메뉴 건너뛰기




Volumn 2013, Issue , 2013, Pages

Endoplasmic reticulum is at the crossroads of autophagy, inflammation, and apoptosis signaling pathways and participates in the pathogenesis of diabetes mellitus

Author keywords

[No Author keywords available]

Indexed keywords

APOPTOSIS; AUTOPHAGY; DIABETES MELLITUS; ENDOPLASMIC RETICULUM; ENDOPLASMIC RETICULUM STRESS; HUMAN; INFLAMMATION; INTRACELLULAR SIGNALING; MOLECULAR MECHANICS; NONHUMAN; PATHOGENESIS; PRIORITY JOURNAL; REVIEW; UNFOLDED PROTEIN RESPONSE; ANIMAL; METABOLISM; PATHOPHYSIOLOGY; PHYSIOLOGY; SIGNAL TRANSDUCTION;

EID: 84878687221     PISSN: 23146745     EISSN: 23146753     Source Type: Journal    
DOI: 10.1155/2013/193461     Document Type: Review
Times cited : (65)

References (70)
  • 1
    • 84872008953 scopus 로고    scopus 로고
    • Sirtuins and renal diseases: Relationship with aging and diabetic nephropathy
    • Kitada M., Kume S., Takeda-Watanabe A., Sirtuins and renal diseases: relationship with aging and diabetic nephropathy. Clinical Science 2013 124 3 153 164
    • (2013) Clinical Science , vol.124 , Issue.3 , pp. 153-164
    • Kitada, M.1    Kume, S.2    Takeda-Watanabe, A.3
  • 2
    • 84864923640 scopus 로고    scopus 로고
    • Post-prandial glucose and diabetic complications: Systematic review of observational studies
    • Mannucci E., Monami M., Lamanna C., Post-prandial glucose and diabetic complications: systematic review of observational studies. Acta Diabetologica 2012 49 4 307 314
    • (2012) Acta Diabetologica , vol.49 , Issue.4 , pp. 307-314
    • Mannucci, E.1    Monami, M.2    Lamanna, C.3
  • 3
    • 84861355284 scopus 로고    scopus 로고
    • Diabetes
    • Brody H., Diabetes. Nature 2012 485 7398 S1
    • (2012) Nature , vol.485 , Issue.7398
    • Brody, H.1
  • 4
    • 82255161944 scopus 로고    scopus 로고
    • Road to ruin: Targeting proteins for degradation in the endoplasmic reticulum
    • Smith M. H., Ploegh H. L., Weissman J. S., Road to ruin: targeting proteins for degradation in the endoplasmic reticulum. Science 2011 334 6059 1086 1090
    • (2011) Science , vol.334 , Issue.6059 , pp. 1086-1090
    • Smith, M.H.1    Ploegh, H.L.2    Weissman, J.S.3
  • 5
    • 77950343252 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
    • 2-s2.0-77950343252 10.1016/j.cell.2010.02.034
    • Hotamisligil G. S., Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell 2010 140 6 900 917 2-s2.0-77950343252 10.1016/j.cell.2010.02.034
    • (2010) Cell , vol.140 , Issue.6 , pp. 900-917
    • Hotamisligil, G.S.1
  • 7
    • 84859530797 scopus 로고    scopus 로고
    • ER stress as a trigger for beta-cell dysfunction and autoimmunity in type 1 diabetes
    • O'Sullivan-Murphy B., Urano F., ER stress as a trigger for beta-cell dysfunction and autoimmunity in type 1 diabetes. Diabetes 2012 61 4 780 781
    • (2012) Diabetes , vol.61 , Issue.4 , pp. 780-781
    • O'Sullivan-Murphy, B.1    Urano, F.2
  • 8
    • 34250899722 scopus 로고    scopus 로고
    • Signal integration in the endoplasmic reticulum unfolded protein response
    • DOI 10.1038/nrm2199, PII NRM2199
    • Ron D., Walter P., Signal integration in the endoplasmic reticulum unfolded protein response. Nature Reviews Molecular Cell Biology 2007 8 7 519 529 2-s2.0-34250899722 10.1038/nrm2199 (Pubitemid 46985379)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.7 , pp. 519-529
    • Ron, D.1    Walter, P.2
  • 9
    • 84858324600 scopus 로고    scopus 로고
    • The role of glucosamine-induced ER stress in diabetic atherogenesis
    • 187018 10.1155/2012/187018
    • Beriault D. R., Werstuck G. H., The role of glucosamine-induced ER stress in diabetic atherogenesis. Experimental Diabetes Research 2012 2012 11 187018 10.1155/2012/187018
    • (2012) Experimental Diabetes Research , vol.2012 , pp. 11
    • Beriault, D.R.1    Werstuck, G.H.2
  • 10
    • 0033782015 scopus 로고    scopus 로고
    • Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response
    • 2-s2.0-0033782015 10.1038/35014014
    • Bertolotti A., Zhang Y., Hendershot L. M., Harding H. P., Ron D., Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response. Nature Cell Biology 2000 2 6 326 332 2-s2.0-0033782015 10.1038/35014014
    • (2000) Nature Cell Biology , vol.2 , Issue.6 , pp. 326-332
    • Bertolotti, A.1    Zhang, Y.2    Hendershot, L.M.3    Harding, H.P.4    Ron, D.5
  • 11
    • 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
    • DOI 10.1074/jbc.M110636200
    • 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. Journal of Biological Chemistry 2002 277 15 13045 13052 2-s2.0-0037066741 10.1074/jbc.M110636200 (Pubitemid 34952673)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.15 , pp. 13045-13052
    • Chen, X.1    Shen, J.2    Prywes, R.3
  • 12
    • 33846223428 scopus 로고    scopus 로고
    • Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress
    • DOI 10.1128/MCB.00408-06
    • Nadanaka S., Okada T., Yoshida H., Mori K., Role of disulfide bridges formed in the luminal domain of ATF6 in sensing endoplasmic reticulum stress. Molecular and Cellular Biology 2007 27 3 1027 1043 2-s2.0-33846223428 10.1128/MCB.00408-06 (Pubitemid 46174565)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.3 , pp. 1027-1043
    • Nadanaka, S.1    Okada, T.2    Yoshida, H.3    Mori, K.4
  • 13
    • 0034644111 scopus 로고    scopus 로고
    • ER stress response: Getting the UPR hand on misfolded proteins
    • DOI 10.1016/S0960-9822(00)00583-2
    • Hampton R. Y., ER stress response: getting the UPR hand on misfolded proteins. Current Biology 2000 10 14 R518 R521 2-s2.0-0034644111 10.1016/S0960-9822(00)00583-2 (Pubitemid 30597194)
    • (2000) Current Biology , vol.10 , Issue.14
    • Hampton, R.Y.1
  • 14
    • 84855597540 scopus 로고    scopus 로고
    • ER stress and apoptosis: A new mechanism for retinal cell death
    • 589589 10.1155/2012/589589
    • Jing G., Wang J. J., Zhang S. X., ER stress and apoptosis: a new mechanism for retinal cell death. Experimental Diabetes Research 2012 2012 11 589589 10.1155/2012/589589
    • (2012) Experimental Diabetes Research , vol.2012 , pp. 11
    • Jing, G.1    Wang, J.J.2    Zhang, S.X.3
  • 15
  • 16
    • 84864865373 scopus 로고    scopus 로고
    • The unfolded protein response controls induction and activation of ADAM17/TACE by severe hypoxia and ER stress
    • Rzymski T., Petry A., Kracun D., The unfolded protein response controls induction and activation of ADAM17/TACE by severe hypoxia and ER stress. Oncogene 2012 31 31 3621 3634
    • (2012) Oncogene , vol.31 , Issue.31 , pp. 3621-3634
    • Rzymski, T.1    Petry, A.2    Kracun, D.3
  • 17
    • 77649196117 scopus 로고    scopus 로고
    • Integration of ER stress, oxidative stress and the inflammatory response in health and disease
    • Zhang K., Integration of ER stress, oxidative stress and the inflammatory response in health and disease. International Journal of Clinical and Experimental Medicine 2010 3 1 33 40
    • (2010) International Journal of Clinical and Experimental Medicine , vol.3 , Issue.1 , pp. 33-40
    • Zhang, K.1
  • 18
    • 27644484061 scopus 로고    scopus 로고
    • Autophagy: Molecular machinery for self-eating
    • DOI 10.1038/sj.cdd.4401765, PII 4401765
    • Yorimitsu T., Klionsky D. J., Autophagy: molecular machinery for self-eating. Cell Death and Differentiation 2005 12 2 1542 1552 2-s2.0-27644484061 10.1038/sj.cdd.4401765 (Pubitemid 41553991)
    • (2005) Cell Death and Differentiation , vol.12 , Issue.SUPPL. 2 , pp. 1542-1552
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 19
    • 39849109338 scopus 로고    scopus 로고
    • Autophagy fights disease through cellular self-digestion
    • DOI 10.1038/nature06639, PII NATURE06639
    • Mizushima N., Levine B., Cuervo A. M., Klionsky D. J., Autophagy fights disease through cellular self-digestion. Nature 2008 451 7182 1069 1075 2-s2.0-39849109338 10.1038/nature06639 (Pubitemid 351317450)
    • (2008) Nature , vol.451 , Issue.7182 , pp. 1069-1075
    • Mizushima, N.1    Levine, B.2    Cuervo, A.M.3    Klionsky, D.J.4
  • 20
    • 78649338141 scopus 로고    scopus 로고
    • Autophagy and the integrated stress response
    • 2-s2.0-78649338141 10.1016/j.molcel.2010.09.023
    • Kroemer G., Mariño G., Levine B., Autophagy and the integrated stress response. Molecular Cell 2010 40 2 280 293 2-s2.0-78649338141 10.1016/j.molcel.2010.09.023
    • (2010) Molecular Cell , vol.40 , Issue.2 , pp. 280-293
    • Kroemer, G.1    Mariño, G.2    Levine, B.3
  • 21
    • 84863181426 scopus 로고    scopus 로고
    • The role of autophagy in endoplasmic reticulum stress-induced pancreatic beta cell death
    • Yin J. J., Li Y. B., Wang Y., The role of autophagy in endoplasmic reticulum stress-induced pancreatic beta cell death. Autophagy 2012 8 2 158 164
    • (2012) Autophagy , vol.8 , Issue.2 , pp. 158-164
    • Yin, J.J.1    Li, Y.B.2    Wang, Y.3
  • 22
    • 34249668329 scopus 로고    scopus 로고
    • Eating the endoplasmic reticulum: quality control by autophagy
    • DOI 10.1016/j.tcb.2007.04.005, PII S0962892407000967
    • Yorimitsu T., Klionsky D. J., Eating the endoplasmic reticulum: quality control by autophagy. Trends in Cell Biology 2007 17 6 279 285 2-s2.0-34249668329 10.1016/j.tcb.2007.04.005 (Pubitemid 46829849)
    • (2007) Trends in Cell Biology , vol.17 , Issue.6 , pp. 279-285
    • Yorimitsu, T.1    Klionsky, D.J.2
  • 23
    • 33750363298 scopus 로고    scopus 로고
    • The roles of intracellular protein-degradation pathways in neurodegeneration
    • DOI 10.1038/nature05291, PII NATURE05291
    • Rubinsztein D. C., The roles of intracellular protein-degradation pathways in neurodegeneration. Nature 2006 443 7113 780 786 2-s2.0-33750363298 10.1038/nature05291 (Pubitemid 44622682)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 780-786
    • Rubinsztein, D.C.1
  • 25
    • 84855185046 scopus 로고    scopus 로고
    • Autophagy as a therapeutic target in diabetic nephropathy
    • 628978 10.1155/2012/628978
    • Tanaka Y., Kume S., Kitada M., Autophagy as a therapeutic target in diabetic nephropathy. Experimental Diabetes Research 2012 2012 12 628978 10.1155/2012/628978
    • (2012) Experimental Diabetes Research , vol.2012 , pp. 12
    • Tanaka, Y.1    Kume, S.2    Kitada, M.3
  • 28
    • 65449133190 scopus 로고    scopus 로고
    • The α -glucosidase inhibitor acarbose prevents obesity and simple steatosis in sequestosome 1/A170/p62 deficient mice
    • 2-s2.0-65449133190 10.1111/j.1872-034X.2008.00478.x
    • Okada K., Yanagawa T., Warabi E., Yamastu K., Uwayama J., Takeda K., Utsunomiya H., Yoshida H., Shoda J., Ishii T., The α -glucosidase inhibitor acarbose prevents obesity and simple steatosis in sequestosome 1/A170/p62 deficient mice. Hepatology Research 2009 39 5 490 500 2-s2.0-65449133190 10.1111/j.1872-034X.2008.00478.x
    • (2009) Hepatology Research , vol.39 , Issue.5 , pp. 490-500
    • Okada, K.1    Yanagawa, T.2    Warabi, E.3    Yamastu, K.4    Uwayama, J.5    Takeda, K.6    Utsunomiya, H.7    Yoshida, H.8    Shoda, J.9    Ishii, T.10
  • 29
    • 84857815981 scopus 로고    scopus 로고
    • Sequestosome 1/p62: Across diseases
    • Geetha T., Vishwaprakash N., Sycheva M., Sequestosome 1/p62: across diseases. Biomarkers 2012 17 2 99 103
    • (2012) Biomarkers , vol.17 , Issue.2 , pp. 99-103
    • Geetha, T.1    Vishwaprakash, N.2    Sycheva, M.3
  • 31
    • 33646685457 scopus 로고    scopus 로고
    • The molecular inflammatory process in aging
    • DOI 10.1089/ars.2006.8.572
    • Chung H. Y., Sung B., Jung K. J., Zou Y., Yu B. P., The molecular inflammatory process in aging. Antioxidants and Redox Signaling 2006 8 3-4 572 581 2-s2.0-33646685457 10.1089/ars.2006.8.572 (Pubitemid 43741326)
    • (2006) Antioxidants and Redox Signaling , vol.8 , Issue.3-4 , pp. 572-581
    • Chung, H.Y.1    Sung, B.2    Jung, K.J.3    Zou, Y.4    Yu, B.P.5
  • 32
    • 79957874666 scopus 로고    scopus 로고
    • Inflammatory molecules and pathways in the pathogenesis of diabetic nephropathy
    • 2-s2.0-79957874666 10.1038/nrneph.2011.51
    • Navarro-González J. F., Mora-Fernández C., De Fuentes M. M., García-Pérez J., Inflammatory molecules and pathways in the pathogenesis of diabetic nephropathy. Nature Reviews Nephrology 2011 7 6 327 340 2-s2.0-79957874666 10.1038/nrneph.2011.51
    • (2011) Nature Reviews Nephrology , vol.7 , Issue.6 , pp. 327-340
    • Navarro-González, J.F.1    Mora-Fernández, C.2    De Fuentes, M.M.3    García-Pérez, J.4
  • 33
    • 33645815074 scopus 로고    scopus 로고
    • Autocrine tumor necrosis factor alpha links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1 α -mediated NF- B activation and down-regulation of TRAF2 expression
    • 2-s2.0-33645815074 10.1128/MCB.26.8.3071-3084.2006
    • Hu P., Han Z., Couvillon A. D., Kaufman R. J., Exton J. H., Autocrine tumor necrosis factor alpha links endoplasmic reticulum stress to the membrane death receptor pathway through IRE1 α -mediated NF- B activation and down-regulation of TRAF2 expression. Molecular and Cellular Biology 2006 26 8 3071 3084 2-s2.0-33645815074 10.1128/MCB.26.8.3071-3084.2006
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.8 , pp. 3071-3084
    • Hu, P.1    Han, Z.2    Couvillon, A.D.3    Kaufman, R.J.4    Exton, J.H.5
  • 34
    • 84861743338 scopus 로고    scopus 로고
    • Transient aggregation of ubiquitinated proteins is a cytosolic unfolded protein response to inflammation and endoplasmic reticulum stress
    • Liu X. D., Ko S., Xu Y., Transient aggregation of ubiquitinated proteins is a cytosolic unfolded protein response to inflammation and endoplasmic reticulum stress. The Journal of Biological Chemistry 2012 287 23 19687 19698
    • (2012) The Journal of Biological Chemistry , vol.287 , Issue.23 , pp. 19687-19698
    • Liu, X.D.1    Ko, S.2    Xu, Y.3
  • 35
    • 0027459878 scopus 로고
    • Adipose expression of tumor necrosis factor-α: Direct role in obesity-linked insulin resistance
    • Hotamisligil G. S., Shargill N. S., Spiegelman B. M., Adipose expression of tumor necrosis factor- α: direct role in obesity-linked insulin resistance. Science 1993 259 5091 87 91 2-s2.0-0027459878 (Pubitemid 23036092)
    • (1993) Science , vol.259 , Issue.5091 , pp. 87-91
    • Hotamisligil, G.S.1    Shargill, N.S.2    Spiegelman, B.M.3
  • 36
    • 0037153158 scopus 로고    scopus 로고
    • A central, role for JNK in obesity and insulin resistance
    • DOI 10.1038/nature01137
    • Hirosumi J., Tuncman G., Chang L., Görgün C. Z., Uysal K. T., Maeda K., Karin M., Hotamisligil G. S., A central, role for JNK in obesity and insulin resistance. Nature 2002 420 6913 333 336 2-s2.0-0037153158 10.1038/nature01137 (Pubitemid 35398190)
    • (2002) Nature , vol.420 , Issue.6913 , pp. 333-336
    • Hirosumi, J.1    Tuncman, G.2    Chang, L.3    Gorgun, C.Z.4    Uysal, K.T.5    Maeda, K.6    Karin, M.7    Hotamisligil, G.S.8
  • 38
    • 52349105273 scopus 로고    scopus 로고
    • A predominant role for parenchymal c-Jun amino terminal kinase (JNK) in the regulation of systemic insulin sensitivity
    • ARTICLE E3151 2-s2.0-52349105273 10.1371/journal.pone.0003151
    • Vallerie S. N., Furuhashi M., Fucho R., Hotamisligil G. S., A predominant role for parenchymal c-Jun amino terminal kinase (JNK) in the regulation of systemic insulin sensitivity. PLoS ONE 2008 3 9, article e3151 2-s2.0-52349105273 10.1371/journal.pone.0003151
    • (2008) PLoS ONE , vol.3 , Issue.9
    • Vallerie, S.N.1    Furuhashi, M.2    Fucho, R.3    Hotamisligil, G.S.4
  • 39
    • 33745861300 scopus 로고    scopus 로고
    • Inflammation and insulin resistance
    • 2-s2.0-33745861300 10.1172/JCI29069
    • Shoelson S. E., Lee J., Goldfine A. B., Inflammation and insulin resistance. Journal of Clinical Investigation 2006 116 7 1793 1801 2-s2.0-33745861300 10.1172/JCI29069
    • (2006) Journal of Clinical Investigation , vol.116 , Issue.7 , pp. 1793-1801
    • Shoelson, S.E.1    Lee, J.2    Goldfine, A.B.3
  • 42
    • 33845866857 scopus 로고    scopus 로고
    • Inflammation and metabolic disorders
    • DOI 10.1038/nature05485, PII NATURE05485
    • Hotamisligil G. S., Inflammation and metabolic disorders. Nature 2006 444 7121 860 867 2-s2.0-33845866857 10.1038/nature05485 (Pubitemid 46024993)
    • (2006) Nature , vol.444 , Issue.7121 , pp. 860-867
    • Hotamisligil, G.S.1
  • 43
    • 77950677297 scopus 로고    scopus 로고
    • Adipocytes as immune cells: Differential expression of TWEAK, BAFF, and APRIL and their receptors (Fn14, BAFF-R, TACI, and BCMA) at different stages of normal and pathological adipose tissue development
    • 2-s2.0-77950677297 10.4049/jimmunol.0901186
    • Alexaki V. I., Notas G., Pelekanou V., Kampa M., Valkanou M., Theodoropoulos P., Stathopoulos E. N., Tsapis A., Castanas E., Adipocytes as immune cells: differential expression of TWEAK, BAFF, and APRIL and their receptors (Fn14, BAFF-R, TACI, and BCMA) at different stages of normal and pathological adipose tissue development. Journal of Immunology 2009 183 9 5948 5956 2-s2.0-77950677297 10.4049/jimmunol.0901186
    • (2009) Journal of Immunology , vol.183 , Issue.9 , pp. 5948-5956
    • Alexaki, V.I.1    Notas, G.2    Pelekanou, V.3    Kampa, M.4    Valkanou, M.5    Theodoropoulos, P.6    Stathopoulos, E.N.7    Tsapis, A.8    Castanas, E.9
  • 44
    • 70349755645 scopus 로고    scopus 로고
    • How punctual ablation of regulatory T cells unleashes an autoimmune lesion within the pancreatic islets
    • 2-s2.0-70349755645 10.1016/j.immuni.2009.08.023
    • Feuerer M., Shen Y., Littman D. R., Benoist C., Mathis D., How punctual ablation of regulatory T cells unleashes an autoimmune lesion within the pancreatic islets. Immunity 2009 31 4 654 664 2-s2.0-70349755645 10.1016/j.immuni.2009.08.023
    • (2009) Immunity , vol.31 , Issue.4 , pp. 654-664
    • Feuerer, M.1    Shen, Y.2    Littman, D.R.3    Benoist, C.4    Mathis, D.5
  • 45
    • 84869184022 scopus 로고    scopus 로고
    • Obesity-induced endoplasmic reticulum stress causes chronic inflammation in adipose tissue
    • Kawasaki N., Asada R., Saito A., Obesity-induced endoplasmic reticulum stress causes chronic inflammation in adipose tissue. Scientific Reports 2012 2, article 799
    • (2012) Scientific Reports , vol.2799
    • Kawasaki, N.1    Asada, R.2    Saito, A.3
  • 46
    • 84863378809 scopus 로고    scopus 로고
    • The role of endoplasmic reticulum stress in autoimmune-mediated beta-cell destruction in type 1 diabetes
    • 238980 10.1155/2012/238980
    • Zhong J., Rao X., Xu J. F., The role of endoplasmic reticulum stress in autoimmune-mediated beta-cell destruction in type 1 diabetes. Experimental Diabetes Research 2012 2012 12 238980 10.1155/2012/238980
    • (2012) Experimental Diabetes Research , vol.2012 , pp. 12
    • Zhong, J.1    Rao, X.2    Xu, J.F.3
  • 47
    • 84865497318 scopus 로고    scopus 로고
    • Adipocytes secrete leukotrienes: Contribution to obesity-associated inflammation and insulin resistance in mice
    • Mothe-Satney I., Filloux C., Amghar H., Adipocytes secrete leukotrienes: contribution to obesity-associated inflammation and insulin resistance in mice. Diabetes 2012 61 9 2311 2319
    • (2012) Diabetes , vol.61 , Issue.9 , pp. 2311-2319
    • Mothe-Satney, I.1    Filloux, C.2    Amghar, H.3
  • 48
    • 84863484585 scopus 로고    scopus 로고
    • Perk-dependent repression of miR-106b-25 cluster is required for ER stress-induced apoptosis
    • Gupta S., Read D. E., Deepti A., Perk-dependent repression of miR-106b-25 cluster is required for ER stress-induced apoptosis. Cell Death and Disease 2012 3, article e333
    • (2012) Cell Death and Disease , vol.3333
    • Gupta, S.1    Read, D.E.2    Deepti, A.3
  • 49
    • 1842843860 scopus 로고    scopus 로고
    • Coupling endoplasmic reticulum stress to the cell death program
    • DOI 10.1038/sj.cdd.4401378
    • Rao R. V., Ellerby H. M., Bredesen D. E., Coupling endoplasmic reticulum stress to the cell death program. Cell Death and Differentiation 2004 11 4 372 380 2-s2.0-1842843860 10.1038/sj.cdd.4401378 (Pubitemid 38489415)
    • (2004) Cell Death and Differentiation , vol.11 , Issue.4 , pp. 372-380
    • Rao, R.V.1    Ellerby, H.M.2    Bredesen, D.E.3
  • 50
    • 1442321303 scopus 로고    scopus 로고
    • Activation signal of nuclear factor-κB in response to endoplasmic reticulum stress is transduced via IRE1 and tumor necrosis factor receptor-associated factor 2
    • Kaneko M., Niinuma Y., Nomura Y., Activation signal of nuclear factor- B in response to endoplasmic reticulum stress is transduced via IRE1 and tumor necrosis factor receptor-associated factor 2. Biological and Pharmaceutical Bulletin 2003 26 7 931 935 2-s2.0-1442321303 (Pubitemid 41685414)
    • (2003) Biological and Pharmaceutical Bulletin , vol.26 , Issue.7 , pp. 931-935
    • Kaneko, M.1    Niinuma, Y.2    Nomura, Y.3
  • 51
    • 36049049392 scopus 로고    scopus 로고
    • IRE1 signaling affects cell fate during the unfolded protein response
    • DOI 10.1126/science.1146361
    • Lin J. H., Li H., Yasumura D., Cohen H. R., Zhang C., Panning B., Shokat K. M., LaVail M. M., Walter P., IRE1 signaling affects cell fate during the unfolded protein response. Science 2007 318 5852 944 949 2-s2.0-36049049392 10.1126/science.1146361 (Pubitemid 350098984)
    • (2007) Science , vol.318 , Issue.5852 , pp. 944-949
    • Lin, J.H.1    Li, H.2    Yasumura, D.3    Cohen, H.R.4    Zhang, C.5    Panning, B.6    Shokat, K.M.7    LaVail, M.M.8    Walter, P.9
  • 53
    • 68049110633 scopus 로고    scopus 로고
    • IRE1 α kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates
    • 2-s2.0-68049110633 10.1016/j.cell.2009.07.017
    • Han D., Lerner A. G., Vande Walle L., Upton J. P., Xu W., Hagen A., Backes B. J., Oakes S. A., Papa F. R., IRE1 α kinase activation modes control alternate endoribonuclease outputs to determine divergent cell fates. Cell 2009 138 3 562 575 2-s2.0-68049110633 10.1016/j.cell.2009.07.017
    • (2009) Cell , vol.138 , Issue.3 , pp. 562-575
    • Han, D.1    Lerner, A.G.2    Vande Walle, L.3    Upton, J.P.4    Xu, W.5    Hagen, A.6    Backes, B.J.7    Oakes, S.A.8    Papa, F.R.9
  • 56
    • 84858315403 scopus 로고    scopus 로고
    • Endothelial dysfunction in diabetes mellitus: Possible involvement of endoplasmic reticulum stress?
    • 481840 10.1155/2012/481840
    • Basha B., Samuel S. M., Triggle C. R., Endothelial dysfunction in diabetes mellitus: possible involvement of endoplasmic reticulum stress? Experimental Diabetes Research 2012 2012 14 481840 10.1155/2012/481840
    • (2012) Experimental Diabetes Research , vol.2012 , pp. 14
    • Basha, B.1    Samuel, S.M.2    Triggle, C.R.3
  • 58
    • 66449137379 scopus 로고    scopus 로고
    • GRP78 expression inhibits insulin and ER stress-induced SREBP-1c activation and reduces hepatic steatosis in mice
    • 2-s2.0-66449137379 10.1172/JCI37007
    • Kammoun H. L., Chabanon H., Hainault I., Luquet S., Magnan C., Koike T., Ferré P., Foufelle F., GRP78 expression inhibits insulin and ER stress-induced SREBP-1c activation and reduces hepatic steatosis in mice. Journal of Clinical Investigation 2009 119 5 1201 1215 2-s2.0-66449137379 10.1172/JCI37007
    • (2009) Journal of Clinical Investigation , vol.119 , Issue.5 , pp. 1201-1215
    • Kammoun, H.L.1    Chabanon, H.2    Hainault, I.3    Luquet, S.4    Magnan, C.5    Koike, T.6    Ferré, P.7    Foufelle, F.8
  • 59
    • 0034973982 scopus 로고    scopus 로고
    • Translational control is required for the unfolded protein response and in vivo glucose homeostasis
    • DOI 10.1016/S1097-2765(01)00265-9
    • Scheuner D., Song B., McEwen E., Liu C., Laybutt R., Gillespie P., Saunders T., Bonner-Weir S., Kaufman R. J., Translational control is required for the unfolded protein response and in vivo glucose homeostasis. Molecular Cell 2001 7 6 1165 1176 2-s2.0-0034973982 10.1016/S1097-2765(01)00265-9 (Pubitemid 32607351)
    • (2001) Molecular Cell , vol.7 , Issue.6 , pp. 1165-1176
    • Scheuner, D.1    Song, B.2    McEwen, E.3    Liu, C.4    Laybutt, R.5    Gillespie, P.6    Saunders, T.7    Bonner-Weir, S.8    Kaufman, R.J.9
  • 60
    • 0034968330 scopus 로고    scopus 로고
    • Diabetes mellitus and exocrine pancreatic dysfunction in Perk-/- mice reveals a role for translational control in secretory cell survival
    • DOI 10.1016/S1097-2765(01)00264-7
    • Harding H. P., Zeng H., Zhang Y., Jungries R., Chung P., Plesken H., Sabatini D. D., Ron D., Diabetes mellitus and exocrine pancreatic dysfunction in Perk-/- mice reveals a role for translational control in secretory cell survival. Molecular Cell 2001 7 6 1153 1163 2-s2.0-0034968330 10.1016/S1097-2765(01)00264-7 (Pubitemid 32607350)
    • (2001) Molecular Cell , vol.7 , Issue.6 , pp. 1153-1163
    • Harding, H.P.1    Zeng, H.2    Zhang, Y.3    Jungries, R.4    Chung, P.5    Plesken, H.6    Sabatini, D.D.7    Ron, D.8
  • 61
    • 67649450485 scopus 로고    scopus 로고
    • Translation attenuation through eIF2 α phosphorylation prevents oxidative stress and maintains the differentiated state in β cells
    • 2-s2.0-67649450485 10.1016/j.cmet.2009.06.002
    • Back S. H., Scheuner D., Han J., Song B., Ribick M., Wang J., Gildersleeve R. D., Pennathur S., Kaufman R. J., Translation attenuation through eIF2 α phosphorylation prevents oxidative stress and maintains the differentiated state in β cells. Cell Metabolism 2009 10 1 13 26 2-s2.0-67649450485 10.1016/j.cmet.2009.06.002
    • (2009) Cell Metabolism , vol.10 , Issue.1 , pp. 13-26
    • Back, S.H.1    Scheuner, D.2    Han, J.3    Song, B.4    Ribick, M.5    Wang, J.6    Gildersleeve, R.D.7    Pennathur, S.8    Kaufman, R.J.9
  • 63
    • 0036091476 scopus 로고    scopus 로고
    • The PERK eukaryotic initiation factor 2α kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas
    • DOI 10.1128/MCB.22.11.3864-3874.2002
    • Zhang P., McGrath B., Li S., Frank A., Zambito F., Reinert J., Gannon M., Ma K., McNaughton K., Cavener D. R., The PERK eukaryotic initiation factor 2 α kinase is required for the development of the skeletal system, postnatal growth, and the function and viability of the pancreas. Molecular and Cellular Biology 2002 22 11 3864 3874 2-s2.0-0036091476 10.1128/MCB.22.11.3864-3874.2002 (Pubitemid 34525227)
    • (2002) Molecular and Cellular Biology , vol.22 , Issue.11 , pp. 3864-3874
    • Zhang, P.1    McGrath, B.2    Li, S.3    Frank, A.4    Zambito, F.5    Reinert, J.6    Gannon, M.7    Ma, K.8    McNaughton, K.9    Cavener, D.R.10
  • 64
    • 28244435870 scopus 로고    scopus 로고
    • WFS1 is a novel component of the unfolded protein response and maintains homeostasis of the endoplasmic reticulum in pacreatic β-cells
    • DOI 10.1074/jbc.M507426200
    • Fonseca S. G., Fukuma M., Lipson K. L., Nguyen L. X., Allen J. R., Oka Y., Urano F., WFS1 is a novel component of the unfolded protein response and maintains homeostasis of the endoplasmic reticulum in pacreatic β -cells. Journal of Biological Chemistry 2005 280 47 39609 39615 2-s2.0-28244435870 10.1074/jbc.M507426200 (Pubitemid 41713920)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.47 , pp. 39609-39615
    • Fonseca, S.G.1    Fukuma, M.2    Lipson, K.L.3    Nguyen, L.X.4    Allen, J.R.5    Oka, Y.6    Urano, F.7
  • 65
    • 33748069813 scopus 로고    scopus 로고
    • Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes
    • DOI 10.1126/science.1128294
    • Özcan U., Yilmaz E., Özcan L., Furuhashi M., Vaillancourt E., Smith R. O., Görgün C. Z., Hotamisligil G. S., Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes. Science 2006 313 5790 1137 1140 2-s2.0-33748069813 10.1126/science.1128294 (Pubitemid 44300242)
    • (2006) Science , vol.313 , Issue.5790 , pp. 1137-1140
    • Ozcan, U.1    Yilmaz, E.2    Ozcan, L.3    Furuhashi, M.4    Vaillancourt, E.5    Smith, R.O.6    Gorgun, C.Z.7    Hotamisligil, G.S.8
  • 66
    • 38149136598 scopus 로고    scopus 로고
    • Inhibition of apolipoprotein B100 secretion by lipid-induced hepatic endoplasmic reticulum stress in rodents
    • 2-s2.0-38149136598 10.1172/JCI32752
    • Ota T., Gayet C., Ginsberg H. N., Inhibition of apolipoprotein B100 secretion by lipid-induced hepatic endoplasmic reticulum stress in rodents. Journal of Clinical Investigation 2008 118 1 316 332 2-s2.0-38149136598 10.1172/JCI32752
    • (2008) Journal of Clinical Investigation , vol.118 , Issue.1 , pp. 316-332
    • Ota, T.1    Gayet, C.2    Ginsberg, H.N.3
  • 67
    • 13644256191 scopus 로고    scopus 로고
    • A selective inhibitor of elF2α dephosphorylation protects cells from ER stress
    • DOI 10.1126/science.1101902
    • Boyce M., Bryant K. F., Jousse C., Long K., Harding H. P., Scheuner D., Kaufman R. J., Ma D., Coen D. M., Ron D., Yuan J., A selective inhibitor of elF2 α dephosphorylation protects cells from ER stress. Science 2005 307 5711 935 939 2-s2.0-13644256191 10.1126/science.1101902 (Pubitemid 40229232)
    • (2005) Science , vol.307 , Issue.5711 , pp. 935-939
    • Boyce, M.1    Bryant, K.F.2    Jousse, C.3    Long, K.4    Harding, H.P.5    Scheuner, D.6    Kaufman, R.J.7    Ma, D.8    Coen, D.M.9    Ron, D.10    Yuan, J.11
  • 68
    • 33747849846 scopus 로고    scopus 로고
    • Regulation of insulin biosynthesis in pancreatic beta cells by an endoplasmic reticulum-resident protein kinase IRE1
    • DOI 10.1016/j.cmet.2006.07.007, PII S1550413106002701
    • Lipson K. L., Fonseca S. G., Ishigaki S., Nguyen L. X., Foss E., Bortell R., Rossini A. A., Urano F., Regulation of insulin biosynthesis in pancreatic beta cells by an endoplasmic reticulum-resident protein kinase IRE1. Cell Metabolism 2006 4 3 245 254 2-s2.0-33747849846 10.1016/j.cmet.2006.07.007 (Pubitemid 44283955)
    • (2006) Cell Metabolism , vol.4 , Issue.3 , pp. 245-254
    • Lipson, K.L.1    Fonseca, S.G.2    Ishigaki, S.3    Nguyen, L.X.4    Foss, E.5    Bortell, R.6    Rossini, A.A.7    Urano, F.8
  • 69
    • 33846569938 scopus 로고    scopus 로고
    • Targeting mammalian target of rapamycin (mTOR) for health and diseases
    • DOI 10.1016/j.drudis.2006.12.008, PII S1359644606004910
    • Tsang C. K., Qi H., Liu L. F., Zheng X. F. S., Targeting mammalian target of rapamycin (mTOR) for health and diseases. Drug Discovery Today 2007 12 3-4 112 124 2-s2.0-33846569938 10.1016/j.drudis.2006.12.008 (Pubitemid 46176669)
    • (2007) Drug Discovery Today , vol.12 , Issue.3-4 , pp. 112-124
    • Tsang, C.K.1    Qi, H.2    Liu, L.F.3    Zheng, X.F.S.4
  • 70
    • 65349177200 scopus 로고    scopus 로고
    • AMPK: An emerging drug target for diabetes and the metabolic syndrome
    • 2-s2.0-65349177200 10.1016/j.cmet.2009.03.012
    • Zhang B. B., Zhou G., Li C., AMPK: an emerging drug target for diabetes and the metabolic syndrome. Cell Metabolism 2009 9 5 407 416 2-s2.0-65349177200 10.1016/j.cmet.2009.03.012
    • (2009) Cell Metabolism , vol.9 , Issue.5 , pp. 407-416
    • Zhang, B.B.1    Zhou, G.2    Li, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.