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Volumn 12, Issue 7, 2012, Pages 807-814

Therapeutic strategies to correct proteostasis-imbalance in chronic obstructive lung diseases

Author keywords

Autophagy; Chronic obstructive pulmonary disease (COPD); Cigarette smoke (CS); Emphysema; Proteostasis imbalance; Proteostasis regulators

Indexed keywords

BORTEZOMIB; PROTEASOME INHIBITOR; TRANSCRIPTION FACTOR NRF2; TRANSFORMING GROWTH FACTOR BETA1; TRANSMEMBRANE CONDUCTANCE REGULATOR; UBIQUITIN;

EID: 84863506784     PISSN: 15665240     EISSN: 18755666     Source Type: Journal    
DOI: 10.2174/156652412801318809     Document Type: Article
Times cited : (31)

References (82)
  • 1
    • 0012626868 scopus 로고    scopus 로고
    • New concepts in chronic obstructive pulmonary disease
    • Barnes PJ. New concepts in chronic obstructive pulmonary disease. Annu Rev Med 2003; 54: 113-29.
    • (2003) Annu Rev Med , vol.54 , pp. 113-129
    • Barnes, P.J.1
  • 2
    • 33750620057 scopus 로고    scopus 로고
    • Oxidative stress and redox regulation of lung inflammation in COPD
    • Rahman I, Adcock IM. Oxidative stress and redox regulation of lung inflammation in COPD. Eur Respir J 2006; 28: 219-42.
    • (2006) Eur Respir J , vol.28 , pp. 219-242
    • Rahman, I.1    Adcock, I.M.2
  • 3
    • 0141928029 scopus 로고    scopus 로고
    • Chronic obstructive pulmonary disease: Molecular and cellular mechanisms
    • Barnes PJ, Shapiro SD and Pauwels RA. Chronic obstructive pulmonary disease: molecular and cellular mechanisms. Eur Respir J 2003; 22: 672-88.
    • (2003) Eur Respir J , vol.22 , pp. 672-688
    • Barnes, P.J.1    Shapiro, S.D.2    Pauwels, R.A.3
  • 4
    • 34447556991 scopus 로고    scopus 로고
    • Pathobiology of cigarette smoke induced chronic obstructive pulmonary disease
    • Yoshida T, Tuder RM. Pathobiology of cigarette smoke induced chronic obstructive pulmonary disease. Physiol Rev 2007; 87: 1047-82.
    • (2007) Physiol Rev , vol.87 , pp. 1047-1082
    • Yoshida, T.1    Tuder, R.M.2
  • 5
    • 79952227062 scopus 로고    scopus 로고
    • Neutral sphingomyelinase 2: A novel target in cigarette smoke induced apoptosis and lung injury
    • Filosto S, Castillo S, Danielson A, et al. Neutral sphingomyelinase 2: a novel target in cigarette smoke induced apoptosis and lung injury. Am J Respir Cell Mol Biol 2011; 44: 50-60.
    • (2011) Am J Respir Cell Mol Biol , vol.44 , pp. 50-60
    • Filosto, S.1    Castillo, S.2    Danielson, A.3
  • 6
  • 7
    • 38449099679 scopus 로고    scopus 로고
    • Role of proteasomes in disease
    • Dahlmann B. Role of proteasomes in disease. BMC Biochem 2007; 8 Suppl 1: S3.
    • (2007) BMC Biochem , Issue.8 SUPPL. 1
    • Dahlmann, B.1
  • 8
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 2006; 75: 333-66.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 9
    • 79960013933 scopus 로고    scopus 로고
    • Critical role of proteostasis-imbalance in pathogenesis of COPD and severe emphysema
    • Min T, Bodas M, Mazur S and Vij N. Critical role of proteostasis-imbalance in pathogenesis of COPD and severe emphysema. J Mol Med (Berl) 2011; 89: 577-93.
    • (2011) J Mol Med (Berl) , vol.89 , pp. 577-593
    • Min, T.1    Bodas, M.2    Mazur, S.3    Vij, N.4
  • 11
    • 77956180402 scopus 로고    scopus 로고
    • SIRT1 is a redoxsensitive deacetylase that is post-translationally modified by oxidants and carbonyl stress
    • Caito S, Rajendrasozhan S, Cook S, et al. SIRT1 is a redoxsensitive deacetylase that is post-translationally modified by oxidants and carbonyl stress. Faseb J 2010; 24: 3145-59.
    • (2010) Faseb J , vol.24 , pp. 3145-3159
    • Caito, S.1    Rajendrasozhan, S.2    Cook, S.3
  • 12
    • 57149130824 scopus 로고    scopus 로고
    • AAA ATPase p97/VCP: Cellular functions, disease and therapeutic potential
    • Vij N. AAA ATPase p97/VCP: cellular functions, disease and therapeutic potential. J Cell Mol Med 2008; 12: 2511-8.
    • (2008) J Cell Mol Med , vol.12 , pp. 2511-2518
    • Vij, N.1
  • 13
    • 0031716649 scopus 로고    scopus 로고
    • The proteasome: A protein-destroying machine
    • Tanaka K, Chiba T. The proteasome: a protein-destroying machine. Genes Cells 1998; 3: 499-510.
    • (1998) Genes Cells , vol.3 , pp. 499-510
    • Tanaka, K.1    Chiba, T.2
  • 14
    • 23144449789 scopus 로고    scopus 로고
    • Ubiquitin signalling in the NF-kappaB pathway
    • Chen ZJ. Ubiquitin signalling in the NF-kappaB pathway. Nat Cell Biol 2005; 7: 758-65.
    • (2005) Nat Cell Biol , vol.7 , pp. 758-765
    • Chen, Z.J.1
  • 15
    • 0036678959 scopus 로고    scopus 로고
    • Role and function of the 26S proteasome in proliferation and apoptosis
    • Naujokat C, Hoffmann S. Role and function of the 26S proteasome in proliferation and apoptosis. Lab Invest 2002; 82: 965-80.
    • (2002) Lab Invest , vol.82 , pp. 965-980
    • Naujokat, C.1    Hoffmann, S.2
  • 16
    • 78649754758 scopus 로고    scopus 로고
    • Early-age-related changes in proteostasis augment immunopathogenesis of sepsis and acute lung injury
    • Bodas M, Min T and Vij N. Early-age-related changes in proteostasis augment immunopathogenesis of sepsis and acute lung injury. PLoS One 2010; 5: e15480.
    • (2010) PLoS One , vol.5
    • Bodas, M.1    Min, T.2    Vij, N.3
  • 18
    • 40149100476 scopus 로고    scopus 로고
    • Regulation of proteasome-mediated protein degradation during oxidative stress and aging
    • Breusing N, Grune T. Regulation of proteasome-mediated protein degradation during oxidative stress and aging. Biol Chem 2008; 389: 203-9.
    • (2008) Biol Chem , vol.389 , pp. 203-209
    • Breusing, N.1    Grune, T.2
  • 19
    • 79958198426 scopus 로고    scopus 로고
    • Critical role of CFTR dependent lipid-rafts in cigarette smoke induced lung epithelial injury
    • Bodas M, Min T and Vij N. Critical role of CFTR dependent lipid-rafts in cigarette smoke induced lung epithelial injury. Am J Physiol Lung Cell Mol Physiol 2011; 300: L811-820.
    • (2011) Am J Physiol Lung Cell Mol Physiol , vol.300
    • Bodas, M.1    Min, T.2    Vij, N.3
  • 20
    • 78650434097 scopus 로고    scopus 로고
    • Autophagy protein microtubule-associated protein 1 light chain-3B (LC3B) activates extrinsic apoptosis during cigarette smoke-induced emphysema
    • Chen ZH, Lam HC, Jin Y, et al. Autophagy protein microtubule-associated protein 1 light chain-3B (LC3B) activates extrinsic apoptosis during cigarette smoke-induced emphysema. Proc Natl Acad Sci USA 2010; 107: 18880-5.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 18880-18885
    • Chen, Z.H.1    Lam, H.C.2    Jin, Y.3
  • 21
    • 69249124617 scopus 로고    scopus 로고
    • Mechanisms of emphysema in alpha1-antitrypsin deficiency: Molecular and cellular insights
    • Gooptu B, Ekeowa UI and Lomas DA. Mechanisms of emphysema in alpha1-antitrypsin deficiency: molecular and cellular insights. Eur Respir J 2009; 34: 475-88.
    • (2009) Eur Respir J , vol.34 , pp. 475-488
    • Gooptu, B.1    Ekeowa, U.I.2    Lomas, D.A.3
  • 22
    • 79251588056 scopus 로고    scopus 로고
    • Critical modifier role of membrane-cystic fibrosis transmembrane conductance regulator-dependent ceramide signaling in lung injury and emphysema
    • Bodas M, Min T, Mazur S and Vij N. Critical modifier role of membrane-cystic fibrosis transmembrane conductance regulator-dependent ceramide signaling in lung injury and emphysema. J Immunol 2011; 186: 602-13.
    • (2011) J Immunol , vol.186 , pp. 602-613
    • Bodas, M.1    Min, T.2    Mazur, S.3    Vij, N.4
  • 23
    • 41849092177 scopus 로고    scopus 로고
    • Ceramide accumulation mediates inflammation, cell death and infection susceptibility in cystic fibrosis
    • Teichgraber V, Ulrich M, Endlich N, et al. Ceramide accumulation mediates inflammation, cell death and infection susceptibility in cystic fibrosis. Nat Med 2008; 14: 382-91.
    • (2008) Nat Med , vol.14 , pp. 382-391
    • Teichgraber, V.1    Ulrich, M.2    Endlich, N.3
  • 25
    • 0035840849 scopus 로고    scopus 로고
    • Oxidative stress and lung inflammation in airways disease
    • MacNee W. Oxidative stress and lung inflammation in airways disease. Eur J Pharmacol 2001; 429: 195-207.
    • (2001) Eur J Pharmacol , vol.429 , pp. 195-207
    • Macnee, W.1
  • 26
    • 27644565844 scopus 로고    scopus 로고
    • Pathogenesis of chronic obstructive pulmonary disease
    • MacNee W. Pathogenesis of chronic obstructive pulmonary disease. Proc Am Thorac Soc 2005; 2: 258-66.
    • (2005) Proc Am Thorac Soc , vol.2 , pp. 258-266
    • Macnee, W.1
  • 27
    • 0021919760 scopus 로고
    • Elastases and emphysema. Current assessment of the protease-antiprotease hypothesis
    • Janoff A. Elastases and emphysema. Current assessment of the protease-antiprotease hypothesis. Am Rev Respir Dis 1985; 132: 417-33.
    • (1985) Am Rev Respir Dis , vol.132 , pp. 417-433
    • Janoff, A.1
  • 28
    • 0014678424 scopus 로고
    • Serum elastase inhibitor deficiency and alpha 1-antitrypsin deficiency in patients with obstructive emphysema
    • Turino GM, Seniorrm, Garg BD, Keller S, Levi MM and Mandl I. Serum elastase inhibitor deficiency and alpha 1-antitrypsin deficiency in patients with obstructive emphysema. Science 1969; 165: 709-11.
    • (1969) Science , vol.165 , pp. 709-711
    • Turino, G.M.1    Seniorrm, G.B.D.2    Keller, S.3    Levi, M.M.4    Mandl, I.5
  • 29
    • 79953331218 scopus 로고    scopus 로고
    • The role of matrix metalloproteinase-9 in cigarette smoke-induced emphysema
    • Atkinson JJ, Lutey BA, Suzuki Y, et al. The role of matrix metalloproteinase-9 in cigarette smoke-induced emphysema. Am J Respir Crit Care Med 2011; 183: 876-84.
    • (2011) Am J Respir Crit Care Med , vol.183 , pp. 876-884
    • Atkinson, J.J.1    Lutey, B.A.2    Suzuki, Y.3
  • 30
    • 0042031488 scopus 로고    scopus 로고
    • alpha-1-Antitrypsin ameliorates cigarette smoke-induced emphysema in the mouse
    • Churg A, Wang RD, Xie C and Wright JL. alpha-1-Antitrypsin ameliorates cigarette smoke-induced emphysema in the mouse. Am J Respir Crit Care Med 2003; 168: 199-207.
    • (2003) Am J Respir Crit Care Med , vol.168 , pp. 199-207
    • Churg, A.1    Wang, R.D.2    Xie, C.3    Wright, J.L.4
  • 31
    • 19944430698 scopus 로고    scopus 로고
    • Polymers of Z alpha1-antitrypsin co-localize with neutrophils in emphysematous alveoli and are chemotactic in vivo
    • Mahadeva R, Atkinson C, Li Z, et al. Polymers of Z alpha1-antitrypsin co-localize with neutrophils in emphysematous alveoli and are chemotactic in vivo. Am J Pathol 2005; 166: 377-86.
    • (2005) Am J Pathol , vol.166 , pp. 377-386
    • Mahadeva, R.1    Atkinson, C.2    Li, Z.3
  • 32
    • 2442488539 scopus 로고    scopus 로고
    • Z alpha1-antitrypsin polymerizes in the lung and acts as a neutrophil chemoattractant
    • Mulgrew AT, Taggart CC, Lawless MW, et al. Z alpha1-antitrypsin polymerizes in the lung and acts as a neutrophil chemoattractant. Chest 2004; 125: 1952-7.
    • (2004) Chest , vol.125 , pp. 1952-1957
    • Mulgrew, A.T.1    Taggart, C.C.2    Lawless, M.W.3
  • 33
    • 2142768895 scopus 로고    scopus 로고
    • Activation of endoplasmic reticulumspecific stress responses associated with the conformational disease Z alpha 1-antitrypsin deficiency
    • Lawless MW, Greene CM, Mulgrew A, Taggart CC, O'Neill SJ and McElvaney NG. Activation of endoplasmic reticulumspecific stress responses associated with the conformational disease Z alpha 1-antitrypsin deficiency. J Immunol 2004; 172: 5722-6.
    • (2004) J Immunol , vol.172 , pp. 5722-5726
    • Lawless, M.W.1    Greene, C.M.2    Mulgrew, A.3    Taggart, C.C.4    O'Neill, S.J.5    McElvaney, N.G.6
  • 34
    • 79953144385 scopus 로고    scopus 로고
    • Chronic obstructive pulmonary disease and lung cancer: New molecular insights
    • Adcock IM, Caramori G and Barnes PJ. Chronic obstructive pulmonary disease and lung cancer: new molecular insights. Respiration 2011;81: 265-84.
    • (2011) Respiration , vol.81 , pp. 265-284
    • Adcock, I.M.1    Caramori, G.2    Barnes, P.J.3
  • 35
    • 79952673351 scopus 로고    scopus 로고
    • Common pathogenic mechanisms and pathways in the development of COPD and lung cancer
    • Yang IA, Relan V, Wright CM, et al. Common pathogenic mechanisms and pathways in the development of COPD and lung cancer. Expert Opin Ther Targets 2011; 15: 439-56.
    • (2011) Expert Opin Ther Targets , vol.15 , pp. 439-456
    • Yang, I.A.1    Relan, V.2    Wright, C.M.3
  • 36
    • 34248187981 scopus 로고    scopus 로고
    • Heat shock protein 90: The cancer chaperone
    • Neckers L. Heat shock protein 90: the cancer chaperone. J Biosci 2007; 32: 517-30.
    • (2007) J Biosci , vol.32 , pp. 517-530
    • Neckers, L.1
  • 38
    • 70350669664 scopus 로고    scopus 로고
    • Proteasome inhibitors induce apoptosis in human lung cancer cells through a positive feedback mechanism and the subsequent Mcl-1 protein cleavage
    • Yuan BZ, Chapman J and Reynolds SH. Proteasome inhibitors induce apoptosis in human lung cancer cells through a positive feedback mechanism and the subsequent Mcl-1 protein cleavage. Oncogene 2009; 28: 3775-86.
    • (2009) Oncogene , vol.28 , pp. 3775-3786
    • Yuan, B.Z.1    Chapman, J.2    Reynolds, S.H.3
  • 40
    • 33750945704 scopus 로고    scopus 로고
    • Randomized phase II study of bortezomib alone and bortezomib in combination with docetaxel in previously treated advanced non-small-cell lung cancer
    • Fanucchi MP, Fossella FV, Belt R, et al. Randomized phase II study of bortezomib alone and bortezomib in combination with docetaxel in previously treated advanced non-small-cell lung cancer. J Clin Oncol 2006; 24: 5025-33.
    • (2006) J Clin Oncol , vol.24 , pp. 5025-5033
    • Fanucchi, M.P.1    Fossella, F.V.2    Belt, R.3
  • 41
    • 79960208716 scopus 로고    scopus 로고
    • Novel Proteasome Inhibitors to Overcome Bortezomib Resistance
    • Ruschak AM, Slassi M, Kay LE and Schimmer AD. Novel Proteasome Inhibitors to Overcome Bortezomib Resistance. J Natl Cancer Inst 2011; 103 (13): 1007-17.
    • (2011) J Natl Cancer Inst , vol.103 , Issue.13 , pp. 1007-1017
    • Ruschak, A.M.1    Slassi, M.2    Kay, L.E.3    Schimmer, A.D.4
  • 42
    • 84055172732 scopus 로고    scopus 로고
    • Critical role of VCP/p97 in the pathogenesis and progression of non-small cell lung carcinoma
    • Valle CW, Min T, Bodas M et al. Critical role of VCP/p97 in the pathogenesis and progression of non-small cell lung carcinoma. PLoS One 2011; (6): e29073.
    • (2011) PLoS One , Issue.6
    • Valle, C.W.1    Min, T.2    Bodas, M.3
  • 44
    • 0036086293 scopus 로고    scopus 로고
    • Smad3 deficiency attenuates bleomycin-induced pulmonary fibrosis in mice
    • Zhao J, Shi W, Wang YL, et al. Smad3 deficiency attenuates bleomycin-induced pulmonary fibrosis in mice. Am J Physiol Lung Cell Mol Physiol 2002; 282: L585-93.
    • (2002) Am J Physiol Lung Cell Mol Physiol , vol.282
    • Zhao, J.1    Shi, W.2    Wang, Y.L.3
  • 45
    • 0035020567 scopus 로고    scopus 로고
    • Fibrosis of the lung and other tissues: New concepts in pathogenesis and treatment
    • Sime PJ, O'Reilly KM. Fibrosis of the lung and other tissues: new concepts in pathogenesis and treatment. Clin Immunol 2001; 99: 308-19.
    • (2001) Clin Immunol , vol.99 , pp. 308-319
    • Sime, P.J.1    O'Reilly, K.M.2
  • 46
    • 0346724511 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition and its implications for fibrosis
    • Kalluri R, Neilson EG. Epithelial-mesenchymal transition and its implications for fibrosis. J Clin Invest 2003; 112: 1776-84.
    • (2003) J Clin Invest , vol.112 , pp. 1776-1784
    • Kalluri, R.1    Neilson, E.G.2
  • 47
    • 17844384822 scopus 로고    scopus 로고
    • Induction of epithelial-mesenchymal transition in alveolar epithelial cells by transforming growth factor-beta1: Potential role in idiopathic pulmonary fibrosis
    • Willis BC, Liebler JM, Luby-Phelps K, et al. Induction of epithelial-mesenchymal transition in alveolar epithelial cells by transforming growth factor-beta1: potential role in idiopathic pulmonary fibrosis. Am J Pathol 2005; 166: 1321-32.
    • (2005) Am J Pathol , vol.166 , pp. 1321-1332
    • Willis, B.C.1    Liebler, J.M.2    Luby-Phelps, K.3
  • 48
    • 78149291406 scopus 로고    scopus 로고
    • Role of myofibroblasts in vascular remodelling: Focus on restenosis and aneurysm
    • Forte A, Della Corte A, De Feo M, Cerasuolo F and Cipollaro M. Role of myofibroblasts in vascular remodelling: focus on restenosis and aneurysm. Cardiovasc Res 2010; 88: 395-405.
    • (2010) Cardiovasc Res , vol.88 , pp. 395-405
    • Forte, A.1    della Corte, A.2    de Feo, M.3    Cerasuolo, F.4    Cipollaro, M.5
  • 49
    • 1942534004 scopus 로고    scopus 로고
    • Regulation of the TGFbeta signalling pathway by ubiquitin-mediated degradation
    • Izzi L, Attisano L. Regulation of the TGFbeta signalling pathway by ubiquitin-mediated degradation. Oncogene 2004; 23: 2071-8.
    • (2004) Oncogene , vol.23 , pp. 2071-2078
    • Izzi, L.1    Attisano, L.2
  • 50
    • 79951630982 scopus 로고    scopus 로고
    • The case for therapeutic proteostasis modulators
    • Vij N. The case for therapeutic proteostasis modulators. Expert Opin Ther Targets 2011; 15: 233-6.
    • (2011) Expert Opin Ther Targets , vol.15 , pp. 233-236
    • Vij, N.1
  • 51
    • 63349102653 scopus 로고    scopus 로고
    • Histone deacetylase 2 is phosphorylated, ubiquitinated, and degraded by cigarette smoke
    • Adenuga D, Yao H, March TH, Seagrave J and Rahman I. Histone deacetylase 2 is phosphorylated, ubiquitinated, and degraded by cigarette smoke. Am J Respir Cell Mol Biol 2009; 40: 464-73.
    • (2009) Am J Respir Cell Mol Biol , vol.40 , pp. 464-473
    • Adenuga, D.1    Yao, H.2    March, T.H.3    Seagrave, J.4    Rahman, I.5
  • 52
    • 77249158771 scopus 로고    scopus 로고
    • SIRT1 regulates oxidant-and cigarette smoke-induced eNOS acetylation in endothelial cells: Role of resveratrol
    • Arunachalam G, Yao H, Sundar IK, Caito S and Rahman I. SIRT1 regulates oxidant-and cigarette smoke-induced eNOS acetylation in endothelial cells: Role of resveratrol. Biochem Biophys Res Commun 2010; 393: 66-72.
    • (2010) Biochem Biophys Res Commun , vol.393 , pp. 66-72
    • Arunachalam, G.1    Yao, H.2    Sundar, I.K.3    Caito, S.4    Rahman, I.5
  • 53
    • 22144445316 scopus 로고    scopus 로고
    • Diaphragm dysfunction in chronic obstructive pulmonary disease
    • Ottenheijm CA, Heunks LM, Sieck GC, et al. Diaphragm dysfunction in chronic obstructive pulmonary disease. Am J Respir Crit Care Med 2005; 172: 200-5.
    • (2005) Am J Respir Crit Care Med , vol.172 , pp. 200-205
    • Ottenheijm, C.A.1    Heunks, L.M.2    Sieck, G.C.3
  • 55
    • 72549115279 scopus 로고    scopus 로고
    • Heightened endoplasmic reticulum stress in the lungs of patients with chronic obstructive pulmonary disease: The role of Nrf2-regulated proteasomal activity
    • Malhotra D, Thimmulappa R, Vij N, et al. Heightened endoplasmic reticulum stress in the lungs of patients with chronic obstructive pulmonary disease: the role of Nrf2-regulated proteasomal activity. Am J Respir Crit Care Med 2009; 180: 1196-207.
    • (2009) Am J Respir Crit Care Med , vol.180 , pp. 1196-1207
    • Malhotra, D.1    Thimmulappa, R.2    Vij, N.3
  • 57
    • 70349266064 scopus 로고    scopus 로고
    • Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging
    • Ben-Zvi A, Miller EA and Morimoto RI. Collapse of proteostasis represents an early molecular event in Caenorhabditis elegans aging. Proc Natl Acad Sci USA 2009; 106: 14914-9.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 14914-14919
    • Ben-Zvi, A.1    Miller, E.A.2    Morimoto, R.I.3
  • 58
    • 58249099942 scopus 로고    scopus 로고
    • COPD as a disease of accelerated lung aging
    • Ito K, Barnes PJ. COPD as a disease of accelerated lung aging. Chest 2009;135: 173-80.
    • (2009) Chest , vol.135 , pp. 173-180
    • Ito, K.1    Barnes, P.J.2
  • 59
    • 0034578389 scopus 로고    scopus 로고
    • Aggresomes, inclusion bodies and protein aggregation
    • Kopito RR. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol 2000; 10: 524-30.
    • (2000) Trends Cell Biol , vol.10 , pp. 524-530
    • Kopito, R.R.1
  • 60
    • 79251484668 scopus 로고    scopus 로고
    • Measuring the impact of cigarette smoke on the UPR
    • Zhao H, Yang J, Shan L and Jorgensen ED. Measuring the impact of cigarette smoke on the UPR. Methods Enzymol 2011; 489: 147-64.
    • (2011) Methods Enzymol , vol.489 , pp. 147-164
    • Zhao, H.1    Yang, J.2    Shan, L.3    Jorgensen, E.D.4
  • 61
    • 77956396747 scopus 로고    scopus 로고
    • Defective CFTR induces aggresome formation and lung inflammation in cystic fibrosis through ROS-mediated autophagy inhibition
    • Luciani A, Villella VR, Esposito S, et al. Defective CFTR induces aggresome formation and lung inflammation in cystic fibrosis through ROS-mediated autophagy inhibition. Nat Cell Biol 2010;12: 863-75.
    • (2010) Nat Cell Biol , vol.12 , pp. 863-875
    • Luciani, A.1    Villella, V.R.2    Esposito, S.3
  • 62
    • 0032576605 scopus 로고    scopus 로고
    • Aggresomes: A cellular response to misfolded proteins
    • Johnston JA, Ward CL and Kopito RR. Aggresomes: a cellular response to misfolded proteins. J Cell Biol 1998;143: 1883-98.
    • (1998) J Cell Biol , vol.143 , pp. 1883-1898
    • Johnston, J.A.1    Ward, C.L.2    Kopito, R.R.3
  • 63
    • 19444372847 scopus 로고    scopus 로고
    • Inhibition of sequestosome 1/p62 up-regulation prevents aggregation of ubiquitinated proteins induced by prostaglandin J2 without reducing its neurotoxicity
    • Wang Z, Figueiredo-Pereira ME. Inhibition of sequestosome 1/p62 up-regulation prevents aggregation of ubiquitinated proteins induced by prostaglandin J2 without reducing its neurotoxicity. Mol Cell Neurosci 2005; 29: 222-31.
    • (2005) Mol Cell Neurosci , vol.29 , pp. 222-231
    • Wang, Z.1    Figueiredo-Pereira, M.E.2
  • 64
    • 77956410115 scopus 로고    scopus 로고
    • Selective autophagy: Ubiquitin-mediated recognition and beyond
    • Kraft C, Peter M and Hofmann K. Selective autophagy: ubiquitin-mediated recognition and beyond. Nat Cell Biol 2010; 12: 836-41.
    • (2010) Nat Cell Biol , vol.12 , pp. 836-841
    • Kraft, C.1    Peter, M.2    Hofmann, K.3
  • 65
    • 78751672975 scopus 로고    scopus 로고
    • Autophagy in immunity and inflammation
    • Levine B, Mizushima N and Virgin HW. Autophagy in immunity and inflammation. Nature 2011; 469: 323-35.
    • (2011) Nature , vol.469 , pp. 323-335
    • Levine, B.1    Mizushima, N.2    Virgin, H.W.3
  • 66
    • 78650434097 scopus 로고    scopus 로고
    • Autophagy protein microtubule-associated protein 1 light chain-3B (LC3B) activates extrinsic apoptosis during cigarette smoke-induced emphysema
    • Chen ZH, Lam HC, Jin Y, et al. Autophagy protein microtubule-associated protein 1 light chain-3B (LC3B) activates extrinsic apoptosis during cigarette smoke-induced emphysema. Proc Natl Acad Sci USA 2010; 107: 18880-5.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 18880-18885
    • Chen, Z.H.1    Lam, H.C.2    Jin, Y.3
  • 67
    • 79953657006 scopus 로고    scopus 로고
    • Deadly triplex: Smoke, autophagy, and apoptosis
    • Ryter SW, Lam HC, Chen ZH and Choi AM. Deadly triplex: Smoke, autophagy, and apoptosis. Autophagy 2011; 7 (4): 436-7.
    • (2011) Autophagy , vol.7 , Issue.4 , pp. 436-437
    • Ryter, S.W.1    Lam, H.C.2    Chen, Z.H.3    Choi, A.M.4
  • 68
    • 78149476302 scopus 로고    scopus 로고
    • Identification of an autophagy defect in smokers' alveolar macrophages
    • Monick MM, Powers LS, Walters K, et al. Identification of an autophagy defect in smokers' alveolar macrophages. J Immunol 2010; 185: 5425-35.
    • (2010) J Immunol , vol.185 , pp. 5425-5435
    • Monick, M.M.1    Powers, L.S.2    Walters, K.3
  • 70
    • 79953283054 scopus 로고    scopus 로고
    • A Pseudomonas aeruginosa toxin that hijacks the host ubiquitin proteolytic system
    • Bomberger JM, Ye S, Maceachran DP, et al. A Pseudomonas aeruginosa toxin that hijacks the host ubiquitin proteolytic system. PLoS Pathog 2011; 7: e1001325.
    • (2011) PLoS Pathog , vol.7
    • Bomberger, J.M.1    Ye, S.2    Maceachran, D.P.3
  • 71
    • 77956930518 scopus 로고    scopus 로고
    • Development of PEGylated PLGA nanoparticle for controlled and sustained drug delivery in cystic fibrosis
    • Vij N, Min T, Marasigan R, et al. Development of PEGylated PLGA nanoparticle for controlled and sustained drug delivery in cystic fibrosis. J Nanobiotechnology 2010; 8: 22.
    • (2010) J Nanobiotechnology , vol.8 , pp. 22
    • Vij, N.1    Min, T.2    Marasigan, R.3
  • 72
    • 33748419472 scopus 로고    scopus 로고
    • The role of autophagy in alpha-1-antitrypsin deficiency: A specific cellular response in genetic diseases associated with aggregation-prone proteins
    • Perlmutter DH. The role of autophagy in alpha-1-antitrypsin deficiency: a specific cellular response in genetic diseases associated with aggregation-prone proteins. Autophagy 2006; 2: 258-63.
    • (2006) Autophagy , vol.2 , pp. 258-263
    • Perlmutter, D.H.1
  • 73
    • 0034652248 scopus 로고    scopus 로고
    • Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency
    • Burrows JA, Willis LK and Perlmutter DH. Chemical chaperones mediate increased secretion of mutant alpha 1-antitrypsin (alpha 1-AT) Z: A potential pharmacological strategy for prevention of liver injury and emphysema in alpha 1-AT deficiency. Proc Natl Acad Sci USA 2000; 97: 1796-801.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 1796-1801
    • Burrows, J.A.1    Willis, L.K.2    Perlmutter, D.H.3
  • 74
    • 77950428804 scopus 로고    scopus 로고
    • Reduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosis
    • Hutt DM, Herman D, Rodrigues AP, et al. Reduced histone deacetylase 7 activity restores function to misfolded CFTR in cystic fibrosis. Nat Chem Biol 2010; 6: 25-33.
    • (2010) Nat Chem Biol , vol.6 , pp. 25-33
    • Hutt, D.M.1    Herman, D.2    Rodrigues, A.P.3
  • 75
    • 84863535398 scopus 로고    scopus 로고
    • Class-II HDAC inhibition controls P. aeruginosa LPS induced CF lung disease by modulating NFkB signaling, neutrophil chemotaxis and Treg recruitment
    • Baltimore, MD
    • Vij N, Mazur S, Bodas M, Min T. Class-II HDAC inhibition controls P. aeruginosa LPS induced CF lung disease by modulating NFkB signaling, neutrophil chemotaxis and Treg recruitment. North American Cystic Fibrosis Foundation Conference. 2010; Baltimore, MD.
    • (2010) North American Cystic Fibrosis Foundation Conference
    • Vij, N.1    Mazur, S.2    Bodas, M.3    Min, T.4
  • 76
    • 53349129568 scopus 로고    scopus 로고
    • In vivo investigations on anti-fibrotic potential of proteasome inhibition in lung and skin fibrosis
    • Fineschi S, Bongiovanni M, Donati Y, et al. In vivo investigations on anti-fibrotic potential of proteasome inhibition in lung and skin fibrosis. Am J Respir Cell Mol Biol 2008; 39: 458-65.
    • (2008) Am J Respir Cell Mol Biol , vol.39 , pp. 458-465
    • Fineschi, S.1    Bongiovanni, M.2    Donati, Y.3
  • 77
    • 33645805628 scopus 로고    scopus 로고
    • Proteasome blockade exerts an antifibrotic activity by coordinately down-regulating type I collagen and tissue inhibitor of metalloproteinase-1 and up-regulating metalloproteinase-1 production in human dermal fibroblasts
    • Fineschi S, Reith W, Guerne PA, Dayer JM and Chizzolini C. Proteasome blockade exerts an antifibrotic activity by coordinately down-regulating type I collagen and tissue inhibitor of metalloproteinase-1 and up-regulating metalloproteinase-1 production in human dermal fibroblasts. Faseb J 2006; 20: 562-4.
    • (2006) Faseb J , vol.20 , pp. 562-564
    • Fineschi, S.1    Reith, W.2    Guerne, P.A.3    Dayer, J.M.4    Chizzolini, C.5
  • 78
    • 13644256191 scopus 로고    scopus 로고
    • A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress
    • Boyce M, Bryant KF, Jousse C, et al. A selective inhibitor of eIF2alpha dephosphorylation protects cells from ER stress. Science 2005; 307: 935-9.
    • (2005) Science , vol.307 , pp. 935-939
    • Boyce, M.1    Bryant, K.F.2    Jousse, C.3
  • 79
    • 77954597127 scopus 로고    scopus 로고
    • An autophagy-enhancing drug promotes degradation of mutant alpha1-antitrypsin Z and reduces hepatic fibrosis
    • Hidvegi T, Ewing M, Hale P, et al. An autophagy-enhancing drug promotes degradation of mutant alpha1-antitrypsin Z and reduces hepatic fibrosis. Science 2010; 329: 229-32.
    • (2010) Science , vol.329 , pp. 229-232
    • Hidvegi, T.1    Ewing, M.2    Hale, P.3
  • 81
    • 80052086371 scopus 로고    scopus 로고
    • Nano-based theranostics for chronic obstructive lung diseases: Challenges and therapeutic potential
    • Vij N. Nano-based theranostics for chronic obstructive lung diseases: challenges and therapeutic potential. Expert Opin Drug Deliv 2011; 8: 1105-9.
    • (2011) Expert Opin Drug Deliv , vol.8 , pp. 1105-1109
    • Vij, N.1
  • 82
    • 77949915977 scopus 로고    scopus 로고
    • Nanodelivery in airway diseases: Challenges and therapeutic applications
    • Roy I, Vij N. Nanodelivery in airway diseases: challenges and therapeutic applications. Nanomedicine 2010; 6: 237-44.
    • (2010) Nanomedicine , vol.6 , pp. 237-244
    • Roy, I.1    Vij, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.