메뉴 건너뛰기




Volumn 290, Issue 42, 2015, Pages 25439-25451

A novel role of proline oxidase in HIV-1 envelope glycoprotein-induced neuronal autophagy

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYLATION; CATALYST ACTIVITY; CELL DEATH; DIGITAL STORAGE; GLYCOPROTEINS; PLANTS (BOTANY);

EID: 84944398940     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.652776     Document Type: Article
Times cited : (27)

References (82)
  • 1
    • 0018890003 scopus 로고
    • Metabolism of proline and the hydroxyprolines
    • Adams, E., and Frank, L. (1980) Metabolism of proline and the hydroxyprolines. Annu. Rev. Biochem. 49, 1005-1061
    • (1980) Annu. Rev.Biochem. , vol.49 , pp. 1005-1061
    • Adams, E.1    Frank, L.2
  • 2
    • 0021994031 scopus 로고
    • The regulatory functions of proline and pyrroline-5-carboxylic acid
    • Phang, J. M. (1985) The regulatory functions of proline and pyrroline-5-carboxylic acid. Curr. Top. Cell. Regul. 25, 91-132
    • (1985) Curr. Top.Cell. Regul. , vol.25 , pp. 91-132
    • Phang, J.M.1
  • 3
    • 0023735598 scopus 로고
    • Stimulation of phosphoribosyl pyrophosphate and purine nucleotide production by pyrroline 5-carboxylate in human erythrocytes
    • Yeh, G. C., and Phang, J. M. (1988) Stimulation of phosphoribosyl pyrophosphate and purine nucleotide production by pyrroline 5-carboxylate in human erythrocytes. J. Biol. Chem. 263, 13083-13089
    • (1988) J. Biol.Chem. , vol.263 , pp. 13083-13089
    • Yeh, G.C.1    Phang, J.M.2
  • 4
    • 0035266127 scopus 로고    scopus 로고
    • Proline oxidase, encoded by p53-induced gene-6, catalyzes the generation of proline-dependent reactive oxygen species
    • Donald, S. P., Sun, X. Y., Hu, C. A., Yu, J., Mei, J. M., Valle, D., and Phang, J. M. (2001) Proline oxidase, encoded by p53-induced gene-6, catalyzes the generation of proline-dependent reactive oxygen species. Cancer Res. 61, 1810-1815
    • (2001) Cancer Res , vol.61 , pp. 1810-1815
    • Donald, S.P.1    Sun, X.Y.2    Hu, C.A.3    Yu, J.4    Mei, J.M.5    Valle, D.6    Phang, J.M.7
  • 5
    • 33644850483 scopus 로고    scopus 로고
    • Proline oxidase, a proapoptotic gene, is induced by troglitazone: Evidence for both peroxisome proliferator-activated receptor γ-dependent and -independent mechanisms
    • Pandhare, J., Cooper, S. K., and Phang, J. M. (2006) Proline oxidase, a proapoptotic gene, is induced by troglitazone: evidence for both peroxisome proliferator-activated receptor γ-dependent and -independent mechanisms. J. Biol. Chem. 281, 2044-2052
    • (2006) J. Biol. Chem. , vol.281 , pp. 2044-2052
    • Pandhare, J.1    Cooper, S.K.2    Phang, J.M.3
  • 6
    • 84901316606 scopus 로고    scopus 로고
    • Cellular mechanisms and physiological consequences of redox-dependent signalling
    • Holmström, K. M., and Finkel, T. (2014) Cellular mechanisms and physiological consequences of redox-dependent signalling. Nat. Rev. Mol. Cell Biol. 15, 411-421
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 411-421
    • Holmström, K.M.1    Finkel, T.2
  • 7
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • Finkel, T. (2011) Signal transduction by reactive oxygen species. J. Cell Biol. 194, 7-15
    • (2011) J. Cell Biol. , vol.194 , pp. 7-15
    • Finkel, T.1
  • 8
    • 53849096017 scopus 로고    scopus 로고
    • The metabolism of proline, a stress substrate, modulates carcinogenic pathways
    • Phang, J. M., Donald, S. P., Pandhare, J., and Liu, Y. (2008) The metabolism of proline, a stress substrate, modulates carcinogenic pathways. Amino Acids 35, 681-690
    • (2008) Amino Acids , vol.35 , pp. 681-690
    • Phang, J.M.1    Donald, S.P.2    Pandhare, J.3    Liu, Y.4
  • 10
    • 77955619986 scopus 로고    scopus 로고
    • Proline metabolism and microenvironmental stress
    • Phang, J. M., Liu, W., and Zabirnyk, O. (2010) Proline metabolism and microenvironmental stress. Annu. Rev. Nutr. 30, 441-463
    • (2010) Annu. Rev.Nutr. , vol.30 , pp. 441-463
    • Phang, J.M.1    Liu, W.2    Zabirnyk, O.3
  • 11
    • 77950890848 scopus 로고    scopus 로고
    • Oxidized low-density lipoproteins upregulate proline oxidase to initiate ROS-dependent autophagy
    • Zabirnyk, O., Liu, W., Khalil, S., Sharma, A., and Phang, J. M. (2010) Oxidized low-density lipoproteins upregulate proline oxidase to initiate ROS-dependent autophagy. Carcinogenesis 31, 446-454
    • (2010) Carcinogenesis , vol.31 , pp. 446-454
    • Zabirnyk, O.1    Liu, W.2    Khalil, S.3    Sharma, A.4    Phang, J.M.5
  • 12
    • 84866544950 scopus 로고    scopus 로고
    • Proline dehydrogenase (oxidase), a mitochondrial tumor suppressor, and autophagy under the hypoxia microenvironment
    • Liu, W., and Phang, J. M. (2012) Proline dehydrogenase (oxidase), a mitochondrial tumor suppressor, and autophagy under the hypoxia microenvironment. Autophagy 8, 1407-1409
    • (2012) Autophagy , vol.8 , pp. 1407-1409
    • Liu, W.1    Phang, J.M.2
  • 14
    • 0026716689 scopus 로고
    • Molecular cloning and expression of a high affinity L-proline transporter expressed in putative glutamatergic pathways of rat brain
    • Fremeau, R. T., Jr., Caron, M. G., and Blakely, R. D. (1992) Molecular cloning and expression of a high affinity L-proline transporter expressed in putative glutamatergic pathways of rat brain. Neuron 8, 915-926
    • (1992) Neuron , vol.8 , pp. 915-926
    • Fremeau Jr. T, R.1    Caron, M.G.2    Blakely, R.D.3
  • 15
    • 0032906584 scopus 로고    scopus 로고
    • The mammalian brain high-affinity L-proline transporter is enriched preferentially in synaptic vesicles in a subpopulation of excitatory nerve terminals in rat forebrain
    • Renick, S. E., Kleven, D. T., Chan, J., Stenius, K., Milner, T. A., Pickel, V. M., and Fremeau, R. T., Jr. (1999) The mammalian brain high-affinity L-proline transporter is enriched preferentially in synaptic vesicles in a subpopulation of excitatory nerve terminals in rat forebrain. J. Neurosci. 19, 21-33
    • (1999) J. Neurosci. , vol.19 , pp. 21-33
    • Renick, S.E.1    Kleven, D.T.2    Chan, J.3    Stenius, K.4    Milner, T.A.5    Pickel, V.M.6    Fremeau, T.R.7
  • 16
    • 0030787937 scopus 로고    scopus 로고
    • Proline-induced potentiation of glutamate transmission
    • Cohen, S. M., and Nadler, J. V. (1997) Proline-induced potentiation of glutamate transmission. Brain Res. 761, 271-282
    • (1997) Brain Res. , vol.761 , pp. 271-282
    • Cohen, S.M.1    Nadler, J.V.2
  • 21
    • 67349160223 scopus 로고    scopus 로고
    • A risk PRODH haplotype affects sensorimotor gating, memory, schizotypy, and anxiety in healthy male subjects
    • Roussos, P., Giakoumaki, S. G., and Bitsios, P. (2009) A risk PRODH haplotype affects sensorimotor gating, memory, schizotypy, and anxiety in healthy male subjects. Biol. Psychiatry 65, 1063-1070
    • (2009) Biol. Psychiatry , vol.65 , pp. 1063-1070
    • Roussos, P.1    Giakoumaki, S.G.2    Bitsios, P.3
  • 22
    • 77954891060 scopus 로고    scopus 로고
    • Synapse pathology in psychiatric and neurologic disease
    • van Spronsen, M., and Hoogenraad, C. C. (2010) Synapse pathology in psychiatric and neurologic disease. Curr. Neurol. Neurosci. Rep 10, 207-214
    • (2010) Curr. Neurol. Neurosci. Rep , vol.10 , pp. 207-214
    • Van Spronsen, M.1    Hoogenraad, C.C.2
  • 23
    • 80052296956 scopus 로고    scopus 로고
    • Behavioral and neurochemical effects of proline
    • Wyse, A. T., and Netto, C. A. (2011) Behavioral and neurochemical effects of proline. Metab. Brain Dis 26, 159-172
    • (2011) Metab. Brain Dis , vol.26 , pp. 159-172
    • Wyse, A.T.1    Netto, C.A.2
  • 24
    • 0038136866 scopus 로고    scopus 로고
    • Pathogenesis of human immunodeficiency virus-induced neurological disease
    • Albright, A. V., Soldan, S. S., and González-Scarano, F. (2003) Pathogenesis of human immunodeficiency virus-induced neurological disease. J. Neurovirol. 9, 222-227
    • (2003) J. Neurovirol. , vol.9 , pp. 222-227
    • Albright, A.V.1    Soldan, S.S.2    González-Scarano, F.3
  • 25
    • 77957969916 scopus 로고    scopus 로고
    • Neurologic disease burden in treated HIV/AIDS predicts survival: A population-based study
    • Vivithanaporn, P., Heo, G., Gamble, J., Krentz, H. B., Hoke, A., Gill, M. J., and Power, C. (2010) Neurologic disease burden in treated HIV/AIDS predicts survival: a population-based study. Neurology 75, 1150-1158
    • (2010) Neurology , vol.75 , pp. 1150-1158
    • Vivithanaporn, P.1    Heo, G.2    Gamble, J.3    Krentz, H.B.4    Hoke, A.5    Gill, M.J.6    Power, C.7
  • 26
    • 77952149363 scopus 로고    scopus 로고
    • Does highly active antiretroviral therapy improve neurocognitive function? A systematic review
    • Joska, J. A., Gouse, H., Paul, R. H., Stein, D. J., and Flisher, A. J. (2010) Does highly active antiretroviral therapy improve neurocognitive function? A systematic review. J. Neurovirol. 16, 101-114
    • (2010) J. Neurovirol. , vol.16 , pp. 101-114
    • Joska, J.A.1    Gouse, H.2    Paul, R.H.3    Stein, D.J.4    Flisher, A.J.5
  • 28
    • 77952940200 scopus 로고    scopus 로고
    • Human immunodeficiency virus-associated neurocognitive disorders: Mind the gap
    • McArthur, J. C., Steiner, J., Sacktor, N., and Nath, A. (2010) Human immunodeficiency virus-associated neurocognitive disorders: mind the gap. Ann. Neurol. 67, 699-714
    • (2010) Ann. Neurol. , vol.67 , pp. 699-714
    • McArthur, J.C.1    Steiner, J.2    Sacktor, N.3    Nath, A.4
  • 29
    • 0034092005 scopus 로고    scopus 로고
    • Human immunodeficiency virus-associated dementia
    • Clifford, D. B. (2000) Human immunodeficiency virus-associated dementia. Arch. Neurol. 57, 321-324
    • (2000) Arch. Neurol. , vol.57 , pp. 321-324
    • Clifford, D.B.1
  • 30
    • 84901818666 scopus 로고    scopus 로고
    • Viral and cellular factors underlying neuropathogenesis in HIV-associated neurocognitive disorders (HAND)
    • Rao, V. R., Ruiz, A. P., and Prasad, V. R. (2014) Viral and cellular factors underlying neuropathogenesis in HIV-associated neurocognitive disorders (HAND). AIDS Res. Ther. 11, 13
    • (2014) AIDS Res.Ther. , vol.11 , pp. 13
    • Rao, V.R.1    Ruiz, A.P.2    Prasad, V.R.3
  • 31
    • 0035912198 scopus 로고    scopus 로고
    • Pathways to neuronal injury and apoptosis in HIV-associated dementia
    • Kaul, M., Garden, G. A., and Lipton, S. A. (2001) Pathways to neuronal injury and apoptosis in HIV-associated dementia. Nature 410, 988-994
    • (2001) Nature , vol.410 , pp. 988-994
    • Kaul, M.1    Garden, G.A.2    Lipton, S.A.3
  • 32
    • 0036891081 scopus 로고    scopus 로고
    • Human immunodeficiency virus (HIV) proteins in neuropathogenesis of HIV dementia
    • Nath, A. (2002) Human immunodeficiency virus (HIV) proteins in neuropathogenesis of HIV dementia. J. Infect. Dis. 186, S193-S198
    • (2002) J. Infect.Dis. , vol.186 , pp. S193-S198
    • Nath, A.1
  • 34
    • 84856242946 scopus 로고    scopus 로고
    • Neurotoxicity of human immunodeficiency virus-1: Viral proteins and axonal transport
    • Mocchetti, I., Bachis, A., and Avdoshina, V. (2012) Neurotoxicity of human immunodeficiency virus-1: viral proteins and axonal transport. Neurotox. Res. 21, 79-89
    • (2012) Neurotox. Res. , vol.21 , pp. 79-89
    • Mocchetti, I.1    Bachis, A.2    Avdoshina, V.3
  • 35
    • 2442593764 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 protein gp120 causes neuronal cell death in the rat brain by activating caspases
    • Acquas, E., Bachis, A., Nosheny, R. L., Cernak, I., and Mocchetti, I. (2004) Human immunodeficiency virus type 1 protein gp120 causes neuronal cell death in the rat brain by activating caspases. Neurotox. Res. 5, 605-615
    • (2004) Neurotox. Res. , vol.5 , pp. 605-615
    • Acquas, E.1    Bachis, A.2    Nosheny, R.L.3    Cernak, I.4    Mocchetti, I.5
  • 36
    • 71549124077 scopus 로고    scopus 로고
    • Dopaminergic neurotoxicity of HIV-1 gp120: Reactive oxygen species as signaling intermediates
    • Agrawal, L., Louboutin, J. P., Marusich, E., Reyes, B. A., Van Bockstaele, E. J., and Strayer, D. S. (2010) Dopaminergic neurotoxicity of HIV-1 gp120: reactive oxygen species as signaling intermediates. Brain Res 1306, 116-130
    • (2010) Brain Res , vol.1306 , pp. 116-130
    • Agrawal, L.1    Louboutin, J.P.2    Marusich, E.3    Reyes, B.A.4    Van Bockstaele, E.J.5    Strayer, D.S.6
  • 38
    • 77649132973 scopus 로고    scopus 로고
    • Preferential sensitivity of human dopaminergic neurons to gp120-induced oxidative damage
    • Hu, S., Sheng, W. S., Lokensgard, J. R., Peterson, P. K., and Rock, R. B. (2009) Preferential sensitivity of human dopaminergic neurons to gp120-induced oxidative damage. J. Neurovirol. 15, 401-410
    • (2009) J. Neurovirol. , vol.15 , pp. 401-410
    • Hu, S.1    Sheng, W.S.2    Lokensgard, J.R.3    Peterson, P.K.4    Rock, R.B.5
  • 39
    • 7444266728 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 gp120 induces apoptosis in human primary neurons through redox-regulated activation of neutral sphingomyelinase
    • Jana, A., and Pahan, K. (2004) Human immunodeficiency virus type 1 gp120 induces apoptosis in human primary neurons through redox-regulated activation of neutral sphingomyelinase. J. Neurosci. 24, 9531-9540
    • (2004) J. Neurosci. , vol.24 , pp. 9531-9540
    • Jana, A.1    Pahan, K.2
  • 40
    • 84858141312 scopus 로고    scopus 로고
    • Blood-brain barrier abnormalities caused by HIV-1 gp120: Mechanistic and therapeutic implications
    • Louboutin, J. P., and Strayer, D. S. (2012) Blood-brain barrier abnormalities caused by HIV-1 gp120: mechanistic and therapeutic implications. ScientificWorldJournal 2012, 482575
    • (2012) ScientificWorldJournal , vol.2012 , pp. 482575
    • Louboutin, J.P.1    Strayer, D.S.2
  • 41
    • 78149455160 scopus 로고    scopus 로고
    • Cocaine potentiates astrocyte toxicity mediated by human immunodeficiency virus (HIV-1) protein gp120
    • Yang, Y., Yao, H., Lu, Y., Wang, C., and Buch, S. (2010) Cocaine potentiates astrocyte toxicity mediated by human immunodeficiency virus (HIV-1) protein gp120. PLoS ONE 5, e13427
    • (2010) PLoS ONE , vol.5 , pp. e13427
    • Yang, Y.1    Yao, H.2    Lu, Y.3    Wang, C.4    Buch, S.5
  • 43
    • 67650087634 scopus 로고    scopus 로고
    • Regulation and function of proline oxidase under nutrient stress
    • Pandhare, J., Donald, S. P., Cooper, S. K., and Phang, J. M. (2009) Regulation and function of proline oxidase under nutrient stress. J. Cell. Biochem. 107, 759-768
    • (2009) J. Cell.Biochem. , vol.107 , pp. 759-768
    • Pandhare, J.1    Donald, S.P.2    Cooper, S.K.3    Phang, J.M.4
  • 44
    • 84856821006 scopus 로고    scopus 로고
    • Signal transduction by mitochondrial oxidants
    • Finkel, T. (2012) Signal transduction by mitochondrial oxidants. J. Biol. Chem. 287, 4434-4440
    • (2012) J. Biol.Chem. , vol.287 , pp. 4434-4440
    • Finkel, T.1
  • 45
    • 76049083966 scopus 로고    scopus 로고
    • Reactive oxygen species, cellular redox systems, and apoptosis
    • Circu, M. L., and Aw, T. Y. (2010) Reactive oxygen species, cellular redox systems, and apoptosis. Free Radic. Biol. Med. 48, 749-762
    • (2010) Free Radic. Biol. Med. , vol.48 , pp. 749-762
    • Circu, M.L.1    Aw, T.Y.2
  • 47
    • 78650328444 scopus 로고    scopus 로고
    • Autophagy basics
    • Tanida, I. (2011) Autophagy basics. Microbiol Immunol 55, 1-11
    • (2011) Microbiol Immunol , vol.55 , pp. 1-11
    • Tanida, I.1
  • 48
    • 79956095420 scopus 로고    scopus 로고
    • Autophagosome formation and molecular mechanism of autophagy
    • Tanida, I. (2011) Autophagosome formation and molecular mechanism of autophagy. Antioxid. Redox Signal. 14, 2201-2214
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 2201-2214
    • Tanida, I.1
  • 49
    • 84555195856 scopus 로고    scopus 로고
    • Autophagy, mitochondria and oxidative stress: Cross-talk and redox signalling
    • Lee, J., Giordano, S., and Zhang, J. (2012) Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling. Biochem. J. 441, 523-540
    • (2012) Biochem. J. , vol.441 , pp. 523-540
    • Lee, J.1    Giordano, S.2    Zhang, J.3
  • 50
    • 72549095406 scopus 로고    scopus 로고
    • Regulation mechanisms and signaling pathways of autophagy
    • He, C., and Klionsky, D. J. (2009) Regulation mechanisms and signaling pathways of autophagy. Annu. Rev. Genet. 43, 67-93
    • (2009) Annu. Rev.Genet. , vol.43 , pp. 67-93
    • He, C.1    Klionsky, D.J.2
  • 51
    • 84863896166 scopus 로고    scopus 로고
    • Proline oxidase promotes tumor cell survival in hypoxic tumor microenvironments
    • Liu, W., Glunde, K., Bhujwalla, Z. M., Raman, V., Sharma, A., and Phang, J. M. (2012) Proline oxidase promotes tumor cell survival in hypoxic tumor microenvironments. Cancer Res. 72, 3677-3686
    • (2012) Cancer Res. , vol.72 , pp. 3677-3686
    • Liu, W.1    Glunde, K.2    Bhujwalla, Z.M.3    Raman, V.4    Sharma, A.5    Phang, J.M.6
  • 52
    • 59349105233 scopus 로고    scopus 로고
    • Monitoring autophagy in mammalian cultured cells through the dynamics of LC3
    • Kimura, S., Fujita, N., Noda, T., and Yoshimori, T. (2009) Monitoring autophagy in mammalian cultured cells through the dynamics of LC3. Methods Enzymol. 452, 1-12
    • (2009) Methods Enzymol. , vol.452 , pp. 1-12
    • Kimura, S.1    Fujita, N.2    Noda, T.3    Yoshimori, T.4
  • 53
    • 58149083873 scopus 로고    scopus 로고
    • Selective turnover of p62/A170/SQSTM1 by autophagy
    • Ichimura, Y., Kominami, E., Tanaka, K., and Komatsu, M. (2008) Selective turnover of p62/A170/SQSTM1 by autophagy. Autophagy 4, 1063-1066
    • (2008) Autophagy , vol.4 , pp. 1063-1066
    • Ichimura, Y.1    Kominami, E.2    Tanaka, K.3    Komatsu, M.4
  • 54
    • 84898729030 scopus 로고    scopus 로고
    • How can I halt thee? The puzzles involved in autophagic inhibition
    • Vinod, V., Padmakrishnan, C. J., Vijayan, B., and Gopala, S. (2014) 'How can I halt thee?' The puzzles involved in autophagic inhibition. Pharmacol. Res. 82, 1-8
    • (2014) Pharmacol. Res. , vol.82 , pp. 1-8
    • Vinod, V.1    Padmakrishnan, C.J.2    Vijayan, B.3    Gopala, S.4
  • 55
    • 35648945862 scopus 로고    scopus 로고
    • The glial response to CNS HIV infection includes p53 activation and increased expression of p53 target genes
    • Jayadev, S., Yun, B., Nguyen, H., Yokoo, H., Morrison, R. S., and Garden, G. A. (2007) The glial response to CNS HIV infection includes p53 activation and increased expression of p53 target genes. J Neuroimmune Pharmacol. 2, 359-370
    • (2007) J Neuroimmune Pharmacol , vol.2 , pp. 359-370
    • Jayadev, S.1    Yun, B.2    Nguyen, H.3    Yokoo, H.4    Morrison, R.S.5    Garden, G.A.6
  • 57
    • 18144380368 scopus 로고    scopus 로고
    • The multiple roles of p53 in the pathogenesis of HIV associated dementia
    • Garden, G. A., and Morrison, R. S. (2005) The multiple roles of p53 in the pathogenesis of HIV associated dementia. Biochem. Biophys. Res. Commun. 331, 799-809
    • (2005) Biochem. Biophys.Res. Commun. , vol.331 , pp. 799-809
    • Garden, G.A.1    Morrison, R.S.2
  • 59
    • 78649833334 scopus 로고    scopus 로고
    • p53-dependent regulation of autophagy protein LC3 supports cancer cell survival under prolonged starvation
    • Scherz-Shouval, R., Weidberg, H., Gonen, C., Wilder, S., Elazar, Z., and Oren, M. (2010) p53-dependent regulation of autophagy protein LC3 supports cancer cell survival under prolonged starvation. Proc. Natl. Acad. Sci. U.S.A. 107, 18511-18516
    • (2010) Proc. Natl.Acad. Sci. U.S.A. , vol.107 , pp. 18511-18516
    • Scherz-Shouval, R.1    Weidberg, H.2    Gonen, C.3    Wilder, S.4    Elazar, Z.5    Oren, M.6
  • 62
    • 84896808624 scopus 로고    scopus 로고
    • β-Arrestin1 and distinct CXCR4 structures are required for stromal derived factor-1 to downregulate CXCR4 cell-surface levels in neuroblastoma
    • Clift, I. C., Bamidele, A. O., Rodriguez-Ramirez, C., Kremer, K. N., and Hedin, K. E. (2014) β-Arrestin1 and distinct CXCR4 structures are required for stromal derived factor-1 to downregulate CXCR4 cell-surface levels in neuroblastoma. Mol. Pharmacol. 85, 542-552
    • (2014) Mol. Pharmacol. , vol.85 , pp. 542-552
    • Clift, I.C.1    Bamidele, A.O.2    Rodriguez-Ramirez, C.3    Kremer, K.N.4    Hedin, K.E.5
  • 64
    • 0035887446 scopus 로고    scopus 로고
    • Human immunodeficiency virus 1 envelope glycoprotein complex-induced apoptosis involves mammalian target of rapamycin/FKBP12-rapamycin-associated protein-mediated p53 phosphorylation
    • Castedo, M., Ferri, K. F., Blanco, J., Roumier, T., Larochette, N., Barretina, J., Amendola, A., Nardacci, R., Métivier, D., Este, J. A., Piacentini, M., and Kroemer, G. (2001) Human immunodeficiency virus 1 envelope glycoprotein complex-induced apoptosis involves mammalian target of rapamycin/FKBP12-rapamycin-associated protein-mediated p53 phosphorylation. J. Exp. Med. 194, 1097-1110
    • (2001) J. Exp. Med. , vol.194 , pp. 1097-1110
    • Castedo, M.1    Ferri, K.F.2    Blanco, J.3    Roumier, T.4    Larochette, N.5    Barretina, J.6    Amendola, A.7    Nardacci, R.8    Métivier, D.9    Este, J.A.10    Piacentini, M.11    Kroemer, G.12
  • 65
    • 33750079286 scopus 로고    scopus 로고
    • Human immunodeficiency virus gp120-induced apoptosis of human neuroblastoma cells in the absence of CXCR4 internalization
    • Bardi, G., Sengupta, R., Khan, M. Z., Patel, J. P., and Meucci, O. (2006) Human immunodeficiency virus gp120-induced apoptosis of human neuroblastoma cells in the absence of CXCR4 internalization. J. Neurovirol. 12, 211-218
    • (2006) J. Neurovirol. , vol.12 , pp. 211-218
    • Bardi, G.1    Sengupta, R.2    Khan, M.Z.3    Patel, J.P.4    Meucci, O.5
  • 68
    • 0029067663 scopus 로고
    • Synthesis and structure-activity relationships of phenylenebis(methylene)-linked bis-tetraazamacrocycles that inhibit HIV replication Effects of macrocyclic ring size and substituents on the aromatic linker
    • Bridger, G. J., Skerlj, R. T., Thornton, D., Padmanabhan, S., Martellucci, S. A., Henson, G. W., Abrams, M. J., Yamamoto, N., De Vreese, K., and Pauwels, R. (1995) Synthesis and structure-activity relationships of phenylenebis(methylene)-linked bis-tetraazamacrocycles that inhibit HIV replication. Effects of macrocyclic ring size and substituents on the aromatic linker. J. Med. Chem. 38, 366-378
    • (1995) J. Med. Chem. , vol.38 , pp. 366-378
    • Bridger, G.J.1    Skerlj, R.T.2    Thornton, D.3    Padmanabhan, S.4    Martellucci, S.A.5    Henson, G.W.6    Abrams, M.J.7    Yamamoto, N.8    De Vreese, K.9    Pauwels, R.10
  • 70
    • 78249240388 scopus 로고    scopus 로고
    • Mechanisms of HIV envelope-induced T lymphocyte apoptosis
    • Wan, Z. T., and Chen, X. L. (2010) Mechanisms of HIV envelope-induced T lymphocyte apoptosis. Virol. Sin. 25, 307-315
    • (2010) Virol. Sin. , vol.25 , pp. 307-315
    • Wan, Z.T.1    Chen, X.L.2
  • 72
    • 77649137126 scopus 로고    scopus 로고
    • GCP II inhibition rescues neurons from gp120IIIB-induced neurotoxicity
    • Thomas, A. G., Bodner, A., Ghadge, G., Roos, R. P., and Slusher, B. S. (2009) GCP II inhibition rescues neurons from gp120IIIB-induced neurotoxicity. J. Neurovirol. 15, 449-457
    • (2009) J. Neurovirol. , vol.15 , pp. 449-457
    • Thomas, A.G.1    Bodner, A.2    Ghadge, G.3    Roos, R.P.4    Slusher, B.S.5
  • 73
    • 54749113722 scopus 로고    scopus 로고
    • The metabolism of proline as microenvironmental stress substrate
    • Phang, J. M., Pandhare, J., and Liu, Y. (2008) The metabolism of proline as microenvironmental stress substrate. J. Nutr. 138, 2008S-2015S
    • (2008) J. Nutr. , vol.138 , pp. 2008S-2015S
    • Phang, J.M.1    Pandhare, J.2    Liu, Y.3
  • 74
    • 0034700139 scopus 로고    scopus 로고
    • Differential gene expression in p53-mediated apoptosis-resistant vs apoptosis-sensitive tumor cell lines
    • Maxwell, S. A., and Davis, G. E. (2000) Differential gene expression in p53-mediated apoptosis-resistant vs. apoptosis-sensitive tumor cell lines. Proc. Natl. Acad. Sci. U.S.A. 97, 13009-13014
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13009-13014
    • Maxwell, S.A.1    Davis, G.E.2
  • 75
    • 84931958134 scopus 로고    scopus 로고
    • ROS and autophagy: Interactions and molecular regulatory mechanisms
    • Li, L., Tan, J., Miao, Y., Lei, P., and Zhang, Q. (2015) ROS and autophagy: interactions and molecular regulatory mechanisms. Cell Mol Neurobiol. 35, 615-621
    • (2015) Cell Mol Neurobiol. , vol.35 , pp. 615-621
    • Li, L.1    Tan, J.2    Miao, Y.3    Lei, P.4    Zhang, Q.5
  • 76
    • 60749108379 scopus 로고    scopus 로고
    • Regulation of autophagy by reactive oxygen species (ROS): Implications for cancer progression and treatment
    • Azad, M. B., Chen, Y., and Gibson, S. B. (2009) Regulation of autophagy by reactive oxygen species (ROS): implications for cancer progression and treatment. Antioxid. Redox Signal. 11, 777-790
    • (2009) Antioxid. Redox Signal. , vol.11 , pp. 777-790
    • Azad, M.B.1    Chen, Y.2    Gibson, S.B.3
  • 77
    • 84866155363 scopus 로고    scopus 로고
    • Neuronal autophagy: A housekeeper or a fighter in neuronal cell survival?
    • Lee, J. A. (2012) Neuronal autophagy: a housekeeper or a fighter in neuronal cell survival? Exp. Neurobiol. 21, 1-8
    • (2012) Exp. Neurobiol. , vol.21 , pp. 1-8
    • Lee, J.A.1
  • 78
    • 78649299872 scopus 로고    scopus 로고
    • Autophagy in the central nervous system: Implications for neurodegenerative disorders CNS Neurol
    • Xilouri, M., and Stefanis, L. (2010) Autophagy in the central nervous system: implications for neurodegenerative disorders. CNS Neurol. Disord. Drug Targets 9, 701-719
    • (2010) Disord. Drug Targets , vol.9 , pp. 701-719
    • Xilouri, M.1    Stefanis, L.2
  • 80
    • 44149124887 scopus 로고    scopus 로고
    • Autophagy in neuroprotection and neurodegeneration: A question of balance
    • 3rd
    • Cherra, S. J., 3rd, and Chu, C. T. (2008) Autophagy in neuroprotection and neurodegeneration: A question of balance. Future Neurol. 3, 309-323
    • (2008) Future Neurol. , Issue.3 , pp. 309-323
    • Cherra, S.J.1    Chu, C.T.2
  • 81
    • 79956204926 scopus 로고    scopus 로고
    • Autophagy is increased in postmortem brains of persons with HIV-1-associated encephalitis
    • Zhou, D., Masliah, E., and Spector, S. A. (2011) Autophagy is increased in postmortem brains of persons with HIV-1-associated encephalitis. J. Infect. Dis. 203, 1647-1657
    • (2011) J. Infect.Dis. , vol.203 , pp. 1647-1657
    • Zhou, D.1    Masliah, E.2    Spector, S.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.