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Volumn 53, Issue 7, 2010, Pages 1415-1427

Erratum: Differences between amyloid toxicity in alpha and beta cells in human and mouse islets and the role of caspase-3 (Diabetologia DOI: 10.1007/s00125-010-1717-9);Differences between amyloid toxicity in alpha and beta cells in human and mouse islets and the role of caspase-3

Author keywords

Alpha cell apoptosis; Amylin; Amyloid; Beta cell apoptosis; Caspase 3; Islet amyloid polypeptide; Type 2 diabetes

Indexed keywords

AMYLIN; AMYLOID; CASPASE 3; CASPASE 3 INHIBITOR; CONGO RED;

EID: 77955658749     PISSN: 0012186X     EISSN: 14320428     Source Type: Journal    
DOI: 10.1007/s00125-013-2967-0     Document Type: Erratum
Times cited : (34)

References (49)
  • 1
    • 18644376240 scopus 로고    scopus 로고
    • Type 2 diabetes, insulin secretion and beta-cell mass
    • Ahren B (2005) Type 2 diabetes, insulin secretion and beta-cell mass. Curr Mol Med 5:275-286.
    • (2005) Curr Mol Med , vol.5 , pp. 275-286
    • Ahren, B.1
  • 3
    • 0037379714 scopus 로고    scopus 로고
    • Islet amyloid polypeptide and type 2 diabetes
    • Marzban L, Park K, Verchere CB (2003) Islet amyloid polypeptide and type 2 diabetes. Exp Gerontol 38:347-351.
    • (2003) Exp Gerontol , vol.38 , pp. 347-351
    • Marzban, L.1    Park, K.2    Verchere, C.B.3
  • 4
    • 43549100675 scopus 로고    scopus 로고
    • Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis
    • Haataja L, Gurlo T, Huang CJ, Butler PC (2008) Islet amyloid in type 2 diabetes, and the toxic oligomer hypothesis. Endocr Rev 29:303-316.
    • (2008) Endocr Rev , vol.29 , pp. 303-316
    • Haataja, L.1    Gurlo, T.2    Huang, C.J.3    Butler, P.C.4
  • 5
    • 1542375103 scopus 로고    scopus 로고
    • Islet amyloid: A complication of islet dysfunction or an aetiological factor in type 2 diabetes?
    • Clark A, Nilsson MR (2004) Islet amyloid: a complication of islet dysfunction or an aetiological factor in type 2 diabetes? Diabetologia 47:157-169.
    • (2004) Diabetologia , vol.47 , pp. 157-169
    • Clark, A.1    Nilsson, M.R.2
  • 6
    • 0023192941 scopus 로고
    • Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells
    • Westermark P, Wernstedt C, Wilander E, Hayden DW, O'Brien TD, Johnson KH (1987) Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc Natl Acad Sci USA 84:3881-3885.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3881-3885
    • Westermark, P.1    Wernstedt, C.2    Wilander, E.3    Hayden, D.W.4    O'Brien, T.D.5    Johnson, K.H.6
  • 7
    • 0023579739 scopus 로고
    • Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients
    • Cooper GJ, Willis AC, Clark A, Turner RC, Sim RB, Reid KB (1987) Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci USA 84:8628-8632.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8628-8632
    • Cooper, G.J.1    Willis, A.C.2    Clark, A.3    Turner, R.C.4    Sim, R.B.5    Reid, K.B.6
  • 8
    • 58149343826 scopus 로고    scopus 로고
    • Small interfering RNA-mediated suppression of proislet amyloid polypeptide expression inhibits islet amyloid formation and enhances survival of human islets in culture
    • Marzban L, Tomas A, Becker TC et al (2008) Small interfering RNA-mediated suppression of proislet amyloid polypeptide expression inhibits islet amyloid formation and enhances survival of human islets in culture. Diabetes 57:3045-3055.
    • (2008) Diabetes , vol.57 , pp. 3045-3055
    • Marzban, L.1    Tomas, A.2    Becker, T.C.3
  • 9
    • 0032937607 scopus 로고    scopus 로고
    • Differences in amyloid deposition in islets of transgenic mice expressing human islet amyloid polypeptide vs human islets implanted into nude mice
    • Westermark G, Westermark P, Eizirik DL et al (1999) Differences in amyloid deposition in islets of transgenic mice expressing human islet amyloid polypeptide vs human islets implanted into nude mice. Metabolism 48:448-454.
    • (1999) Metabolism , vol.48 , pp. 448-454
    • Westermark, G.1    Westermark, P.2    Eizirik, D.L.3
  • 10
    • 50449085533 scopus 로고    scopus 로고
    • Widespread amyloid deposition in transplanted human pancreatic islets
    • Westermark GT, Westermark P, Berne C, Korsgren O (2008) Widespread amyloid deposition in transplanted human pancreatic islets. N Engl J Med 359:977-979.
    • (2008) N Engl J Med , vol.359 , pp. 977-979
    • Westermark, G.T.1    Westermark, P.2    Berne, C.3    Korsgren, O.4
  • 11
    • 0024307842 scopus 로고
    • Co-localization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets
    • Lukinius A, Wilander E, Westermark GT, Engstrom U, Westermark P (1989) Co-localization of islet amyloid polypeptide and insulin in the B cell secretory granules of the human pancreatic islets. Diabetologia 32:240-244.
    • (1989) Diabetologia , vol.32 , pp. 240-244
    • Lukinius, A.1    Wilander, E.2    Westermark, G.T.3    Engstrom, U.4    Westermark, P.5
  • 12
    • 0025302287 scopus 로고
    • Evidence of cosecretion of islet amyloid polypeptide and insulin by beta-cells
    • Kahn SE, D'Alessio DA, Schwartz MW et al (1990) Evidence of cosecretion of islet amyloid polypeptide and insulin by beta-cells. Diabetes 39:634-638.
    • (1990) Diabetes , vol.39 , pp. 634-638
    • Kahn, S.E.1    D'Alessio, D.A.2    Schwartz, M.W.3
  • 13
    • 23744503963 scopus 로고    scopus 로고
    • Processing of pro-islet amyloid polypeptide in the constitutive and regulated secretory pathways of beta cells
    • Marzban L, Trigo-Gonzalez G, Verchere CB (2005) Processing of pro-islet amyloid polypeptide in the constitutive and regulated secretory pathways of beta cells. Mol Endocrinol 19:2154-2163.
    • (2005) Mol Endocrinol , vol.19 , pp. 2154-2163
    • Marzban, L.1    Trigo-Gonzalez, G.2    Verchere, C.B.3
  • 15
    • 0032969276 scopus 로고    scopus 로고
    • Islet amyloid: A long-recognized but underappreciated pathological feature of type 2 diabetes
    • Kahn SE, Andrikopoulos S, Verchere CB (1999) Islet amyloid: a long-recognized but underappreciated pathological feature of type 2 diabetes. Diabetes 48:241-253.
    • (1999) Diabetes , vol.48 , pp. 241-253
    • Kahn, S.E.1    Andrikopoulos, S.2    Verchere, C.B.3
  • 16
    • 33749318236 scopus 로고    scopus 로고
    • 2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell death
    • 2-terminal processing of human proislet amyloid polypeptide by the prohormone convertase PC2 leads to amyloid formation and cell death. Diabetes 55:2192-2201.
    • (2006) Diabetes , vol.55 , pp. 2192-2201
    • Marzban, L.1    Rhodes, C.J.2    Steiner, D.F.3    Haataja, L.4    Halban, P.A.5    Verchere, C.B.6
  • 17
    • 0032896436 scopus 로고    scopus 로고
    • Prolonged exposure of pancreatic beta cells to raised glucose concentrations results in increased cellular content of islet amyloid polypeptide precursors
    • Hou X, Ling Z, Quartier E et al (1999) Prolonged exposure of pancreatic beta cells to raised glucose concentrations results in increased cellular content of islet amyloid polypeptide precursors. Diabetologia 42:188-194.
    • (1999) Diabetologia , vol.42 , pp. 188-194
    • Hou, X.1    Ling, Z.2    Quartier, E.3
  • 18
    • 21344470854 scopus 로고    scopus 로고
    • Aberrant processing of human proislet amyloid polypeptide results in increased amyloid formation
    • Paulsson JF, Westermark GT (2005) Aberrant processing of human proislet amyloid polypeptide results in increased amyloid formation. Diabetes 54:2117-2125.
    • (2005) Diabetes , vol.54 , pp. 2117-2125
    • Paulsson, J.F.1    Westermark, G.T.2
  • 19
    • 0033048453 scopus 로고    scopus 로고
    • The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles
    • Janson J, Ashley RH, Harrison D, McIntyre S, Butler PC (1999) The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles. Diabetes 48:491-498.
    • (1999) Diabetes , vol.48 , pp. 491-498
    • Janson, J.1    Ashley, R.H.2    Harrison, D.3    McIntyre, S.4    Butler, P.C.5
  • 20
    • 20444496481 scopus 로고    scopus 로고
    • Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers
    • Demuro A, Mina E, Kayed R, Milton SC, Parker I, Glabe CG (2005) Calcium dysregulation and membrane disruption as a ubiquitous neurotoxic mechanism of soluble amyloid oligomers. J Biol Chem 280:17294-17300.
    • (2005) J Biol Chem , vol.280 , pp. 17294-17300
    • Demuro, A.1    Mina, E.2    Kayed, R.3    Milton, S.C.4    Parker, I.5    Glabe, C.G.6
  • 21
    • 43149118349 scopus 로고    scopus 로고
    • Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane
    • Engel MF, Khemtemourian L, Kleijer CC et al (2008) Membrane damage by human islet amyloid polypeptide through fibril growth at the membrane. Proc Natl Acad Sci USA 105:6033-6038.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 6033-6038
    • Engel, M.F.1    Khemtemourian, L.2    Kleijer, C.C.3
  • 22
    • 0037167613 scopus 로고    scopus 로고
    • Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes
    • Anguiano M, Nowak RJ, Lansbury PT Jr (2002) Protofibrillar islet amyloid polypeptide permeabilizes synthetic vesicles by a pore-like mechanism that may be relevant to type II diabetes. Biochemistry 41:11338-11343.
    • (2002) Biochemistry , vol.41 , pp. 11338-11343
    • Anguiano, M.1    Nowak, R.J.2    Lansbury Jr., P.T.3
  • 23
    • 23044449398 scopus 로고    scopus 로고
    • Amyloid ion channels: A common structural link for protein-misfolding disease
    • Quist A, Doudevski I, Lin H et al (2005) Amyloid ion channels: a common structural link for protein-misfolding disease. Proc Natl Acad Sci USA 102:10427-10432.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 10427-10432
    • Quist, A.1    Doudevski, I.2    Lin, H.3
  • 24
    • 12244284221 scopus 로고    scopus 로고
    • Amylin-induced cytotoxicity is associated with activation of caspase-3 and MAP kinases
    • Rumora L, Hadzija M, Barisic K, Maysinger D, Grubiic TZ (2002) Amylin-induced cytotoxicity is associated with activation of caspase-3 and MAP kinases. Biol Chem 383:1751-1758.
    • (2002) Biol Chem , vol.383 , pp. 1751-1758
    • Rumora, L.1    Hadzija, M.2    Barisic, K.3    Maysinger, D.4    Grubiic, T.Z.5
  • 25
    • 0346101742 scopus 로고    scopus 로고
    • Fibrillogenic amylin evokes islet beta-cell apoptosis through linked activation of a caspase cascade and JNK1
    • Zhang S, Liu J, Dragunow M, Cooper GJ (2003) Fibrillogenic amylin evokes islet beta-cell apoptosis through linked activation of a caspase cascade and JNK1. J Biol Chem 278:52810-52819.
    • (2003) J Biol Chem , vol.278 , pp. 52810-52819
    • Zhang, S.1    Liu, J.2    Dragunow, M.3    Cooper, G.J.4
  • 26
    • 0026688125 scopus 로고
    • Localization of the basement membrane heparan sulfate proteoglycan in islet amyloid deposits in type II diabetes mellitus
    • Young ID, Ailles L, Narindrasorasak S, Tan R, Kisilevsky R (1992) Localization of the basement membrane heparan sulfate proteoglycan in islet amyloid deposits in type II diabetes mellitus. Arch Pathol Lab Med 116:951-954.
    • (1992) Arch Pathol Lab Med , vol.116 , pp. 951-954
    • Young, I.D.1    Ailles, L.2    Narindrasorasak, S.3    Tan, R.4    Kisilevsky, R.5
  • 27
    • 0035907265 scopus 로고    scopus 로고
    • Identification of a heparin binding domain in the N-terminal cleavage site of pro-islet amyloid polypeptide. Implications for islet amyloid formation
    • Park K, Verchere CB (2001) Identification of a heparin binding domain in the N-terminal cleavage site of pro-islet amyloid polypeptide. Implications for islet amyloid formation. J Biol Chem 276:16611-16616.
    • (2001) J Biol Chem , vol.276 , pp. 16611-16616
    • Park, K.1    Verchere, C.B.2
  • 28
    • 55649112259 scopus 로고    scopus 로고
    • Calcium elevation in mouse pancreatic beta cells evoked by extracellular human islet amyloid polypeptide involves activation of the mechanosensitive ion channel TRPV4
    • Casas S, Novials A, Reimann F, Gomis R, Gribble FM (2008) Calcium elevation in mouse pancreatic beta cells evoked by extracellular human islet amyloid polypeptide involves activation of the mechanosensitive ion channel TRPV4. Diabetologia 51:2252-2262.
    • (2008) Diabetologia , vol.51 , pp. 2252-2262
    • Casas, S.1    Novials, A.2    Reimann, F.3    Gomis, R.4    Gribble, F.M.5
  • 29
    • 58149340142 scopus 로고    scopus 로고
    • Spontaneous diabetes in hemizygous human amylin transgenic mice that developed neither islet amyloid nor peripheral insulin resistance
    • Wong WP, Scott DW, Chuang CL et al (2008) Spontaneous diabetes in hemizygous human amylin transgenic mice that developed neither islet amyloid nor peripheral insulin resistance. Diabetes 57:2737-2744.
    • (2008) Diabetes , vol.57 , pp. 2737-2744
    • Wong, W.P.1    Scott, D.W.2    Chuang, C.L.3
  • 30
    • 34547638958 scopus 로고    scopus 로고
    • High expression rates of human islet amyloid polypeptide induce endoplasmic reticulum stress mediated beta-cell apoptosis, a characteristic of humans with type 2 but not type 1 diabetes
    • Huang CJ, Lin CY, Haataja L et al (2007) High expression rates of human islet amyloid polypeptide induce endoplasmic reticulum stress mediated beta-cell apoptosis, a characteristic of humans with type 2 but not type 1 diabetes. Diabetes 56:2016-2027.
    • (2007) Diabetes , vol.56 , pp. 2016-2027
    • Huang, C.J.1    Lin, C.Y.2    Haataja, L.3
  • 31
    • 64649101777 scopus 로고    scopus 로고
    • Successful vs failed adaptation to high fat diet induced insulin resistance; the role of IAPP induced beta cell endoplasmic reticulum stress
    • Matveyenko AV, Gurlo T, Daval M, Butler AE, Butler PC (2009) Successful vs failed adaptation to high fat diet induced insulin resistance; the role of IAPP induced beta cell endoplasmic reticulum stress. Diabetes 58:906-916.
    • (2009) Diabetes , vol.58 , pp. 906-916
    • Matveyenko, A.V.1    Gurlo, T.2    Daval, M.3    Butler, A.E.4    Butler, P.C.5
  • 32
    • 61449123871 scopus 로고    scopus 로고
    • Oxidative stress is induced by islet amyloid formation and time-dependently mediates amyloid-induced beta cell apoptosis
    • Zraika S, Hull RL, Udayasankar J et al (2009) Oxidative stress is induced by islet amyloid formation and time-dependently mediates amyloid-induced beta cell apoptosis. Diabetologia 52:626-635.
    • (2009) Diabetologia , vol.52 , pp. 626-635
    • Zraika, S.1    Hull, R.L.2    Udayasankar, J.3
  • 33
    • 56049121909 scopus 로고    scopus 로고
    • Regulation of CD95/APO-1/Fas-induced apoptosis by protein phosphatases
    • Gloire G, Charlier E, Piette J (2008) Regulation of CD95/APO-1/Fas- induced apoptosis by protein phosphatases. Biochem Pharmacol 76:1451-1458.
    • (2008) Biochem Pharmacol , vol.76 , pp. 1451-1458
    • Gloire, G.1    Charlier, E.2    Piette, J.3
  • 34
    • 20444430478 scopus 로고    scopus 로고
    • Apoptotic pathways: Ten minutes to dead
    • Green DR (2005) Apoptotic pathways: ten minutes to dead. Cell 121:671-674.
    • (2005) Cell , vol.121 , pp. 671-674
    • Green, D.R.1
  • 35
    • 0032780022 scopus 로고    scopus 로고
    • The cellular response to protein misfolding in the endoplasmic reticulum
    • Welihinda AA, Tirasophon W, Kaufman RJ (1999) The cellular response to protein misfolding in the endoplasmic reticulum. Gene Expr 7:293-300.
    • (1999) Gene Expr , vol.7 , pp. 293-300
    • Welihinda, A.A.1    Tirasophon, W.2    Kaufman, R.J.3
  • 36
    • 0029978228 scopus 로고    scopus 로고
    • Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic beta cell expression of human islet amyloid polypeptide
    • Verchere CB, D'Alessio DA, Palmiter RD et al (1996) Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic beta cell expression of human islet amyloid polypeptide. Proc Natl Acad Sci USA 93:3492-3496.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3492-3496
    • Verchere, C.B.1    D'Alessio, D.A.2    Palmiter, R.D.3
  • 37
    • 15644364847 scopus 로고    scopus 로고
    • Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes
    • Woo M, Hakem R, Soengas MS et al (1998) Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes. Genes Dev 12:806-819.
    • (1998) Genes Dev , vol.12 , pp. 806-819
    • Woo, M.1    Hakem, R.2    Soengas, M.S.3
  • 38
    • 0029956641 scopus 로고    scopus 로고
    • Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice
    • Kuida K, Zheng TS, Na S et al (1996) Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice. Nature 384:368-372.
    • (1996) Nature , vol.384 , pp. 368-372
    • Kuida, K.1    Zheng, T.S.2    Na, S.3
  • 39
    • 17644379373 scopus 로고    scopus 로고
    • Caspase-3-dependent beta-cell apoptosis in the initiation of autoimmune diabetes mellitus
    • Liadis N, Murakami K, Eweida M et al (2005) Caspase-3-dependent beta-cell apoptosis in the initiation of autoimmune diabetes mellitus. Mol Cell Biol 25:3620-3629.
    • (2005) Mol Cell Biol , vol.25 , pp. 3620-3629
    • Liadis, N.1    Murakami, K.2    Eweida, M.3
  • 40
    • 0028303844 scopus 로고
    • Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus
    • Lorenzo A, Razzaboni B, Weir GC, Yankner BA (1994) Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus. Nature 368:756-760.
    • (1994) Nature , vol.368 , pp. 756-760
    • Lorenzo, A.1    Razzaboni, B.2    Weir, G.C.3    Yankner, B.A.4
  • 41
    • 0034823116 scopus 로고    scopus 로고
    • Ultrastructural evidence that apoptosis is the mechanism by which human amylin evokes death in RINm5F pancreatic islet beta-cells
    • Saafi EL, Konarkowska B, Zhang S, Kistler J, Cooper GJ (2001) Ultrastructural evidence that apoptosis is the mechanism by which human amylin evokes death in RINm5F pancreatic islet beta-cells. Cell Biol Int 25:339-350.
    • (2001) Cell Biol Int , vol.25 , pp. 339-350
    • Saafi, E.L.1    Konarkowska, B.2    Zhang, S.3    Kistler, J.4    Cooper, G.J.5
  • 42
    • 57249088953 scopus 로고    scopus 로고
    • Amyloid formation results in recurrence of hyperglycaemia following transplantation of human IAPP transgenic mouse islets
    • Udayasankar J, Kodama K, Hull RL et al (2009) Amyloid formation results in recurrence of hyperglycaemia following transplantation of human IAPP transgenic mouse islets. Diabetologia 52:145-153.
    • (2009) Diabetologia , vol.52 , pp. 145-153
    • Udayasankar, J.1    Kodama, K.2    Hull, R.L.3
  • 43
    • 0015930676 scopus 로고
    • Fine structure of islets of Langerhans in insular amyloidosis
    • Westermark P (1973) Fine structure of islets of Langerhans in insular amyloidosis. Virchows Arch A Pathol Anat 359:1-18.
    • (1973) Virchows Arch A Pathol Anat , vol.359 , pp. 1-18
    • Westermark, P.1
  • 44
    • 33646509867 scopus 로고    scopus 로고
    • Intracellular amyloid-like deposits contain unprocessed pro-islet amyloid polypeptide (proIAPP) in beta cells of transgenic mice overexpressing the gene for human IAPP and transplanted human islets
    • Paulsson JF, Andersson A, Westermark P, Westermark GT (2006) Intracellular amyloid-like deposits contain unprocessed pro-islet amyloid polypeptide (proIAPP) in beta cells of transgenic mice overexpressing the gene for human IAPP and transplanted human islets. Diabetologia 49:1237-1246.
    • (2006) Diabetologia , vol.49 , pp. 1237-1246
    • Paulsson, J.F.1    Andersson, A.2    Westermark, P.3    Westermark, G.T.4
  • 46
    • 33847012626 scopus 로고    scopus 로고
    • Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets
    • Ritzel RA, Meier JJ, Lin CY, Veldhuis JD, Butler PC (2007) Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets. Diabetes 56:65-71.
    • (2007) Diabetes , vol.56 , pp. 65-71
    • Ritzel, R.A.1    Meier, J.J.2    Lin, C.Y.3    Veldhuis, J.D.4    Butler, P.C.5
  • 47
    • 0028172886 scopus 로고
    • Beta-amyloid neurotoxicity requires fibril formation and is inhibited by Congo red
    • Lorenzo A, Yankner BA (1994) Beta-amyloid neurotoxicity requires fibril formation and is inhibited by congo red. Proc Natl Acad Sci USA 91:12243-12247.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12243-12247
    • Lorenzo, A.1    Yankner, B.A.2
  • 48
    • 40749084493 scopus 로고    scopus 로고
    • Fas-associated death receptor signaling evoked by human amylin in islet beta-cells
    • Zhang S, Liu H, Yu H, Cooper GJ (2007) Fas-associated death receptor signaling evoked by human amylin in islet beta-cells. Diabetes 57:348-356.
    • (2007) Diabetes , vol.57 , pp. 348-356
    • Zhang, S.1    Liu, H.2    Yu, H.3    Cooper, G.J.4
  • 49
    • 33846265786 scopus 로고    scopus 로고
    • Glucose- and timedependence of islet amyloid formation in vitro
    • Zraika S, Hull RL, Udayasankar J et al (2007) Glucose- and timedependence of islet amyloid formation in vitro. Biochem Biophys Res Commun 354:234-239.
    • (2007) Biochem Biophys Res Commun , vol.354 , pp. 234-239
    • Zraika, S.1    Hull, R.L.2    Udayasankar, J.3


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