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Volumn 38, Issue 2, 2012, Pages 175-200

Activation status of integrated stress response pathways in neurones and astrocytes of HIV-associated neurocognitive disorders (HAND) cortex

Author keywords

Astrocyte; ATF6; ER stress response; HAND; HIV; Neurone

Indexed keywords

ACTIVATING TRANSCRIPTION FACTOR 4; ACTIVATING TRANSCRIPTION FACTOR 6; ACTIVATING TRANSCRIPTION FACTOR 6 BETA; INITIATION FACTOR 2ALPHA; PROTEIN IRE1; PROTEIN IRE1 ALPHA; UNCLASSIFIED DRUG;

EID: 84863229175     PISSN: 03051846     EISSN: 13652990     Source Type: Journal    
DOI: 10.1111/j.1365-2990.2011.01215.x     Document Type: Article
Times cited : (36)

References (101)
  • 1
    • 32944458278 scopus 로고    scopus 로고
    • Implementing an employee portal. Taking steps toward a 'paperless' future
    • Akay L, Coye MJ. Implementing an employee portal. Taking steps toward a 'paperless' future. Healthplan 2001; 42: 66-9
    • (2001) Healthplan , vol.42 , pp. 66-69
    • Akay, L.1    Coye, M.J.2
  • 4
    • 2142708770 scopus 로고    scopus 로고
    • Astrocyte infection by HIV-1: mechanisms of restricted virus replication, and role in the pathogenesis of HIV-1-associated dementia
    • Gorry PR, Ong C, Thorpe J, Bannwarth S, Thompson KA, Gatignol A, Vesselingh SL, Purcell DF. Astrocyte infection by HIV-1: mechanisms of restricted virus replication, and role in the pathogenesis of HIV-1-associated dementia. Curr HIV Res 2003; 1: 463-73
    • (2003) Curr HIV Res , vol.1 , pp. 463-473
    • Gorry, P.R.1    Ong, C.2    Thorpe, J.3    Bannwarth, S.4    Thompson, K.A.5    Gatignol, A.6    Vesselingh, S.L.7    Purcell, D.F.8
  • 5
    • 22744455058 scopus 로고    scopus 로고
    • HIV-1 infection and AIDS: consequences for the central nervous system
    • Kaul M, Zheng J, Okamoto S, Gendelman HE, Lipton SA. HIV-1 infection and AIDS: consequences for the central nervous system. Cell Death Differ 2005; 12 (Suppl. 1): 878-92
    • (2005) Cell Death Differ , vol.12 , Issue.1 SUPPL. , pp. 878-892
    • Kaul, M.1    Zheng, J.2    Okamoto, S.3    Gendelman, H.E.4    Lipton, S.A.5
  • 6
    • 22244484446 scopus 로고    scopus 로고
    • Molecular mechanisms of HIV-1 associated neurodegeneration
    • Ozdener H. Molecular mechanisms of HIV-1 associated neurodegeneration. J Biosci 2005; 30: 391-405
    • (2005) J Biosci , vol.30 , pp. 391-405
    • Ozdener, H.1
  • 8
    • 0038136866 scopus 로고    scopus 로고
    • Pathogenesis of human immunodeficiency virus-induced neurological disease
    • Albright AV, Soldan SS, Gonzalez-Scarano F. Pathogenesis of human immunodeficiency virus-induced neurological disease. J Neurovirol 2003; 9: 222-7
    • (2003) J Neurovirol , vol.9 , pp. 222-227
    • Albright, A.V.1    Soldan, S.S.2    Gonzalez-Scarano, F.3
  • 10
    • 0036853914 scopus 로고    scopus 로고
    • Orchestrating the unfolded protein response in health and disease
    • Kaufman RJ. Orchestrating the unfolded protein response in health and disease. J Clin Invest 2002; 110: 1389-98
    • (2002) J Clin Invest , vol.110 , pp. 1389-1398
    • Kaufman, R.J.1
  • 12
    • 0028339518 scopus 로고
    • Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus
    • Hammond C, Helenius A. Quality control in the secretory pathway: retention of a misfolded viral membrane glycoprotein involves cycling between the ER, intermediate compartment, and Golgi apparatus. J Cell Biol 1994; 126: 41-52
    • (1994) J Cell Biol , vol.126 , pp. 41-52
    • Hammond, C.1    Helenius, A.2
  • 13
    • 0029851855 scopus 로고    scopus 로고
    • Disturbances of calcium homeostasis within the endoplasmic reticulum may contribute to the development of ischemic-cell damage. [Review][57 refs]
    • Paschen W. Disturbances of calcium homeostasis within the endoplasmic reticulum may contribute to the development of ischemic-cell damage. [Review][57 refs]. Med Hypotheses 1996; 47: 283-8
    • (1996) Med Hypotheses , vol.47 , pp. 283-288
    • Paschen, W.1
  • 14
    • 10444226462 scopus 로고    scopus 로고
    • ER stress and the unfolded protein response. [Review][328 refs]
    • Schroder M, Kaufman RJ. ER stress and the unfolded protein response. [Review][328 refs]. Mutat Res 2005; 569: 29-63
    • (2005) Mutat Res , vol.569 , pp. 29-63
    • Schroder, M.1    Kaufman, R.J.2
  • 15
    • 33748667752 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and neurodegeneration in rats neonatally infected with borna disease virus
    • Williams BL, Lipkin WI. Endoplasmic reticulum stress and neurodegeneration in rats neonatally infected with borna disease virus. J Virol 2006; 80: 8613-26
    • (2006) J Virol , vol.80 , pp. 8613-8626
    • Williams, B.L.1    Lipkin, W.I.2
  • 16
    • 2942755868 scopus 로고    scopus 로고
    • Signaling the unfolded protein response from the endoplasmic reticulum. [Review][60 refs]
    • Zhang K, Kaufman RJ. Signaling the unfolded protein response from the endoplasmic reticulum. [Review][60 refs]. J Biol Chem 2004; 279: 25935-8
    • (2004) J Biol Chem , vol.279 , pp. 25935-25938
    • Zhang, K.1    Kaufman, R.J.2
  • 17
    • 0036437307 scopus 로고    scopus 로고
    • Transcriptional and translational control in the Mammalian unfolded protein response. [Review][95 refs]
    • Harding HP, Calfon M, Urano F, Novoa I, Ron D. Transcriptional and translational control in the Mammalian unfolded protein response. [Review][95 refs]. Annu Rev Cell Dev Biol 2002; 18: 575-99
    • (2002) Annu Rev Cell Dev Biol , vol.18 , pp. 575-599
    • Harding, H.P.1    Calfon, M.2    Urano, F.3    Novoa, I.4    Ron, D.5
  • 18
    • 0033562966 scopus 로고    scopus 로고
    • Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. [Review][186 refs]
    • Kaufman RJ. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. [Review][186 refs]. Genes Dev 1999; 13: 1211-33
    • (1999) Genes Dev , vol.13 , pp. 1211-1233
    • Kaufman, R.J.1
  • 19
    • 77957944422 scopus 로고    scopus 로고
    • human cytomegalovirus induces the endoplasmic reticulum chaperone BiP through increased transcription and activation of translation by using the BiP internal ribosome entry site
    • Buchkovich NJ, Yu Y, Pierciey FJ, Alwine JC. human cytomegalovirus induces the endoplasmic reticulum chaperone BiP through increased transcription and activation of translation by using the BiP internal ribosome entry site. J Virol 2010; 84: 11479-86
    • (2010) J Virol , vol.84 , pp. 11479-11486
    • Buchkovich, N.J.1    Yu, Y.2    Pierciey, F.J.3    Alwine, J.C.4
  • 20
    • 13744253138 scopus 로고    scopus 로고
    • Herpes simplex virus 1 infection activates the endoplasmic reticulum resident kinase PERK and mediates eIF-2 dephosphorylation by the 134.5 protein
    • Cheng G, Feng Z, He B. Herpes simplex virus 1 infection activates the endoplasmic reticulum resident kinase PERK and mediates eIF-2 dephosphorylation by the 134.5 protein. J Virol 2005; 79: 1379-88
    • (2005) J Virol , vol.79 , pp. 1379-1388
    • Cheng, G.1    Feng, Z.2    He, B.3
  • 21
    • 77954144139 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress is induced and modulated by enterovirus 71
    • Jheng J-R, Lau KS, Tang W-F, Wu M-S, Horng J-T. Endoplasmic reticulum stress is induced and modulated by enterovirus 71. Cell Microbiol 2010; 12: 796-813
    • (2010) Cell Microbiol , vol.12 , pp. 796-813
    • Jheng, J.-R.1    Lau, K.S.2    Tang, W.-F.3    Wu, M.-S.4    Horng, J.-T.5
  • 22
    • 33947428335 scopus 로고    scopus 로고
    • Maintenance of endoplasmic reticulum (ER) homeostasis in herpes simplex virus type 1-infected cells through the association of a viral glycoprotein with PERK, a cellular ER stress sensor
    • Mulvey M, Arias C, Mohr I. Maintenance of endoplasmic reticulum (ER) homeostasis in herpes simplex virus type 1-infected cells through the association of a viral glycoprotein with PERK, a cellular ER stress sensor. J Virol 2007; 81: 3377-90
    • (2007) J Virol , vol.81 , pp. 3377-3390
    • Mulvey, M.1    Arias, C.2    Mohr, I.3
  • 23
    • 4544359254 scopus 로고    scopus 로고
    • African swine fever virus inhibits induction of the stress-induced proapoptotic transcription factor CHOP/GADD153
    • Netherton CL, Parsley JC, Wileman T. African swine fever virus inhibits induction of the stress-induced proapoptotic transcription factor CHOP/GADD153. J Virol 2004; 78: 10825-8
    • (2004) J Virol , vol.78 , pp. 10825-10828
    • Netherton, C.L.1    Parsley, J.C.2    Wileman, T.3
  • 24
    • 77956268335 scopus 로고    scopus 로고
    • The HPV-16 E5 protein represses expression of stress pathway genes XBP-1 and COX-2 in genital keratinocytes
    • Sudarshan SR, Schlegel R, Liu X. The HPV-16 E5 protein represses expression of stress pathway genes XBP-1 and COX-2 in genital keratinocytes. Biochem Biophys Res Commun 2010; 399: 617-22
    • (2010) Biochem Biophys Res Commun , vol.399 , pp. 617-622
    • Sudarshan, S.R.1    Schlegel, R.2    Liu, X.3
  • 25
    • 0036314483 scopus 로고    scopus 로고
    • Virus subgenomic replicons induce endoplasmic reticulum stress activating an intracellular signaling pathway
    • Tardif KD, Mori K, Siddiqui A, Hepatitis C. Virus subgenomic replicons induce endoplasmic reticulum stress activating an intracellular signaling pathway. J Virol 2002; 76: 7453-9
    • (2002) J Virol , vol.76 , pp. 7453-7459
    • Tardif, K.D.1    Mori, K.2    Siddiqui, A.3    Hepatitis, C.4
  • 26
    • 64049088651 scopus 로고    scopus 로고
    • Human cytomegalovirus protein pUL38 induces ATF4 expression, inhibits persistent JNK phosphorylation, and suppresses endoplasmic reticulum stress-induced cell death
    • Xuan B, Qian Z, Torigoi E, Yu D. Human cytomegalovirus protein pUL38 induces ATF4 expression, inhibits persistent JNK phosphorylation, and suppresses endoplasmic reticulum stress-induced cell death. J Virol 2009; 83: 3463-74
    • (2009) J Virol , vol.83 , pp. 3463-3474
    • Xuan, B.1    Qian, Z.2    Torigoi, E.3    Yu, D.4
  • 27
    • 77956642651 scopus 로고    scopus 로고
    • Coxsackievirus B3 infection activates the unfolded protein response and induces apoptosis through downregulation of p58IPK and activation of CHOP and SREBP1
    • Zhang HM, Ye X, Su Y, Yuan J, Liu Z, Stein DA, Yang D. Coxsackievirus B3 infection activates the unfolded protein response and induces apoptosis through downregulation of p58IPK and activation of CHOP and SREBP1. J Virol 2010; 84: 8446-59
    • (2010) J Virol , vol.84 , pp. 8446-8459
    • Zhang, H.M.1    Ye, X.2    Su, Y.3    Yuan, J.4    Liu, Z.5    Stein, D.A.6    Yang, D.7
  • 28
    • 79952407316 scopus 로고    scopus 로고
    • West Nile virus differentially modulates the unfolded protein response to facilitate replication and immune evasion
    • Ambrose RL, Mackenzie JM. West Nile virus differentially modulates the unfolded protein response to facilitate replication and immune evasion. J Virol 2010; 85: 2723-32
    • (2010) J Virol , vol.85 , pp. 2723-2732
    • Ambrose, R.L.1    Mackenzie, J.M.2
  • 30
    • 18844419215 scopus 로고    scopus 로고
    • Human cytomegalovirus infection activates and regulates the unfolded protein response
    • Isler JA, Skalet AH, Alwine JC. Human cytomegalovirus infection activates and regulates the unfolded protein response. J Virol 2005; 79: 6890-9
    • (2005) J Virol , vol.79 , pp. 6890-6899
    • Isler, J.A.1    Skalet, A.H.2    Alwine, J.C.3
  • 31
    • 2342435179 scopus 로고    scopus 로고
    • Hepatitis C virus suppresses the IRE1-XBP1 Pathway of the unfolded protein response
    • Tardif KD. Hepatitis C virus suppresses the IRE1-XBP1 Pathway of the unfolded protein response. J Biol Chem 2004; 279: 17158-64
    • (2004) J Biol Chem , vol.279 , pp. 17158-17164
    • Tardif, K.D.1
  • 32
    • 30744475504 scopus 로고    scopus 로고
    • Hepatitis C virus non-structural protein NS4B can modulate an unfolded protein response
    • Zheng Y, Gao B, Ye L, Kong L, Jing W, Yang X, Wu Z. Hepatitis C virus non-structural protein NS4B can modulate an unfolded protein response. J Microbiol 2005; 43: 529-36
    • (2005) J Microbiol , vol.43 , pp. 529-536
    • Zheng, Y.1    Gao, B.2    Ye, L.3    Kong, L.4    Jing, W.5    Yang, X.6    Wu, Z.7
  • 33
    • 33748502744 scopus 로고    scopus 로고
    • Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein
    • Chan CP, Siu KL, Chin KT, Yuen KY, Zheng B, Jin DY. Modulation of the unfolded protein response by the severe acute respiratory syndrome coronavirus spike protein. J Virol 2006; 80: 9279-87
    • (2006) J Virol , vol.80 , pp. 9279-9287
    • Chan, C.P.1    Siu, K.L.2    Chin, K.T.3    Yuen, K.Y.4    Zheng, B.5    Jin, D.Y.6
  • 35
    • 1042278009 scopus 로고    scopus 로고
    • Brain trauma induces X-box protein 1 processing indicative of activation of the endoplasmic reticulum unfolded protein response
    • Paschen W, Yatsiv I, Shoham S, Shohami E. Brain trauma induces X-box protein 1 processing indicative of activation of the endoplasmic reticulum unfolded protein response. J Neurochem 2004; 88: 983-92
    • (2004) J Neurochem , vol.88 , pp. 983-992
    • Paschen, W.1    Yatsiv, I.2    Shoham, S.3    Shohami, E.4
  • 36
    • 30444432257 scopus 로고    scopus 로고
    • CHOP plays a pivotal role in the astrocyte death induced by oxygen and glucose deprivation
    • Benavides A, Pastor D, Santos P, Tranque P, Calvo S. CHOP plays a pivotal role in the astrocyte death induced by oxygen and glucose deprivation. Glia 2005; 52: 261-75
    • (2005) Glia , vol.52 , pp. 261-275
    • Benavides, A.1    Pastor, D.2    Santos, P.3    Tranque, P.4    Calvo, S.5
  • 37
    • 33646860572 scopus 로고    scopus 로고
    • Prolonged bihemispheric alterations in unfolded protein response related gene expression after experimental stroke
    • Rissanen A, Sivenius J, Jolkkonen J. Prolonged bihemispheric alterations in unfolded protein response related gene expression after experimental stroke. Brain Res 2006; 1087: 60-6
    • (2006) Brain Res , vol.1087 , pp. 60-66
    • Rissanen, A.1    Sivenius, J.2    Jolkkonen, J.3
  • 38
    • 0034610743 scopus 로고    scopus 로고
    • Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta
    • Nakagawa T, Zhu H, Morishima N, Li E, Xu J, Yankner BA, Yuan J. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta. Nature 2000; 403: 98-103
    • (2000) Nature , vol.403 , pp. 98-103
    • Nakagawa, T.1    Zhu, H.2    Morishima, N.3    Li, E.4    Xu, J.5    Yankner, B.A.6    Yuan, J.7
  • 39
    • 0035967883 scopus 로고    scopus 로고
    • An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin
    • Imai Y, Soda M, Inoue H, Hattori N, Mizuno Y, Takahashi R. An unfolded putative transmembrane polypeptide, which can lead to endoplasmic reticulum stress, is a substrate of Parkin. Cell 2001; 105: 891-902
    • (2001) Cell , vol.105 , pp. 891-902
    • Imai, Y.1    Soda, M.2    Inoue, H.3    Hattori, N.4    Mizuno, Y.5    Takahashi, R.6
  • 40
    • 0037114971 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease
    • Ryu EJ, Harding HP, Angelastro JM, Vitolo OV, Ron D, Greene LA. Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson's disease. J Neurosci 2002; 22: 10690-8
    • (2002) J Neurosci , vol.22 , pp. 10690-10698
    • Ryu, E.J.1    Harding, H.P.2    Angelastro, J.M.3    Vitolo, O.V.4    Ron, D.5    Greene, L.A.6
  • 41
    • 0035144493 scopus 로고    scopus 로고
    • Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state
    • McCullough KD, Martindale JL, Klotz L-O, Aw T-Y, Holbrook NJ. Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol Cell Biol 2001; 21: 1249-59
    • (2001) Mol Cell Biol , vol.21 , pp. 1249-1259
    • McCullough, K.D.1    Martindale, J.L.2    Klotz, L.-O.3    Aw, T.-Y.4    Holbrook, N.J.5
  • 45
    • 79955666781 scopus 로고    scopus 로고
    • Parallel high throughput neuronal toxicity assays demonstrate uncoupling between loss of mitochondrial membrane potential and neuronal damage in a model of HIV-induced neurodegeneration
    • White MG, Wang Y, Akay C, Lindl KA, Kolson DL, Jordan-Sciutto KL. Parallel high throughput neuronal toxicity assays demonstrate uncoupling between loss of mitochondrial membrane potential and neuronal damage in a model of HIV-induced neurodegeneration. Neurosci Res 2011; 70: 220-9
    • (2011) Neurosci Res , vol.70 , pp. 220-229
    • White, M.G.1    Wang, Y.2    Akay, C.3    Lindl, K.A.4    Kolson, D.L.5    Jordan-Sciutto, K.L.6
  • 46
    • 77953917265 scopus 로고    scopus 로고
    • E2F1 localizes predominantly to neuronal cytoplasm and fails to induce expression of its transcriptional targets in human immunodeficiency virus-induced neuronal damage
    • Wang Y, Shyam N, Ting JH, Akay C, Lindl KA, Jordan-Sciutto KL. E2F1 localizes predominantly to neuronal cytoplasm and fails to induce expression of its transcriptional targets in human immunodeficiency virus-induced neuronal damage. Neurosci Lett 2010; 479: 97-101
    • (2010) Neurosci Lett , vol.479 , pp. 97-101
    • Wang, Y.1    Shyam, N.2    Ting, J.H.3    Akay, C.4    Lindl, K.A.5    Jordan-Sciutto, K.L.6
  • 47
    • 35348951126 scopus 로고    scopus 로고
    • How transmembrane proteins sense endoplasmic reticulum stress
    • Kohno K. How transmembrane proteins sense endoplasmic reticulum stress. Antioxid Redox Signal 2007; 9: 2295-303
    • (2007) Antioxid Redox Signal , vol.9 , pp. 2295-2303
    • Kohno, K.1
  • 48
    • 0032693671 scopus 로고    scopus 로고
    • Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress
    • Haze K, Yoshida H, Yanagi H, Yura T, Mori K. Mammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stress. Mol Biol Cell 1999; 10: 3787-99
    • (1999) Mol Biol Cell , vol.10 , pp. 3787-3799
    • Haze, K.1    Yoshida, H.2    Yanagi, H.3    Yura, T.4    Mori, K.5
  • 49
    • 32544446451 scopus 로고    scopus 로고
    • Coping with stress: eIF2 kinases and translational control
    • Wek RC, Jiang HY, Anthony TG. Coping with stress: eIF2 kinases and translational control. Biochem Soc Trans 2006; 34: 7-11
    • (2006) Biochem Soc Trans , vol.34 , pp. 7-11
    • Wek, R.C.1    Jiang, H.Y.2    Anthony, T.G.3
  • 51
    • 9644272621 scopus 로고    scopus 로고
    • HIV dementia: an evolving disease
    • McArthur JC. HIV dementia: an evolving disease. J Neuroimmunol 2004; 157: 3-10
    • (2004) J Neuroimmunol , vol.157 , pp. 3-10
    • McArthur, J.C.1
  • 52
    • 35948964891 scopus 로고    scopus 로고
    • Expression of the endoplasmic reticulum stress response marker, BiP, in the central nervous system of HIV-positive individuals
    • Lindl KA, Akay C, Wang Y, White MG, Jordan-Sciutto KL. Expression of the endoplasmic reticulum stress response marker, BiP, in the central nervous system of HIV-positive individuals. Neuropathol Appl Neurobiol 2007; 33: 658-69
    • (2007) Neuropathol Appl Neurobiol , vol.33 , pp. 658-669
    • Lindl, K.A.1    Akay, C.2    Wang, Y.3    White, M.G.4    Jordan-Sciutto, K.L.5
  • 53
    • 34548010305 scopus 로고    scopus 로고
    • Differential requirement of unfolded protein response pathway for calreticulin expression in Caenorhabditis elegans
    • Lee D, Singaravelu G, Park BJ, Ahnn J. Differential requirement of unfolded protein response pathway for calreticulin expression in Caenorhabditis elegans. J Mol Biol 2007; 372: 331-40
    • (2007) J Mol Biol , vol.372 , pp. 331-340
    • Lee, D.1    Singaravelu, G.2    Park, B.J.3    Ahnn, J.4
  • 54
    • 9144228073 scopus 로고    scopus 로고
    • Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II
    • Yamamoto K, Yoshida H, Kokame K, Kaufman RJ, Mori K. Differential contributions of ATF6 and XBP1 to the activation of endoplasmic reticulum stress-responsive cis-acting elements ERSE, UPRE and ERSE-II. J Biochem 2004; 136: 343-50
    • (2004) J Biochem , vol.136 , pp. 343-350
    • Yamamoto, K.1    Yoshida, H.2    Kokame, K.3    Kaufman, R.J.4    Mori, K.5
  • 55
    • 59849090708 scopus 로고    scopus 로고
    • Transcriptional induction of the human asparagine synthetase gene during the unfolded protein response does not require the ATF6 and IRE1/XBP1 arms of the pathway
    • Gjymishka A, Su N, Kilberg MS. Transcriptional induction of the human asparagine synthetase gene during the unfolded protein response does not require the ATF6 and IRE1/XBP1 arms of the pathway. Biochem J 2009; 417: 695-703
    • (2009) Biochem J , vol.417 , pp. 695-703
    • Gjymishka, A.1    Su, N.2    Kilberg, M.S.3
  • 56
    • 79953192507 scopus 로고    scopus 로고
    • Endoplasmic Reticulum stress induced by Hepatitis B virus X protein enhances cyclooxygenase 2 expression via activating transcription factor-4
    • Cho HK, Cheong KJ, Kim HY, Cheong J. Endoplasmic Reticulum stress induced by Hepatitis B virus X protein enhances cyclooxygenase 2 expression via activating transcription factor-4. Biochem J 2011; 435: 431-9
    • (2011) Biochem J , vol.435 , pp. 431-439
    • Cho, H.K.1    Cheong, K.J.2    Kim, H.Y.3    Cheong, J.4
  • 57
    • 79958061881 scopus 로고    scopus 로고
    • AAV exploits subcellular stress associated with inflammation, endoplasmic reticulum expansion, and misfolded proteins in models of cystic fibrosis
    • Johnson JS, Gentzsch M, Zhang L, Ribeiro CM, Kantor B, Kafri T, Pickles RJ, Samulski RJ. AAV exploits subcellular stress associated with inflammation, endoplasmic reticulum expansion, and misfolded proteins in models of cystic fibrosis. PLoS Pathog 2011; 7: e1002053
    • (2011) PLoS Pathog , vol.7
    • Johnson, J.S.1    Gentzsch, M.2    Zhang, L.3    Ribeiro, C.M.4    Kantor, B.5    Kafri, T.6    Pickles, R.J.7    Samulski, R.J.8
  • 58
    • 79953089155 scopus 로고    scopus 로고
    • Japanese encephalitis virus co-opts the ER-stress response protein GRP78 for viral infectivity
    • Wu Y-P, Chang C-M, Hung C-Y, Tsai M-C, Schuyler SC, Wang R. Japanese encephalitis virus co-opts the ER-stress response protein GRP78 for viral infectivity. Virol J 2011; 8: 128
    • (2011) Virol J , vol.8 , pp. 128
    • Wu, Y.-P.1    Chang, C.-M.2    Hung, C.-Y.3    Tsai, M.-C.4    Schuyler, S.C.5    Wang, R.6
  • 59
    • 0026710871 scopus 로고
    • IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae
    • Nikawa J, Yamashita S. IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae. Mol Microbiol 1992; 6: 1441-6
    • (1992) Mol Microbiol , vol.6 , pp. 1441-1446
    • Nikawa, J.1    Yamashita, S.2
  • 60
    • 0027324844 scopus 로고
    • Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase
    • Cox JS, Shamu CE, Walter P. Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase. Cell 1993; 73: 1197-206
    • (1993) Cell , vol.73 , pp. 1197-1206
    • Cox, J.S.1    Shamu, C.E.2    Walter, P.3
  • 61
    • 0034282912 scopus 로고    scopus 로고
    • Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response
    • Wang Y, Shen J, Arenzana N, Tirasophon W, Kaufman RJ, Prywes R. Activation of ATF6 and an ATF6 DNA binding site by the endoplasmic reticulum stress response. J Biol Chem 2000; 275: 27013-20
    • (2000) J Biol Chem , vol.275 , pp. 27013-27020
    • Wang, Y.1    Shen, J.2    Arenzana, N.3    Tirasophon, W.4    Kaufman, R.J.5    Prywes, R.6
  • 62
    • 0033920261 scopus 로고    scopus 로고
    • ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1
    • Li M, Baumeister P, Roy B, Phan T, Foti D, Luo S, Lee AS. ATF6 as a transcription activator of the endoplasmic reticulum stress element: thapsigargin stress-induced changes and synergistic interactions with NF-Y and YY1. Mol Cell Biol 2000; 20: 5096-106
    • (2000) Mol Cell Biol , vol.20 , pp. 5096-5106
    • Li, M.1    Baumeister, P.2    Roy, B.3    Phan, T.4    Foti, D.5    Luo, S.6    Lee, A.S.7
  • 63
    • 0037083755 scopus 로고    scopus 로고
    • IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response
    • Lee K, Tirasophon W, Shen X, Michalak M, Prywes R, Okada T, Yoshida H, Mori K, Kaufman RJ. IRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein response. Genes Dev 2002; 16: 452-66
    • (2002) Genes Dev , vol.16 , pp. 452-466
    • Lee, K.1    Tirasophon, W.2    Shen, X.3    Michalak, M.4    Prywes, R.5    Okada, T.6    Yoshida, H.7    Mori, K.8    Kaufman, R.J.9
  • 65
    • 0036069980 scopus 로고    scopus 로고
    • ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals
    • Shen J, Chen X, Hendershot L, Prywes R. ER stress regulation of ATF6 localization by dissociation of BiP/GRP78 binding and unmasking of Golgi localization signals. Dev Cell 2002; 3: 99-111
    • (2002) Dev Cell , vol.3 , pp. 99-111
    • Shen, J.1    Chen, X.2    Hendershot, L.3    Prywes, R.4
  • 66
    • 0037066741 scopus 로고    scopus 로고
    • The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi
    • Chen X, Shen J, Prywes R. The luminal domain of ATF6 senses endoplasmic reticulum (ER) stress and causes translocation of ATF6 from the ER to the Golgi. J Biol Chem 2002; 277: 13045-52
    • (2002) J Biol Chem , vol.277 , pp. 13045-13052
    • Chen, X.1    Shen, J.2    Prywes, R.3
  • 70
    • 0041731803 scopus 로고    scopus 로고
    • A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6
    • Okada T, Haze K, Nadanaka S, Yoshida H, Seidah NG, Hirano Y, Sato R, Negishi M, Mori K. A serine protease inhibitor prevents endoplasmic reticulum stress-induced cleavage but not transport of the membrane-bound transcription factor ATF6. J Biol Chem 2003; 278: 31024-32
    • (2003) J Biol Chem , vol.278 , pp. 31024-31032
    • Okada, T.1    Haze, K.2    Nadanaka, S.3    Yoshida, H.4    Seidah, N.G.5    Hirano, Y.6    Sato, R.7    Negishi, M.8    Mori, K.9
  • 72
    • 0028087833 scopus 로고
    • Somatic cell genetic and biochemical characterization of cell lines resulting from human genomic DNA transfections of Chinese hamster ovary cell mutants defective in sterol-dependent activation of sterol synthesis and LDL receptor expression
    • Hasan MT, Chang CC, Chang TY. Somatic cell genetic and biochemical characterization of cell lines resulting from human genomic DNA transfections of Chinese hamster ovary cell mutants defective in sterol-dependent activation of sterol synthesis and LDL receptor expression. Somat Cell Mol Genet 1994; 20: 183-94
    • (1994) Somat Cell Mol Genet , vol.20 , pp. 183-194
    • Hasan, M.T.1    Chang, C.C.2    Chang, T.Y.3
  • 74
    • 33846201752 scopus 로고    scopus 로고
    • Analysis of ATF6 activation in Site-2 protease-deficient Chinese hamster ovary cells
    • Nadanaka S, Yoshida H, Sato R, Mori K. Analysis of ATF6 activation in Site-2 protease-deficient Chinese hamster ovary cells. Cell Struct Funct 2006; 31: 109-16
    • (2006) Cell Struct Funct , vol.31 , pp. 109-116
    • Nadanaka, S.1    Yoshida, H.2    Sato, R.3    Mori, K.4
  • 75
    • 79959332937 scopus 로고    scopus 로고
    • Treatment of acute hepatitis C infection in HIV-infected patients
    • Boesecke C, Rockstroh JK. Treatment of acute hepatitis C infection in HIV-infected patients. Curr Opin HIV AIDS 2011; 6: 278-84
    • (2011) Curr Opin HIV AIDS , vol.6 , pp. 278-284
    • Boesecke, C.1    Rockstroh, J.K.2
  • 77
    • 59649084874 scopus 로고    scopus 로고
    • Impact and management of hepatitis B and hepatitis C virus co-infection in HIV patients
    • Kumar R, Singla V, Kacharya S. Impact and management of hepatitis B and hepatitis C virus co-infection in HIV patients. Trop Gastroenterol 2008; 29: 136-47
    • (2008) Trop Gastroenterol , vol.29 , pp. 136-147
    • Kumar, R.1    Singla, V.2    Kacharya, S.3
  • 78
    • 0042132023 scopus 로고    scopus 로고
    • HIV/HBV and HIV/HCV coinfection, and outcomes following highly active antiretroviral therapy
    • Lincoln D, Petoumenos K, Dore GJ. HIV/HBV and HIV/HCV coinfection, and outcomes following highly active antiretroviral therapy. HIV Med 2003; 4: 241-9
    • (2003) HIV Med , vol.4 , pp. 241-249
    • Lincoln, D.1    Petoumenos, K.2    Dore, G.J.3
  • 81
    • 34547933706 scopus 로고    scopus 로고
    • Effects of the isoform-specific characteristics of ATF6 alpha and ATF6 beta on endoplasmic reticulum stress response gene expression and cell viability
    • Thuerauf DJ, Marcinko M, Belmont PJ, Glembotski CC. Effects of the isoform-specific characteristics of ATF6 alpha and ATF6 beta on endoplasmic reticulum stress response gene expression and cell viability. J Biol Chem 2007; 282: 22865-78
    • (2007) J Biol Chem , vol.282 , pp. 22865-22878
    • Thuerauf, D.J.1    Marcinko, M.2    Belmont, P.J.3    Glembotski, C.C.4
  • 82
    • 2442647920 scopus 로고    scopus 로고
    • Opposing roles for ATF6alpha and ATF6beta in endoplasmic reticulum stress response gene induction
    • Thuerauf DJ, Morrison L, Glembotski CC. Opposing roles for ATF6alpha and ATF6beta in endoplasmic reticulum stress response gene induction. J Biol Chem 2004; 279: 21078-84
    • (2004) J Biol Chem , vol.279 , pp. 21078-21084
    • Thuerauf, D.J.1    Morrison, L.2    Glembotski, C.C.3
  • 83
    • 70350463523 scopus 로고    scopus 로고
    • N-glycosylation of ATF6beta is essential for its proteolytic cleavage and transcriptional repressor function to ATF6alpha
    • Guan D, Wang H, Li VE, Xu Y, Yang M, Shen Z. N-glycosylation of ATF6beta is essential for its proteolytic cleavage and transcriptional repressor function to ATF6alpha. J Cell Biochem 2009; 108: 825-31
    • (2009) J Cell Biochem , vol.108 , pp. 825-831
    • Guan, D.1    Wang, H.2    Li, V.E.3    Xu, Y.4    Yang, M.5    Shen, Z.6
  • 84
    • 34548172495 scopus 로고    scopus 로고
    • Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1
    • Yamamoto K, Sato T, Matsui T, Sato M, Okada T, Yoshida H, Harada A, Mori K. Transcriptional induction of mammalian ER quality control proteins is mediated by single or combined action of ATF6alpha and XBP1. Dev Cell 2007; 13: 365-76
    • (2007) Dev Cell , vol.13 , pp. 365-376
    • Yamamoto, K.1    Sato, T.2    Matsui, T.3    Sato, M.4    Okada, T.5    Yoshida, H.6    Harada, A.7    Mori, K.8
  • 85
    • 16644375815 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress triggers an acute proteasome-dependent degradation of ATF6
    • Hong M, Li M, Mao C, Lee AS. Endoplasmic reticulum stress triggers an acute proteasome-dependent degradation of ATF6. J Cell Biochem 2004; 92: 723-32
    • (2004) J Cell Biochem , vol.92 , pp. 723-732
    • Hong, M.1    Li, M.2    Mao, C.3    Lee, A.S.4
  • 87
    • 33751247922 scopus 로고    scopus 로고
    • Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress
    • Yu CY, Hsu YW, Liao CL, Lin YL. Flavivirus infection activates the XBP1 pathway of the unfolded protein response to cope with endoplasmic reticulum stress. J Virol 2006; 80: 11868-80
    • (2006) J Virol , vol.80 , pp. 11868-11880
    • Yu, C.Y.1    Hsu, Y.W.2    Liao, C.L.3    Lin, Y.L.4
  • 88
    • 77953763317 scopus 로고    scopus 로고
    • Semliki forest virus-induced endoplasmic reticulum stress accelerates apoptotic death of mammalian cells
    • Barry G, Fragkoudis R, Ferguson MC, Lulla A, Merits A, Kohl A, Fazakerley JK. Semliki forest virus-induced endoplasmic reticulum stress accelerates apoptotic death of mammalian cells. J Virol 2010; 84: 7369-77
    • (2010) J Virol , vol.84 , pp. 7369-7377
    • Barry, G.1    Fragkoudis, R.2    Ferguson, M.C.3    Lulla, A.4    Merits, A.5    Kohl, A.6    Fazakerley, J.K.7
  • 89
    • 60149091189 scopus 로고    scopus 로고
    • Regulation of translation initiation in eukaryotes: mechanisms and biological targets
    • Sonenberg N, Hinnebusch AG. Regulation of translation initiation in eukaryotes: mechanisms and biological targets. Cell 2009; 136: 731-45
    • (2009) Cell , vol.136 , pp. 731-745
    • Sonenberg, N.1    Hinnebusch, A.G.2
  • 91
    • 21244431682 scopus 로고    scopus 로고
    • Internal ribosome entry sites in cellular mRNAs: mystery of their existence
    • Komar AA, Hatzoglou M. Internal ribosome entry sites in cellular mRNAs: mystery of their existence. J Biol Chem 2005; 280: 23425-8
    • (2005) J Biol Chem , vol.280 , pp. 23425-23428
    • Komar, A.A.1    Hatzoglou, M.2
  • 94
    • 73349141743 scopus 로고    scopus 로고
    • Adaptive suppression of the ATF4-CHOP branch of the unfolded protein response by toll-like receptor signalling
    • Woo CW, Cui D, Arellano J, Dorweiler B, Harding H, Fitzgerald KA, Ron D, Tabas I. Adaptive suppression of the ATF4-CHOP branch of the unfolded protein response by toll-like receptor signalling. Nat Cell Biol 2009; 11: 1473-80
    • (2009) Nat Cell Biol , vol.11 , pp. 1473-1480
    • Woo, C.W.1    Cui, D.2    Arellano, J.3    Dorweiler, B.4    Harding, H.5    Fitzgerald, K.A.6    Ron, D.7    Tabas, I.8
  • 95
    • 77958472998 scopus 로고    scopus 로고
    • Both transcriptional regulation and translational control of ATF4 are central to the integrated stress response
    • Dey S, Baird TD, Zhou D, Palam LR, Spandau DF, Wek RC. Both transcriptional regulation and translational control of ATF4 are central to the integrated stress response. J Biol Chem 2010; 285: 33165-74
    • (2010) J Biol Chem , vol.285 , pp. 33165-33174
    • Dey, S.1    Baird, T.D.2    Zhou, D.3    Palam, L.R.4    Spandau, D.F.5    Wek, R.C.6
  • 96
    • 79955929541 scopus 로고    scopus 로고
    • Transcriptional regulation of activating transcription factor 4 under oxidative stress in retinal pigment epithelial ARPE-19/HPV-16 cells
    • Miyamoto N, Izumi H, Miyamoto R, Bin H, Kondo H, Tawara A, Sasaguri Y, Kohno K. Transcriptional regulation of activating transcription factor 4 under oxidative stress in retinal pigment epithelial ARPE-19/HPV-16 cells. Invest Ophthalmol Vis Sci 2010; 52: 1226-34
    • (2010) Invest Ophthalmol Vis Sci , vol.52 , pp. 1226-1234
    • Miyamoto, N.1    Izumi, H.2    Miyamoto, R.3    Bin, H.4    Kondo, H.5    Tawara, A.6    Sasaguri, Y.7    Kohno, K.8
  • 97
    • 20744452215 scopus 로고    scopus 로고
    • Up-regulation of astrocyte cyclooxygenase-2, CCAAT/enhancer-binding protein, glucose-related protein 78, eukaryotic initiation factor 2α, and c-Jun N-terminal kinase by a neurovirulent murine retrovirus
    • Kim H-T, Qiang W, Liu N, Scofield VL, Wong PKY, Stoica G. Up-regulation of astrocyte cyclooxygenase-2, CCAAT/enhancer-binding protein, glucose-related protein 78, eukaryotic initiation factor 2α, and c-Jun N-terminal kinase by a neurovirulent murine retrovirus. J Neurovirol 2005; 11: 166-79
    • (2005) J Neurovirol , vol.11 , pp. 166-179
    • Kim, H.-T.1    Qiang, W.2    Liu, N.3    Scofield, V.L.4    Wong, P.K.Y.5    Stoica, G.6
  • 99
    • 0037996661 scopus 로고    scopus 로고
    • Coordinate regulation of glutathione biosynthesis and release by Nrf2-expressing glia potently protects neurons from oxidative stress
    • Shih AY, Johnson DA, Wong G, Kraft AD, Jiang L, Erb H, Johnson JA, Murphy TH. Coordinate regulation of glutathione biosynthesis and release by Nrf2-expressing glia potently protects neurons from oxidative stress. J Neurosci 2003; 23: 3394-406
    • (2003) J Neurosci , vol.23 , pp. 3394-3406
    • Shih, A.Y.1    Johnson, D.A.2    Wong, G.3    Kraft, A.D.4    Jiang, L.5    Erb, H.6    Johnson, J.A.7    Murphy, T.H.8
  • 100
    • 0018963749 scopus 로고
    • Transport interaction of L-cystine and L-glutamate in human diploid fibroblasts in culture
    • Bannai S, Kitamura E. Transport interaction of L-cystine and L-glutamate in human diploid fibroblasts in culture. J Biol Chem 1980; 255: 2372-6
    • (1980) J Biol Chem , vol.255 , pp. 2372-2376
    • Bannai, S.1    Kitamura, E.2
  • 101
    • 0023178836 scopus 로고
    • Induction of cystine transport activity in mouse peritoneal macrophages
    • Watanabe H, Bannai S. Induction of cystine transport activity in mouse peritoneal macrophages. J Exp Med 1987; 165: 628-40
    • (1987) J Exp Med , vol.165 , pp. 628-640
    • Watanabe, H.1    Bannai, S.2


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