp. 1707-1719
    • Shivers, K.Y.1    Nikolopoulou, A.2    McHlovi, S.I.3    Vallabhajosula, S.4    Figueiredo-Pereira, M.E.5
  • 198
    • 4143107932 scopus 로고    scopus 로고
    • Cyclooxygenase isozymes: The biology of prostaglandin synthesis and inhibition
    • Simmons, D. L., Botting, R. M., and Hla, T. (2004). Cyclooxygenase isozymes: the biology of prostaglandin synthesis and inhibition. Pharmacol. Rev. 56, 387-437. doi: 10.1124/pr.56.3.3
    • (2004) Pharmacol. Rev , vol.56 , pp. 387-437
    • Simmons, D.L.1    Botting, R.M.2    Hla, T.3
  • 199
    • 0033791318 scopus 로고    scopus 로고
    • Cyclooxygenases: Structural, cellular, and molecular biology
    • Smith, W. L., DeWitt, D. L., and Garavito, R. M. (2000). Cyclooxygenases: structural, cellular, and molecular biology. Annu. Rev. Biochem. 69, 145-182. doi: 10.1146/annurev.biochem.69.1.145
    • (2000) Annu. Rev. Biochem , vol.69 , pp. 145-182
    • Smith, W.L.1    DeWitt, D.L.2    Garavito, R.M.3
  • 200
    • 66349102248 scopus 로고    scopus 로고
    • Prostanoids in health and disease
    • Smyth, E. M., Grosser, T., Wang, M., Yu, Y., and FitzGerald, G. A. (2009). Prostanoids in health and disease. J. Lipid Res. 50(Suppl.), S423-S428. doi: 10.1194/jlr.R800094-JLR200
    • (2009) J. Lipid Res , vol.50 , pp. S423-S428
    • Smyth, E.M.1    Grosser, T.2    Wang, M.3    Yu, Y.4    FitzGerald, G.A.5
  • 201
    • 33645459848 scopus 로고    scopus 로고
    • Identification of novel protein targets for modification by 15-deoxy-Delta12,14-prostaglandin J2 in mesangial cells reveals multiple interactions with the cytoskeleton
    • Stamatakis, K., Sanchez-Gomez, F. J., and Perez-Sala, D. (2006). Identification of novel protein targets for modification by 15-deoxy-Delta12,14-prostaglandin J2 in mesangial cells reveals multiple interactions with the cytoskeleton. J. Am. Soc. Nephrol. 17, 89-98. doi: 10.1681/ASN.2005030329
    • (2006) J. Am. Soc. Nephrol , vol.17 , pp. 89-98
    • Stamatakis, K.1    Sanchez-Gomez, F.J.2    Perez-Sala, D.3
  • 202
    • 84887912227 scopus 로고    scopus 로고
    • Developments in neuroimaging: Positron emission tomography
    • Stoessl, A. J. (2014). Developments in neuroimaging: positron emission tomography. Parkinsonism Relat. Disord. 20(Suppl. 1), S180-S183. doi: 10.1016/S1353-8020(13)70042-7
    • (2014) Parkinsonism Relat. Disord , vol.20 , pp. S180-S183
    • Stoessl, A.J.1
  • 203
    • 0035053973 scopus 로고    scopus 로고
    • Cyclopentenone prostaglandins: New insights on biological activities and cellular targets
    • Straus, D. S., and Glass, C. K. (2001). Cyclopentenone prostaglandins: new insights on biological activities and cellular targets. Med. Res. Rev. 21, 185-210. doi: 10.1002/med.1006
    • (2001) Med. Res. Rev , vol.21 , pp. 185-210
    • Straus, D.S.1    Glass, C.K.2
  • 204
    • 0034712933 scopus 로고    scopus 로고
    • 15-deoxy-delta 12,14-prostaglandin J2 inhibits multiple steps in the NF-kappa B signaling pathway
    • Straus, D. S., Pascual, G., Li, M., Welch, J. S., Ricote, M., Hsiang, C. H., et al. (2000). 15-deoxy-delta 12,14-prostaglandin J2 inhibits multiple steps in the NF-kappa B signaling pathway. Proc. Natl. Acad. Sci. U.S.A. 97, 4844-4849. doi: 10.1073/pnas.97.9.4844
    • (2000) Proc. Natl. Acad. Sci. U.S.A , vol.97 , pp. 4844-4849
    • Straus, D.S.1    Pascual, G.2    Li, M.3    Welch, J.S.4    Ricote, M.5    Hsiang, C.H.6
  • 205
    • 55749086991 scopus 로고    scopus 로고
    • 15-deoxy-Delta12,14-prostaglandin J2 up-regulates death receptor 5 gene expression in HCT116 cells: Involvement of reactive oxygen species and C/EBP homologous transcription factor gene transcription
    • Su, R. Y., Chi, K. H., Huang, D. Y., Tai, M. H., and Lin, W. W. (2008). 15-deoxy-Delta12,14-prostaglandin J2 up-regulates death receptor 5 gene expression in HCT116 cells: involvement of reactive oxygen species and C/EBP homologous transcription factor gene transcription. Mol. Cancer Ther. 7, 3429-3440. doi: 10.1158/1535-7163.MCT-08-0498
    • (2008) Mol. Cancer Ther , vol.7 , pp. 3429-3440
    • Su, R.Y.1    Chi, K.H.2    Huang, D.Y.3    Tai, M.H.4    Lin, W.W.5
  • 206
    • 77956867597 scopus 로고    scopus 로고
    • Exosomes account for vesicle-mediated transcellular transport of activatable phospholipases and prostaglandins
    • Subra, C., Grand, D., Laulagnier, K., Stella, A., Lambeau, G., Paillasse, M., et al. (2010). Exosomes account for vesicle-mediated transcellular transport of activatable phospholipases and prostaglandins. J. Lipid Res. 51, 2105-2120. doi: 10.1194/jlr.M003657
    • (2010) J. Lipid Res , vol.51 , pp. 2105-2120
    • Subra, C.1    Grand, D.2    Laulagnier, K.3    Stella, A.4    Lambeau, G.5    Paillasse, M.6
  • 207
    • 80054702892 scopus 로고    scopus 로고
    • 15-Deoxy-Delta(1)(2),(1)(4)-prostaglandin J(2), an electrophilic lipid mediator of anti-inflammatory and pro-resolving signaling
    • Surh, Y. J., Na, H. K., Park, J. M., Lee, H. N., Kim, W., Yoon, I. S., et al. (2011). 15-Deoxy-Delta(1)(2),(1)(4)-prostaglandin J(2), an electrophilic lipid mediator of anti-inflammatory and pro-resolving signaling. Biochem. Pharmacol. 82, 1335-1351. doi: 10.1016/j.bcp.2011.07.100
    • (2011) Biochem. Pharmacol , vol.82 , pp. 1335-1351
    • Surh, Y.J.1    Na, H.K.2    Park, J.M.3    Lee, H.N.4    Kim, W.5    Yoon, I.S.6
  • 208
    • 0022558367 scopus 로고
    • Transport of prostaglandin D2 into brain
    • Suzuki, F., Hayashi, H., and Hayaishi, O. (1986). Transport of prostaglandin D2 into brain. Brain Res. 385, 321-328. doi: 10.1016/0006-8993(86)91079-6
    • (1986) Brain Res , vol.385 , pp. 321-328
    • Suzuki, F.1    Hayashi, H.2    Hayaishi, O.3
  • 209
    • 83855160829 scopus 로고    scopus 로고
    • Prostaglandin catabolic enzymes as tumor suppressors
    • Tai, H. H. (2011). Prostaglandin catabolic enzymes as tumor suppressors. Cancer Metastasis Rev. 30, 409-417. doi: 10.1007/s10555-011-9314-z
    • (2011) Cancer Metastasis Rev , vol.30 , pp. 409-417
    • Tai, H.H.1
  • 210
    • 33645979989 scopus 로고    scopus 로고
    • NAD+-linked 15-hydroxyprostaglandin dehydrogenase: Structure and biological functions
    • Tai, H. H., Cho, H., Tong, M., and Ding, Y. (2006). NAD+-linked 15-hydroxyprostaglandin dehydrogenase: structure and biological functions. Curr. Pharm. Des. 12, 955-962. doi: 10.2174/138161206776055958
    • (2006) Curr. Pharm. Des , vol.12 , pp. 955-962
    • Tai, H.H.1    Cho, H.2    Tong, M.3    Ding, Y.4
  • 213
    • 80053352130 scopus 로고    scopus 로고
    • Mitochondrial quality control by the ubiquitin-proteasome system
    • Taylor, E. B., and Rutter, J. (2011). Mitochondrial quality control by the ubiquitin-proteasome system. Biochem. Soc. Trans. 39, 1509-1513. doi: 10.1042/BST0391509
    • (2011) Biochem. Soc. Trans , vol.39 , pp. 1509-1513
    • Taylor, E.B.1    Rutter, J.2
  • 214
    • 0038641723 scopus 로고    scopus 로고
    • Cyclooxygenase-2 is instrumental in Parkinson's disease neurodegeneration
    • Teismann, P., Tieu, K., Choi, D. K., Wu, D. C., Naini, A., Hunot, S., et al. (2003). Cyclooxygenase-2 is instrumental in Parkinson's disease neurodegeneration. Proc. Natl. Acad. Sci. U.S.A. 100, 5473-5478. doi: 10.1073/pnas.0837397100
    • (2003) Proc. Natl. Acad. Sci. U.S.A , vol.100 , pp. 5473-5478
    • Teismann, P.1    Tieu, K.2    Choi, D.K.3    Wu, D.C.4    Naini, A.5    Hunot, S.6
  • 215
    • 38949126129 scopus 로고    scopus 로고
    • 15-Deoxy-Delta(12,14)-prostaglandin J2: An electrophilic trigger of cellular responses
    • Uchida, K., and Shibata, T. (2008). 15-Deoxy-Delta(12,14)-prostaglandin J2: an electrophilic trigger of cellular responses. Chem. Res. Toxicol. 21, 138-144. doi: 10.1021/tx700177j
    • (2008) Chem. Res. Toxicol , vol.21 , pp. 138-144
    • Uchida, K.1    Shibata, T.2
  • 216
    • 38449094180 scopus 로고    scopus 로고
    • Role of the ubiquitin proteasome system in Alzheimer's disease
    • Upadhya, S. C., and Hegde, A. N. (2007). Role of the ubiquitin proteasome system in Alzheimer's disease. BMC Biochem. 8(Suppl. 1):S12. doi: 10.1186/1471-2091-8-S1-S12
    • (2007) BMC Biochem , vol.8 , pp. S12
    • Upadhya, S.C.1    Hegde, A.N.2
  • 217
    • 0036669560 scopus 로고    scopus 로고
    • Lipocalin-type and hematopoietic prostaglandin D synthases as a novel example of functional convergence
    • Urade, Y., and Eguchi, N. (2002). Lipocalin-type and hematopoietic prostaglandin D synthases as a novel example of functional convergence. Prostaglandins Other Lipid Mediat. 68-69, 375-382. doi: 10.1016/S0090-6980(02)00042-4
    • (2002) Prostaglandins Other Lipid Mediat , vol.69-69 , pp. 375-382
    • Urade, Y.1    Eguchi, N.2
  • 218
    • 0033627825 scopus 로고    scopus 로고
    • Prostaglandin D synthase: Structure and function
    • Urade, Y., and Hayaishi, O. (2000). Prostaglandin D synthase: structure and function. Vitam. Horm. 58, 89-120. doi: 10.1016/S0083-6729(00)58022-4
    • (2000) Vitam. Horm , vol.58 , pp. 89-120
    • Urade, Y.1    Hayaishi, O.2
  • 219
    • 84897914359 scopus 로고    scopus 로고
    • Protein modifications by electrophilic lipoxidation products: Adduct formation, chemical strategies and tandem mass spectrometry for their detection and identification
    • Vasil'ev, Y. V., Tzeng, S. C., Huang, L., and Maier, C. S. (2014). Protein modifications by electrophilic lipoxidation products: adduct formation, chemical strategies and tandem mass spectrometry for their detection and identification. Mass Spectrom. Rev. 33, 157-182. doi: 10.1002/mas.21389
    • (2014) Mass Spectrom. Rev , vol.33 , pp. 157-182
    • Vasil'ev, Y.V.1    Tzeng, S.C.2    Huang, L.3    Maier, C.S.4
  • 220
  • 221
    • 43149102747 scopus 로고    scopus 로고
    • Protective effects of NSAIDs on the development of Alzheimer disease
    • Vlad, S. C., Miller, D. R., Kowall, N. W., and Felson, D. T. (2008). Protective effects of NSAIDs on the development of Alzheimer disease. Neurology 70, 1672-1677. doi: 10.1212/01.wnl.0000311269.57716.63
    • (2008) Neurology , vol.70 , pp. 1672-1677
    • Vlad, S.C.1    Miller, D.R.2    Kowall, N.W.3    Felson, D.T.4
  • 222
    • 84867169460 scopus 로고    scopus 로고
    • Oxidative modification of proteins: An emerging mechanism of cell signaling
    • Wall, S. B., Oh, J. Y., Diers, A. R., and Landar, A. (2012). Oxidative modification of proteins: an emerging mechanism of cell signaling. Front. Physiol. 3:369. doi: 10.3389/fphys.2012.00369
    • (2012) Front. Physiol , vol.3 , pp. 369
    • Wall, S.B.1    Oh, J.Y.2    Diers, A.R.3    Landar, A.4
  • 223
    • 33746366513 scopus 로고    scopus 로고
    • Prostaglandin J2 alters pro-survival and pro-death gene expression patterns and 26 S proteasome assembly in human neuroblastoma cells
    • Wang, Z., Aris, V. M., Ogburn, K. D., Soteropoulos, P., and Figueiredo-Pereira, M. E. (2006). Prostaglandin J2 alters pro-survival and pro-death gene expression patterns and 26 S proteasome assembly in human neuroblastoma cells. J. Biol. Chem. 281, 21377-21386. doi: 10.1074/jbc.M601201200
    • (2006) J. Biol. Chem , vol.281 , pp. 21377-21386
    • Wang, Z.1    Aris, V.M.2    Ogburn, K.D.3    Soteropoulos, P.4    Figueiredo-Pereira, M.E.5
  • 224
    • 0026757444 scopus 로고
    • Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases
    • Wilkinson, K. D., Deshpande, S., and Larsen, C. N. (1992). Comparisons of neuronal (PGP 9.5) and non-neuronal ubiquitin C-terminal hydrolases. Biochem. Soc. Trans. 20, 631-637.
    • (1992) Biochem. Soc. Trans , vol.20 , pp. 631-637
    • Wilkinson, K.D.1    Deshpande, S.2    Larsen, C.N.3
  • 225
    • 0034805226 scopus 로고    scopus 로고
    • A cyclopentenone prostaglandin activates mesangial MAP kinase independently of PPARgamma
    • Wilmer, W. A., Dixon, C., Lu, L., Hilbelink, T., and Rovin, B. H. (2001). A cyclopentenone prostaglandin activates mesangial MAP kinase independently of PPARgamma. Biochem. Biophys. Res. Commun. 281, 57-62. doi: 10.1006/bbrc.2001.4301
    • (2001) Biochem. Biophys. Res. Commun , vol.281 , pp. 57-62
    • Wilmer, W.A.1    Dixon, C.2    Lu, L.3    Hilbelink, T.4    Rovin, B.H.5
  • 226
    • 0036685522 scopus 로고    scopus 로고
    • Inflammation in neurodegenerative disease-a double-edged sword
    • Wyss-Coray, T., and Mucke, L. (2002). Inflammation in neurodegenerative disease-a double-edged sword. Neuron35, 419-432. doi: 10.1016/S0896-6273(02)00794-8
    • (2002) Neuron , vol.35 , pp. 419-432
    • Wyss-Coray, T.1    Mucke, L.2
  • 227
    • 0034684232 scopus 로고    scopus 로고
    • Lipocalins as biochemical markers of disease
    • Xu, S., and Venge, P. (2000). Lipocalins as biochemical markers of disease. Biochim. Biophys. Acta 1482, 298-307. doi: 10.1016/S0167-4838(00)00163-1
    • (2000) Biochim. Biophys. Acta , vol.1482 , pp. 298-307
    • Xu, S.1    Venge, P.2
  • 228
    • 33646024670 scopus 로고    scopus 로고
    • Cerebral arachidonate cascade in dementia: Alzheimer's disease and vascular dementia
    • Yagami, T. (2006). Cerebral arachidonate cascade in dementia: Alzheimer's disease and vascular dementia. Curr. Neuropharmacol. 4, 87-100. doi: 10.2174/157015906775203011
    • (2006) Curr. Neuropharmacol , vol.4 , pp. 87-100
    • Yagami, T.1
  • 229
    • 0027290813 scopus 로고
    • Expression of a mitogen-inducible cyclooxygenase in brain neurons: Regulation by synaptic activity and glucocorticoids
    • Yamagata, K., Andreasson, K. I., Kaufmann, W. E., Barnes, C. A., and Worley, P. F. (1993). Expression of a mitogen-inducible cyclooxygenase in brain neurons: regulation by synaptic activity and glucocorticoids. Neuron 11, 371-386. doi: 10.1016/0896-6273(93)90192-T
    • (1993) Neuron , vol.11 , pp. 371-386
    • Yamagata, K.1    Andreasson, K.I.2    Kaufmann, W.E.3    Barnes, C.A.4    Worley, P.F.5
  • 230
    • 79952784842 scopus 로고    scopus 로고
    • Proteomic identification of protein targets for 15-deoxy-Delta(12,14)-prostaglandin J2 in neuronal plasma membrane
    • Yamamoto, Y., Takase, K., Kishino, J., Fujita, M., Okamura, N., Sakaeda, T., et al. (2011). Proteomic identification of protein targets for 15-deoxy-Delta(12,14)-prostaglandin J2 in neuronal plasma membrane. PLoS ONE 6:e17552. doi: 10.1371/journal.pone.0017552
    • (2011) PLoS ONE , vol.6
    • Yamamoto, Y.1    Takase, K.2    Kishino, J.3    Fujita, M.4    Okamura, N.5    Sakaeda, T.6
  • 231
    • 84855398969 scopus 로고    scopus 로고
    • Rapid degradation of cyclooxygenase-1 and hematopoietic prostaglandin D synthase through ubiquitin-proteasome system in response to intracellular calcium level
    • Yazaki, M., Kashiwagi, K., Aritake, K., Urade, Y., and Fujimori, K. (2012). Rapid degradation of cyclooxygenase-1 and hematopoietic prostaglandin D synthase through ubiquitin-proteasome system in response to intracellular calcium level. Mol. Biol. Cell 23, 12-21. doi: 10.1091/mbc.E11-07-0623
    • (2012) Mol. Biol. Cell , vol.23 , pp. 12-21
    • Yazaki, M.1    Kashiwagi, K.2    Aritake, K.3    Urade, Y.4    Fujimori, K.5
  • 232
    • 33846538660 scopus 로고    scopus 로고
    • Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model
    • Yoshiyama, Y., Higuchi, M., Zhang, B., Huang, S. M., Iwata, N., Saido, T. C., et al. (2007). Synapse loss and microglial activation precede tangles in a P301S tauopathy mouse model. Neuron 53, 337-351. doi: 10.1016/j.neuron.2007.01.010
    • (2007) Neuron , vol.53 , pp. 337-351
    • Yoshiyama, Y.1    Higuchi, M.2    Zhang, B.3    Huang, S.M.4    Iwata, N.5    Saido, T.C.6
  • 233
    • 23844500606 scopus 로고    scopus 로고
    • Prostaglandin H(2)-derived adducts of proteins correlate with Alzheimer's disease severity
    • Zagol-Ikapitte, I., Masterson, T. S., Amarnath, V., Montine, T. J., Andreasson, K. I., Boutaud, O., et al. (2005). Prostaglandin H(2)-derived adducts of proteins correlate with Alzheimer's disease severity. J. Neurochem. 94, 1140-1145. doi: 10.1111/j.1471-4159.2005.03264.x
    • (2005) J. Neurochem , vol.94 , pp. 1140-1145
    • Zagol-Ikapitte, I.1    Masterson, T.S.2    Amarnath, V.3    Montine, T.J.4    Andreasson, K.I.5    Boutaud, O.6
  • 234
    • 77549088434 scopus 로고    scopus 로고
    • Alteration of biochemical and pathological properties of TDP-43 protein by a lipid mediator, 15-deoxy-Delta(12,14)-prostaglandin J(2)
    • Zhang, H. X., Tanji, K., Yoshida, H., Hayakari, M., Shibata, T., Mori, F., et al. (2010). Alteration of biochemical and pathological properties of TDP-43 protein by a lipid mediator, 15-deoxy-Delta(12,14)-prostaglandin J(2). Exp. Neurol. 222, 296-303. doi: 10.1016/j.expneurol.2010.01.007
    • (2010) Exp. Neurol , vol.222 , pp. 296-303
    • Zhang, H.X.1    Tanji, K.2    Yoshida, H.3    Hayakari, M.4    Shibata, T.5    Mori, F.6
  • 235
    • 0035876919 scopus 로고    scopus 로고
    • Differential regulation of chemokine gene expression by 15-deoxy-delta 12,14 prostaglandin J2
    • Zhang, X., Wang, J. M., Gong, W. H., Mukaida, N., and Young, H. A. (2001). Differential regulation of chemokine gene expression by 15-deoxy-delta 12,14 prostaglandin J2. J. Immunol. 166, 7104-7111. doi: 10.4049/jimmunol.166.12.7104
    • (2001) J. Immunol , vol.166 , pp. 7104-7111
    • Zhang, X.1    Wang, J.M.2    Gong, W.H.3    Mukaida, N.4    Young, H.A.5
  • 236
    • 33749080403 scopus 로고    scopus 로고
    • Intracrine signaling through lipid mediators and their cognate nuclear G-protein-coupled receptors: A paradigm based on PGE2, PAF, and LPA1 receptors
    • Zhu, T., Gobeil, F., Vazquez-Tello, A., Leduc, M., Rihakova, L., Bossolasco, M., et al. (2006). Intracrine signaling through lipid mediators and their cognate nuclear G-protein-coupled receptors: a paradigm based on PGE2, PAF, and LPA1 receptors. Can. J. Physiol. Pharmacol. 84, 377-391. doi: 10.1139/y05-147
    • (2006) Can. J. Physiol. Pharmacol , vol.84 , pp. 377-391
    • Zhu, T.1    Gobeil, F.2    Vazquez-Tello, A.3    Leduc, M.4    Rihakova, L.5    Bossolasco, M.6
  • 237
    • 72949092495 scopus 로고    scopus 로고
    • Involvement of pro- and anti-inflammatory cytokines and chemokines in the pathophysiology of traumatic brain injury
    • Ziebell, J. M., and Morganti-Kossmann, M. C. (2010). Involvement of pro- and anti-inflammatory cytokines and chemokines in the pathophysiology of traumatic brain injury. Neurotherapeutics 7, 22-30. doi: 10.1016/j.nurt.2009.10.016
    • (2010) Neurotherapeutics , vol.7 , pp. 22-30
    • Ziebell, J.M.1    Morganti-Kossmann, M.C.2


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