메뉴 건너뛰기




Volumn 124, Issue 8, 2014, Pages 3489-3500

Autophagy defends pancreatic β cells from Human islet amyloid polypeptide-induced toxicity

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PROTEIN; OLIGOMER; POLYPEPTIDE; AMYLIN; HEAT SHOCK PROTEIN; INSULIN; NFE2L2 PROTEIN, MOUSE; RECOMBINANT PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; SQSTM1 PROTEIN, MOUSE; TRANSCRIPTION FACTOR NRF2;

EID: 84905460026     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI71981     Document Type: Article
Times cited : (195)

References (54)
  • 1
    • 0037219411 scopus 로고    scopus 로고
    • β-Cell deficit and increased β-cell apoptosis in humans with type 2 diabetes
    • Butler AE, Janson J, Bonner-Weir S, Ritzel R, Rizza RA, Butler PC. β-Cell deficit and increased β-cell apoptosis in humans with type 2 diabetes. Diabetes. 2003;52(1):102-110.
    • (2003) Diabetes , vol.52 , Issue.1 , pp. 102-110
    • Butler, A.E.1    Janson, J.2    Bonner-Weir, S.3    Ritzel, R.4    Rizza, R.A.5    Butler, P.C.6
  • 2
    • 43549100675 scopus 로고    scopus 로고
    • Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis
    • Haataja L, Gurlo T, Huang CJ, Butler PC. Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis. Endocr Rev. 2008;29(3):303-316.
    • (2008) Endocr Rev. , vol.29 , Issue.3 , pp. 303-316
    • Haataja, L.1    Gurlo, T.2    Huang, C.J.3    Butler, P.C.4
  • 3
    • 76149102617 scopus 로고    scopus 로고
    • Evidence for proteotoxicity in β cells in type 2 diabetes: Toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway
    • Gurlo T, et al. Evidence for proteotoxicity in β cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway. Am J Pathol. 2010;176(2):861-869.
    • (2010) Am J Pathol. , vol.176 , Issue.2 , pp. 861-869
    • Gurlo, T.1
  • 4
    • 2542581025 scopus 로고    scopus 로고
    • Diabetes due to a progressive defect in β-cell mass in rats transgenic for human islet amyloid polypeptide (HIP rat) - A new model for type 2 diabetes
    • Butler AE, Jang J, Gurlo T, Carty MD, Soeller WC, Butler PC. Diabetes due to a progressive defect in β-cell mass in rats transgenic for human islet amyloid polypeptide (HIP rat) - a new model for type 2 diabetes. Diabetes. 2004;53(6):1509-1516.
    • (2004) Diabetes , vol.53 , Issue.6 , pp. 1509-1516
    • Butler, A.E.1    Jang, J.2    Gurlo, T.3    Carty, M.D.4    Soeller, W.C.5    Butler, P.C.6
  • 5
    • 0141780910 scopus 로고    scopus 로고
    • Extensive islet amyloid formation is induced by development of type II diabetes mellitus and contributes to its progression: Pathogenesis of diabetes in a mouse model
    • Hoppener J W M, et al. Extensive islet amyloid formation is induced by development of type II diabetes mellitus and contributes to its progression: pathogenesis of diabetes in a mouse model. Diabetologia. 1999;42(4):427-434.
    • (1999) Diabetologia , vol.42 , Issue.4 , pp. 427-434
    • Hoppener, J.W.M.1
  • 6
    • 37149012111 scopus 로고    scopus 로고
    • Induction of endoplasmic reticulum stress-induced β-cell apoptosis and accumulation of polyubiquitinated proteins by human islet amyloid polypeptide
    • Huang CJ, et al. Induction of endoplasmic reticulum stress-induced β-cell apoptosis and accumulation of polyubiquitinated proteins by human islet amyloid polypeptide. Am J Physiol Endocrinol Metab. 2007;293(6):E1656- E1662.
    • (2007) Am J Physiol Endocrinol Metab. , vol.293 , Issue.6
    • Huang, C.J.1
  • 7
    • 34547638958 scopus 로고    scopus 로고
    • High expression rates of human islet amyloid polypeptide induce endoplasmic reticulum stress-mediated β-cell apoptosis, a characteristic of humans with type 2 but not type 1 diabetes
    • Huang CJ, et al. High expression rates of human islet amyloid polypeptide induce endoplasmic reticulum stress-mediated β-cell apoptosis, a characteristic of humans with type 2 but not type 1 diabetes. Diabetes. 2007;56(8):2016-2027.
    • (2007) Diabetes , vol.56 , Issue.8 , pp. 2016-2027
    • Huang, C.J.1
  • 8
    • 65549142204 scopus 로고    scopus 로고
    • A role for ubiquitin in selective autophagy
    • Kirkin V, McEwan DG, Novak I, Dikic I. A role for ubiquitin in selective autophagy. Mol Cell. 2009;34(3):259-269.
    • (2009) Mol Cell. , vol.34 , Issue.3 , pp. 259-269
    • Kirkin, V.1    McEwan, D.G.2    Novak, I.3    Dikic, I.4
  • 9
    • 52749093177 scopus 로고    scopus 로고
    • Autophagy is important in islet homeostasis and compensatory increase of β cell mass in response to high-fat diet
    • Ebato C, et al. Autophagy is important in islet homeostasis and compensatory increase of β cell mass in response to high-fat diet. Cell Metab. 2008;8(4):325-332.
    • (2008) Cell Metab. , vol.8 , Issue.4 , pp. 325-332
    • Ebato, C.1
  • 10
    • 52749094770 scopus 로고    scopus 로고
    • Loss of autophagy diminishes pancreatic β cell mass and function with resultant hyperglycemia
    • Jung HS, et al. Loss of autophagy diminishes pancreatic β cell mass and function with resultant hyperglycemia. Cell Metab. 2008;8(4):318-324.
    • (2008) Cell Metab. , vol.8 , Issue.4 , pp. 318-324
    • Jung, H.S.1
  • 11
    • 84875416620 scopus 로고    scopus 로고
    • Stimulation of autophagy improves endoplasmic reticulum stressinduced diabetes
    • Bachar-Wikstrom E, et al. Stimulation of autophagy improves endoplasmic reticulum stressinduced diabetes. Diabetes. 2013;62(4):1227-1237.
    • (2013) Diabetes , vol.62 , Issue.4 , pp. 1227-1237
    • Bachar-Wikstrom, E.1
  • 12
    • 0028954799 scopus 로고
    • Non-parallelism of islet amyloid polypeptide (amylin) and insulin gene expression in rats islets following dexamethasone treatment
    • Mulder H, Ahren B, Stridsberg M, Sundler F. Non-parallelism of islet amyloid polypeptide (amylin) and insulin gene expression in rats islets following dexamethasone treatment. Diabetologia. 1995;38(4):395-402.
    • (1995) Diabetologia , vol.38 , Issue.4 , pp. 395-402
    • Mulder, H.1    Ahren, B.2    Stridsberg, M.3    Sundler, F.4
  • 14
    • 79251498807 scopus 로고    scopus 로고
    • Protein homeostasis and aging: The importance of exquisite quality control
    • Koga H, Kaushik S, Cuervo AM. Protein homeostasis and aging: The importance of exquisite quality control. Ageing Res Rev. 2011;10(2):205-215.
    • (2011) Ageing Res Rev. , vol.10 , Issue.2 , pp. 205-215
    • Koga, H.1    Kaushik, S.2    Cuervo, A.M.3
  • 15
    • 79951672803 scopus 로고    scopus 로고
    • Human-IAPP disrupts the autophagy/lysosomal pathway in pancreatic β-cells: Protective role of p62-positive cytoplasmic inclusions
    • Rivera JF, et al. Human-IAPP disrupts the autophagy/lysosomal pathway in pancreatic β-cells: protective role of p62-positive cytoplasmic inclusions. Cell Death Differ. 2011;18(3):415-426.
    • (2011) Cell Death Differ. , vol.18 , Issue.3 , pp. 415-426
    • Rivera, J.F.1
  • 16
    • 37649024076 scopus 로고    scopus 로고
    • Small molecule regulators of autophagy identified by an image-based high-throughput screen
    • Zhang L, et al. Small molecule regulators of autophagy identified by an image-based high-throughput screen. Proc Natl Acad Sci U S A. 2007;104(48):19023-19028.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , Issue.48 , pp. 19023-19028
    • Zhang, L.1
  • 17
    • 78751490442 scopus 로고    scopus 로고
    • β-Cell dysfunctional ERAD/ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCHL1 deficiency
    • Costes S, et al. β-Cell dysfunctional ERAD/ubiquitin/proteasome system in type 2 diabetes mediated by islet amyloid polypeptide-induced UCHL1 deficiency. Diabetes. 2011;60(1):227-238.
    • (2011) Diabetes , vol.60 , Issue.1 , pp. 227-238
    • Costes, S.1
  • 18
    • 79953198258 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 promotes pancreatic β-cell survival via Fak-Akt signaling pathways
    • Daval M, Gurlo T, Costes S, Huang CJ, Butler PC. Cyclin-dependent kinase 5 promotes pancreatic β-cell survival via Fak-Akt signaling pathways. Diabetes. 2011;60(4):1186-1197.
    • (2011) Diabetes , vol.60 , Issue.4 , pp. 1186-1197
    • Daval, M.1    Gurlo, T.2    Costes, S.3    Huang, C.J.4    Butler, P.C.5
  • 19
    • 73649114570 scopus 로고    scopus 로고
    • Calcium-activated calpain-2 is a mediator of β cell dysfunction and apoptosis in type 2 diabetes
    • Huang CJ, et al. Calcium-activated calpain-2 is a mediator of β cell dysfunction and apoptosis in type 2 diabetes. J Biol Chem. 2010;285(1):339-348.
    • (2010) J Biol Chem. , vol.285 , Issue.1 , pp. 339-348
    • Huang, C.J.1
  • 20
    • 43749109844 scopus 로고    scopus 로고
    • Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1
    • Shaw BF, et al. Detergent-insoluble aggregates associated with amyotrophic lateral sclerosis in transgenic mice contain primarily full-length, unmodified superoxide dismutase-1. J Biol Chem. 2008;283(13):8340-8350.
    • (2008) J Biol Chem. , vol.283 , Issue.13 , pp. 8340-8350
    • Shaw, B.F.1
  • 21
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, et al. Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science. 2003;300(5618):486-489.
    • (2003) Science , vol.300 , Issue.5618 , pp. 486-489
    • Kayed, R.1
  • 22
    • 84891719799 scopus 로고    scopus 로고
    • Evidence for rapamycin toxicity in pancreatic β-cells and a review of the underlying molecular mechanisms
    • Barlow AD, Nicholson ML, Herbert TP. Evidence for rapamycin toxicity in pancreatic β-cells and a review of the underlying molecular mechanisms. Diabetes. 2013;62(8):2674-2682.
    • (2013) Diabetes , vol.62 , Issue.8 , pp. 2674-2682
    • Barlow, A.D.1    Nicholson, M.L.2    Herbert, T.P.3
  • 23
    • 0024593798 scopus 로고
    • Inhibition of calpain in intact platelets by the thiol protease inhibitor E-64d
    • McGowan EB, Becker E, Detwiler TC. Inhibition of calpain in intact platelets by the thiol protease inhibitor E-64d. Biochem Biophys Res Commun. 1989;158(2):432-435.
    • (1989) Biochem Biophys Res Commun. , vol.158 , Issue.2 , pp. 432-435
    • McGowan, E.B.1    Becker, E.2    Detwiler, T.C.3
  • 25
    • 84862295360 scopus 로고    scopus 로고
    • Guidelines for the use and interpretation of assays for monitoring autophagy
    • Klionsky DJ, et al. Guidelines for the use and interpretation of assays for monitoring autophagy. Autophagy. 2012;8(4):445-544.
    • (2012) Autophagy , vol.8 , Issue.4 , pp. 445-544
    • Klionsky, D.J.1
  • 26
    • 59849126863 scopus 로고    scopus 로고
    • Biochemical and morphological detection of inclusion bodies in autophagy-deficient mice
    • Waguri S, Komatsu M. Biochemical and morphological detection of inclusion bodies in autophagy-deficient mice. Methods Enzymol. 2009;453:181-196.
    • (2009) Methods Enzymol. , vol.453 , pp. 181-196
    • Waguri, S.1    Komatsu, M.2
  • 27
    • 0029742232 scopus 로고    scopus 로고
    • Treatment with growth hormone and dexamethasone in mice transgenic for human islet amyloid polypeptide causes islet amyloidosis and β-cell dysfunction
    • Couce M, et al. Treatment with growth hormone and dexamethasone in mice transgenic for human islet amyloid polypeptide causes islet amyloidosis and β-cell dysfunction. Diabetes. 1996;45(8):1094-1101.
    • (1996) Diabetes , vol.45 , Issue.8 , pp. 1094-1101
    • Couce, M.1
  • 28
    • 77952409809 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress mediate the physiological impairment induced by the disruption of autophagy
    • Wu JJ, et al. Mitochondrial dysfunction and oxidative stress mediate the physiological impairment induced by the disruption of autophagy. Aging (Albany NY). 2009;1(4):425-437.
    • (2009) Aging (Albany NY) , vol.1 , Issue.4 , pp. 425-437
    • Wu, J.J.1
  • 29
    • 5644248079 scopus 로고    scopus 로고
    • Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet β cells in diabetes
    • Robertson RP. Chronic oxidative stress as a central mechanism for glucose toxicity in pancreatic islet β cells in diabetes. J Biol Chem. 2004;279(41):42351-42354.
    • (2004) J Biol Chem. , vol.279 , Issue.41 , pp. 42351-42354
    • Robertson, R.P.1
  • 30
    • 34547673497 scopus 로고    scopus 로고
    • Peroxynitrite: Biochemistry, pathophysiology and development of therapeutics
    • Szabo C, Ischiropoulos H, Radi R. Peroxynitrite: biochemistry, pathophysiology and development of therapeutics. Nat Rev Drug Discov. 2007;6(8):662-680.
    • (2007) Nat Rev Drug Discov. , vol.6 , Issue.8 , pp. 662-680
    • Szabo, C.1    Ischiropoulos, H.2    Radi, R.3
  • 31
    • 77649265091 scopus 로고    scopus 로고
    • The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1
    • Komatsu M, et al. The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1. Nat Cell Biol. 2010;12(3):213-223.
    • (2010) Nat Cell Biol. , vol.12 , Issue.3 , pp. 213-223
    • Komatsu, M.1
  • 32
    • 36849089101 scopus 로고    scopus 로고
    • Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagydeficient mice
    • Komatsu M, et al. Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagydeficient mice. Cell. 2007;131(6):1149-1163.
    • (2007) Cell , vol.131 , Issue.6 , pp. 1149-1163
    • Komatsu, M.1
  • 33
    • 77953366801 scopus 로고    scopus 로고
    • A noncanonical mechanism of Nrf2 activation by autophagy deficiency: Direct interaction between Keap1 and p62
    • Lau A, et al. A noncanonical mechanism of Nrf2 activation by autophagy deficiency: direct interaction between Keap1 and p62. Mol Cell Biol. 2010;30(13):3275-3285.
    • (2010) Mol Cell Biol. , vol.30 , Issue.13 , pp. 3275-3285
    • Lau, A.1
  • 34
    • 79954416526 scopus 로고    scopus 로고
    • The cytoprotective role of the Keap1-Nrf2 pathway
    • Baird L, Dinkova-Kostova AT. The cytoprotective role of the Keap1-Nrf2 pathway. Arch Toxicol. 2011;85(4):241-272.
    • (2011) Arch Toxicol. , vol.85 , Issue.4 , pp. 241-272
    • Baird, L.1    Dinkova-Kostova, A.T.2
  • 35
    • 33646418968 scopus 로고    scopus 로고
    • Activation of Nrf2/ARE pathway protects endothelial cells from oxidant injury and inhibits inflammatory gene expression
    • Chen XL, et al. Activation of Nrf2/ARE pathway protects endothelial cells from oxidant injury and inhibits inflammatory gene expression. Am J Physiol Heart Circ Physiol. 2006;290(5):H1862-H1870.
    • (2006) Am J Physiol Heart Circ Physiol. , vol.290 , Issue.5
    • Chen, X.L.1
  • 36
    • 0036854702 scopus 로고    scopus 로고
    • The transcriptional activation of the human copper/zinc superoxide dismutase gene by 2, 3, 7, 8-tetrachlorodibenzo-p-dioxin through two different regulator sites, the antioxidant responsive element and xenobiotic responsive element
    • Park EY, Rho HM. The transcriptional activation of the human copper/zinc superoxide dismutase gene by 2, 3, 7, 8-tetrachlorodibenzo-p-dioxin through two different regulator sites, the antioxidant responsive element and xenobiotic responsive element. Mol Cell Biochem. 2002;240(1-2):47-55.
    • (2002) Mol Cell Biochem. , vol.240 , Issue.1-2 , pp. 47-55
    • Park, E.Y.1    Rho, H.M.2
  • 37
    • 6344291668 scopus 로고    scopus 로고
    • Activation of transcription factor Nrf-2 and its downstream targets in response to moloney murine leukemia virus ts1-induced thiol depletion and oxidative stress in astrocytes
    • Qiang W, et al. Activation of transcription factor Nrf-2 and its downstream targets in response to moloney murine leukemia virus ts1-induced thiol depletion and oxidative stress in astrocytes. J Virol. 2004;78(21):11926-11938.
    • (2004) J Virol. , vol.78 , Issue.21 , pp. 11926-11938
    • Qiang, W.1
  • 38
    • 84888224672 scopus 로고    scopus 로고
    • Exendin-4 improves β-cell function in autophagy-deficient β-cells
    • Abe H, et al. Exendin-4 improves β-cell function in autophagy-deficient β-cells. Endocrinology. 2013;154(12):4512-4524.
    • (2013) Endocrinology , vol.154 , Issue.12 , pp. 4512-4524
    • Abe, H.1
  • 39
    • 67349150186 scopus 로고    scopus 로고
    • Autophagy in human type 2 diabetes pancreatic β cells
    • Masini M, et al. Autophagy in human type 2 diabetes pancreatic β cells. Diabetologia. 2009;52(6):1083-1086.
    • (2009) Diabetologia , vol.52 , Issue.6 , pp. 1083-1086
    • Masini, M.1
  • 40
    • 77953139736 scopus 로고    scopus 로고
    • Fighting disease by selective autophagy of aggregate-prone proteins
    • Knaevelsrud H, Simonsen A. Fighting disease by selective autophagy of aggregate-prone proteins. FEBS Lett. 2010;584(12):2635-2645.
    • (2010) FEBS Lett. , vol.584 , Issue.12 , pp. 2635-2645
    • Knaevelsrud, H.1    Simonsen, A.2
  • 41
    • 79952355107 scopus 로고    scopus 로고
    • Selective autophagy mediated by autophagic adapter proteins
    • Johansen T, Lamark T. Selective autophagy mediated by autophagic adapter proteins. Autophagy. 2011;7(3):279-296.
    • (2011) Autophagy , vol.7 , Issue.3 , pp. 279-296
    • Johansen, T.1    Lamark, T.2
  • 42
    • 0028123618 scopus 로고
    • Islet amyloid polypeptide in human insulinomas. Evidence for intracellular amyloidogenesis
    • O'Brien TD, Butler AE, Roche PC, Johnson KH, Butler PC. Islet amyloid polypeptide in human insulinomas. Evidence for intracellular amyloidogenesis. Diabetes. 1994;43(2):329-336.
    • (1994) Diabetes , vol.43 , Issue.2 , pp. 329-336
    • O'Brien, T.D.1    Butler, A.E.2    Roche, P.C.3    Johnson, K.H.4    Butler, P.C.5
  • 43
    • 27944504351 scopus 로고    scopus 로고
    • P62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death
    • Bjorkoy G, et al. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. J Cell Biol. 2005;171(4):603-614.
    • (2005) J Cell Biol. , vol.171 , Issue.4 , pp. 603-614
    • Bjorkoy, G.1
  • 44
    • 84871742997 scopus 로고    scopus 로고
    • P62/SQSTM1-dependent autophagy of Lewy body-like alpha-synuclein inclusions
    • Watanabe Y, et al. p62/SQSTM1-dependent autophagy of Lewy body-like alpha-synuclein inclusions. PLoS One. 2012;7(12):e52868.
    • (2012) PLoS One , vol.7 , Issue.12
    • Watanabe, Y.1
  • 45
    • 77953161017 scopus 로고    scopus 로고
    • Proteomics analysis of bladder cancer exosomes
    • Welton JL, et al. Proteomics analysis of bladder cancer exosomes. Mol Cell Proteomics. 2010;9(6):1324-1338.
    • (2010) Mol Cell Proteomics. , vol.9 , Issue.6 , pp. 1324-1338
    • Welton, J.L.1
  • 46
    • 84865307818 scopus 로고    scopus 로고
    • Exosomal cell-to-cell transmission of alpha synuclein oligomers
    • Danzer KM, et al. Exosomal cell-to-cell transmission of alpha synuclein oligomers. Mol Neurodegener. 2012;7:42.
    • (2012) Mol Neurodegener. , vol.7 , pp. 42
    • Danzer, K.M.1
  • 47
    • 84867875430 scopus 로고    scopus 로고
    • Involvement of the Nrf2-proteasome pathway in the endoplasmic reticulum stress response in pancreatic β-cells
    • Lee S, Hur EG, Ryoo IG, Jung KA, Kwak J, Kwak MK. Involvement of the Nrf2-proteasome pathway in the endoplasmic reticulum stress response in pancreatic β-cells. Toxicol Appl Pharmacol. 2012;264(3):431-438.
    • (2012) Toxicol Appl Pharmacol. , vol.264 , Issue.3 , pp. 431-438
    • Lee, S.1    Hur, E.G.2    Ryoo, I.G.3    Jung, K.A.4    Kwak, J.5    Kwak, M.K.6
  • 48
    • 84880682182 scopus 로고    scopus 로고
    • The Keap1-Nrf2 system prevents onset of diabetes mellitus
    • Uruno A, et al. The Keap1-Nrf2 system prevents onset of diabetes mellitus. Mol Cell Biol. 2013;33(15):2996-3010.
    • (2013) Mol Cell Biol. , vol.33 , Issue.15 , pp. 2996-3010
    • Uruno, A.1
  • 49
    • 84893132156 scopus 로고    scopus 로고
    • Nrf2 protects pancreatic β-cells from oxidative and nitrosative stress in diabetic model mice
    • Yagishita Y, et al. Nrf2 protects pancreatic β-cells from oxidative and nitrosative stress in diabetic model mice. Diabetes. 2014;63(2):605-618.
    • (2014) Diabetes , vol.63 , Issue.2 , pp. 605-618
    • Yagishita, Y.1
  • 50
    • 84863430453 scopus 로고    scopus 로고
    • Mitophagy: A complex mechanism of mitochondrial removal
    • Novak I. Mitophagy: a complex mechanism of mitochondrial removal. Antioxid Redox Signal. 2012;17(5):794-802.
    • (2012) Antioxid Redox Signal. , vol.17 , Issue.5 , pp. 794-802
    • Novak, I.1
  • 51
    • 21044455137 scopus 로고    scopus 로고
    • Impairment of starvationinduced and constitutive autophagy in Atg7-deficient mice
    • Komatsu M, et al. Impairment of starvationinduced and constitutive autophagy in Atg7-deficient mice. J Cell Biol. 2005;169(3):425-434.
    • (2005) J Cell Biol. , vol.169 , Issue.3 , pp. 425-434
    • Komatsu, M.1
  • 52
    • 0034121735 scopus 로고    scopus 로고
    • Adult insulin- and glucagon-producing cells differentiate from two independent cell lineages
    • Herrera PL. Adult insulin- and glucagon-producing cells differentiate from two independent cell lineages. Development. 2000;127(11):2317-2322.
    • (2000) Development. , vol.127 , Issue.11 , pp. 2317-2322
    • Herrera, P.L.1
  • 53
    • 65449133190 scopus 로고    scopus 로고
    • The alpha-glucosidase inhibitor acarbose prevents obesity and simple steatosis in sequestosome 1/A170/p62 deficient mice
    • Okada K, et al. The alpha-glucosidase inhibitor acarbose prevents obesity and simple steatosis in sequestosome 1/A170/p62 deficient mice. Hepatol Res. 2009;39(5):490-500.
    • (2009) Hepatol Res. , vol.39 , Issue.5 , pp. 490-500
    • Okada, K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.