메뉴 건너뛰기




Volumn 9, Issue MAY, 2015, Pages

Amylin at the interface between metabolic and neurodegenerative disorders

Author keywords

Alzheimer's disease (AD); Amylin; Dementia; Hyperglycemia; Insulin; Obesity; Type 2 diabetes; amyloid

Indexed keywords

AMYLIN; AMYLIN DERIVATIVE; AMYLIN RECEPTOR; AMYLOID; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; CALCITONIN[8-32][30 ASPARAGINE 32 TYROSINAMIDE]; CHOLECYSTOKININ; INSULIN; LEPTIN; PRAMLINTIDE;

EID: 84930634209     PISSN: 16624548     EISSN: 1662453X     Source Type: Journal    
DOI: 10.3389/fnins.2015.00216     Document Type: Article
Times cited : (74)

References (147)
  • 4
    • 85027945322 scopus 로고    scopus 로고
    • Amylin receptor signaling in the nucleus accumbens negatively modulates μ-opioid-driven feeding
    • Baisley S.K., Baldo, B.A. (2014). Amylin receptor signaling in the nucleus accumbens negatively modulates μ-opioid-driven feeding. Neuropsychopharmacol. 39, 3009-3017.
    • (2014) Neuropsychopharmacol , vol.39 , pp. 3009-3017
    • Baisley, S.K.1    Baldo, B.A.2
  • 5
    • 0031837461 scopus 로고    scopus 로고
    • Differential permeability of the blood-brain barrier to two pancreatic peptides: insulin and amylin
    • Banks, W.A., Kastin, A.J. (1998). Differential permeability of the blood-brain barrier to two pancreatic peptides: insulin and amylin. Peptides. 19, 883-889.
    • (1998) Peptides , vol.19 , pp. 883-889
    • Banks, W.A.1    Kastin, A.J.2
  • 7
    • 84901825835 scopus 로고    scopus 로고
    • Insulin IGF- 1 and GLP-1 signaling in neurodegenerative disorders: targets for disease modification?
    • Bassil, F., Fernagut, P.O., Bezard, E., Meissner, W.G. (2014). Insulin, IGF- 1 and GLP-1 signaling in neurodegenerative disorders: targets for disease modification? Prog. Neurobiol. 118, 1-18.
    • (2014) Prog. Neurobiol. , vol.118 , pp. 1-18
    • Bassil, F.1    Fernagut, P.O.2    Bezard, E.3    Meissner, W.G.4
  • 8
    • 0042822110 scopus 로고    scopus 로고
    • An insulin-degrading enzyme inhibitor decreases amylin degradation, increases amylin-induced cytotoxicity, and increases amyloid formation in insulinoma cell cultures
    • Bennett, R.G., Hamel, F.G., Duckworth, W.C. (2003). An insulin-degrading enzyme inhibitor decreases amylin degradation, increases amylin-induced cytotoxicity, and increases amyloid formation in insulinoma cell cultures. Diabetes. 52, 2315-2320.
    • (2003) Diabetes , vol.52 , pp. 2315-2320
    • Bennett, R.G.1    Hamel, F.G.2    Duckworth, W.C.3
  • 9
    • 0032423613 scopus 로고    scopus 로고
    • What is the role of dopamine in reward: hedonic impact, reward learning, or incentive salience?
    • Berridge, K.C., Robinson, T.E. (1998). What is the role of dopamine in reward: hedonic impact, reward learning, or incentive salience? Brain Res. Brain Res. Rev. 28, 309-369.
    • (1998) Brain Res. Brain Res. Rev , vol.28 , pp. 309-369
    • Berridge, K.C.1    Robinson, T.E.2
  • 10
    • 0024400674 scopus 로고
    • Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species
    • Betsholtz, C., Christmansson, L., Engström, U., Rorsman, F., Svensson, V., Johnson, K.H., Westermark, P. (1989). Sequence divergence in a specific region of islet amyloid polypeptide (IAPP) explains differences in islet amyloid formation between species. FEBS Lett. 251, 261-264.
    • (1989) FEBS Lett , vol.251 , pp. 261-264
    • Betsholtz, C.1    Christmansson, L.2    Engström, U.3    Rorsman, F.4    Svensson, V.5    Johnson, K.H.6    Westermark, P.7
  • 11
    • 0031720338 scopus 로고    scopus 로고
    • Synergy between amylin and cholecystokinin for inhibition of food intake in mice
    • Bhavsar, S., Watkins, J., Young, A. (1998). Synergy between amylin and cholecystokinin for inhibition of food intake in mice. Physiol. Behav. 64, 557-561.
    • (1998) Physiol. Behav. , vol.64 , pp. 557-561
    • Bhavsar, S.1    Watkins, J.2    Young, A.3
  • 12
    • 79957645885 scopus 로고    scopus 로고
    • Amylinergic control of food intake in lean and obese rodents
    • Boyle, C.N., Lutz, T.A. (2011). Amylinergic control of food intake in lean and obese rodents. Physiol. Behav. 105, 129-137.
    • (2011) Physiol. Behav. , vol.105 , pp. 129-137
    • Boyle, C.N.1    Lutz, T.A.2
  • 13
    • 79957636761 scopus 로고    scopus 로고
    • Influence of high-fat feeding, diet-induced obesity, and hyperamylinemia on the sensitivity to acute amylin
    • Boyle, C.N., Rossier, M.M., Lutz, T.A. (2011). Influence of high-fat feeding, diet-induced obesity, and hyperamylinemia on the sensitivity to acute amylin. Physiol. Behav. 104, 20-28.
    • (2011) Physiol. Behav. , vol.104 , pp. 20-28
    • Boyle, C.N.1    Rossier, M.M.2    Lutz, T.A.3
  • 14
    • 84908251156 scopus 로고    scopus 로고
    • The role of the area postrema in the anorectic effects of amylin and salmon calcitonin: behavioral and neuronal phenotyping
    • Braegger, F.E., Asarian, L., Dahl, K., Lutz, T.A., Boyle, C.N. (2014). The role of the area postrema in the anorectic effects of amylin and salmon calcitonin: behavioral and neuronal phenotyping. Eur. J. Neurosci. 40, 3055-3066.
    • (2014) Eur. J. Neurosci. , vol.40 , pp. 3055-3066
    • Braegger, F.E.1    Asarian, L.2    Dahl, K.3    Lutz, T.A.4    Boyle, C.N.5
  • 16
    • 84904113244 scopus 로고    scopus 로고
    • Elevated risk of type 2 diabetes for development of Alzheimer disease: a key role for oxidative stress in brain
    • Butterfield, D.A., Di Domenico, F., Barone, E. (2014). Elevated risk of type 2 diabetes for development of Alzheimer disease: a key role for oxidative stress in brain. Biochim. Biophys. Acta. 1842, 1693-1706.
    • (2014) Biochim. Biophys. Acta. , vol.1842 , pp. 1693-1706
    • Butterfield, D.A.1    Di Domenico, F.2    Barone, E.3
  • 17
    • 84899895001 scopus 로고    scopus 로고
    • Oxidative stress in Alzheimer's disease
    • Chen, Z., Zhong, C. (2014). Oxidative stress in Alzheimer's disease. Neurosci. Bull. 30, 271-281.
    • (2014) Neurosci. Bull. , vol.30 , pp. 271-281
    • Chen, Z.1    Zhong, C.2
  • 19
    • 1542375103 scopus 로고    scopus 로고
    • Islet amyloid: a complication of islet dysfunction or an aetiological factor in Type 2 diabetes?
    • Clark, A., Nilsson, M.R. (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
  • 20
    • 42449136183 scopus 로고    scopus 로고
    • Untangling the unfolded protein response
    • Davenport, E.L., Morgan, G.J., Davies, F.E. (2008). Untangling the unfolded protein response. Cell Cycle. 7, 865-869.
    • (2008) Cell Cycle , vol.7 , pp. 865-869
    • Davenport, E.L.1    Morgan, G.J.2    Davies, F.E.3
  • 21
    • 84055193428 scopus 로고    scopus 로고
    • Contributions of brain insulin resistance and deficiency in amyloid related neurodegeneration in Alzheimer's disease
    • de la Monte, S.M. (2012). Contributions of brain insulin resistance and deficiency in amyloid related neurodegeneration in Alzheimer's disease. Drugs. 72, 49-66.
    • (2012) Drugs , vol.72 , pp. 49-66
    • de la Monte, S.M.1
  • 22
    • 84897954482 scopus 로고    scopus 로고
    • Brain metabolic dysfunction at the core of Alzheimer's disease
    • de la Monte, S.M., Tong, M. (2014). Brain metabolic dysfunction at the core of Alzheimer's disease. Biochem. Pharmacol. 88, 548-559.
    • (2014) Biochem. Pharmacol. , vol.88 , pp. 548-559
    • de la Monte, S.M.1    Tong, M.2
  • 23
    • 68949089312 scopus 로고    scopus 로고
    • Alzheimer's disease i s type 3 diabetes-evidence reviewed
    • de la Monte, S.M., Wands, J.R. (2008). Alzheimer's disease i s type 3 diabetes-evidence reviewed. J. Diabetes Sci. Technol. 2, 1101-1113.
    • (2008) J. Diabetes Sci. Technol. , vol.2 , pp. 1101-1113
    • de la Monte, S.M.1    Wands, J.R.2
  • 25
    • 84878782369 scopus 로고    scopus 로고
    • Inflammation in obesity and diabetes: islet dysfunction and therapeutic opportunity
    • Donath, M.Y., Dalmas, É., Sauter, N.S., Böni-Schnetzler, M. (2013). Inflammation in obesity and diabetes: islet dysfunction and therapeutic opportunity. Cell Metab. 17, 860-872.
    • (2013) Cell Metab , vol.17 , pp. 860-872
    • Donath, M.Y.1    Dalmas, É.2    Sauter, N.S.3    Böni-Schnetzler, M.4
  • 26
    • 79151478555 scopus 로고    scopus 로고
    • Type 2 diabetes as an inflammatory disease
    • Donath, M.Y., Shoelson, S.E. (2011). Type 2 diabetes as an inflammatory disease. Nat. Rev. Immunol. 11, 98-107.
    • (2011) Nat. Rev. Immunol. , vol.11 , pp. 98-107
    • Donath, M.Y.1    Shoelson, S.E.2
  • 27
    • 0001458174 scopus 로고    scopus 로고
    • Amylin: localization, effects on cerebral arteries and on local cerebral blood flow in the cat
    • Edvinsson, L., Goadsby, P.J., Uddman, R. (2001). Amylin: localization, effects on cerebral arteries and on local cerebral blood flow in the cat. ScientificWorldJournal. 1, 168-80.
    • (2001) ScientificWorldJournal , vol.1 , pp. 168-180
    • Edvinsson, L.1    Goadsby, P.J.2    Uddman, R.3
  • 28
    • 0002400494 scopus 로고    scopus 로고
    • Area postrem (AP)-lesions block the regulation of gastric emptying by amylin
    • Edwards, G.L., Gedulin, B.R., C. J, Dilts RP, C.C. M, and Young A. (1998). Area postrem (AP)-lesions block the regulation of gastric emptying by amylin. Neurogastroenterol. Motil. 10, 26.
    • (1998) Neurogastroenterol. Motil. , vol.10 , pp. 26
    • Edwards, G.L.1    Gedulin, B.R.2    Dilts, R.P.3    Young, A.4
  • 30
    • 84914674716 scopus 로고    scopus 로고
    • 2003-2013: a decade of body mass index, Alzheimer's disease, and dementia
    • Emmerzaal, T.L., Kiliaan, A.J., Gustafson, D.R. (2015). 2003-2013: a decade of body mass index, Alzheimer's disease, and dementia. J. Alzheimers Dis. 43, 739-755.
    • (2015) J. Alzheimers Dis. , vol.43 , pp. 739-755
    • Emmerzaal, T.L.1    Kiliaan, A.J.2    Gustafson, D.R.3
  • 31
    • 0026512386 scopus 로고
    • Plasma islet amyloid polypeptide levels in obesity, impaired glucose tolerance and non-insulin-dependent diabetes mellitus
    • Enoki, S., Mitsukawa, T., Takemura, J., Nakazato, M., Aburaya, J., Toshimori, H., Matsukara, S. (1992). Plasma islet amyloid polypeptide levels in obesity, impaired glucose tolerance and non-insulin-dependent diabetes mellitus. Diabetes Res. Clin. Pract. 15, 97-102.
    • (1992) Diabetes Res. Clin. Pract. , vol.15 , pp. 97-102
    • Enoki, S.1    Mitsukawa, T.2    Takemura, J.3    Nakazato, M.4    Aburaya, J.5    Toshimori, H.6    Matsukara, S.7
  • 35
    • 84859325175 scopus 로고    scopus 로고
    • Defining Alzheimer as a common age-related neurodegenerative process not inevitably leading to dementia
    • Ferrer, I. (2012). Defining Alzheimer as a common age-related neurodegenerative process not inevitably leading to dementia. Prog. Neurobiol. 97, 38-51.
    • (2012) Prog. Neurobiol , vol.97 , pp. 38-51
    • Ferrer, I.1
  • 36
    • 0030639578 scopus 로고    scopus 로고
    • Leptin, leptin receptors and the control of body weight
    • Friedman, J.M. (1997). Leptin, leptin receptors and the control of body weight. Eur. J. Med. Res. 2, 7-13.
    • (1997) Eur. J. Med. Res. , vol.2 , pp. 7-13
    • Friedman, J.M.1
  • 37
    • 84872312497 scopus 로고    scopus 로고
    • Electrophysiologically identified presynaptic mechanisms underlying amylinergic modulation of area postrema neuronal excitability in rat brain slices
    • Fukuda, T., Hirai, Y., Maezawa, H., Kitagawa, Y., Funahashi, M. (2013). Electrophysiologically identified presynaptic mechanisms underlying amylinergic modulation of area postrema neuronal excitability in rat brain slices. Brain Res. 1494, 9-16.
    • (2013) Brain Res , vol.1494 , pp. 9-16
    • Fukuda, T.1    Hirai, Y.2    Maezawa, H.3    Kitagawa, Y.4    Funahashi, M.5
  • 38
    • 84874548101 scopus 로고    scopus 로고
    • Global prevalence and future of diabetes mellitus
    • Ginter, E., Simko, V. (2012a). Global prevalence and future of diabetes mellitus. Adv. Exp. Med. Biol. 771, 35-41.
    • (2012) Adv. Exp. Med. Biol. , vol.771 , pp. 35-41
    • Ginter, E.1    Simko, V.2
  • 39
    • 84874535427 scopus 로고    scopus 로고
    • Type 2 diabetes mellitus, pandemic in 21st century
    • Ginter, E., Simko, V. (2012b). Type 2 diabetes mellitus, pandemic in 21st century. Adv. Exp. Med. Biol. 771, 42-50.
    • (2012) Adv. Exp. Med. Biol. , vol.771 , pp. 42-50
    • Ginter, E.1    Simko, V.2
  • 40
    • 84883497509 scopus 로고    scopus 로고
    • Lessons from two prevalent amyloidoses-what amylin and Aβ have in common
    • Götz, J., Lim, Y.A., Eckert, A. (2013). Lessons from two prevalent amyloidoses-what amylin and Aβ have in common. Front Aging Neurosci. 5, 38.
    • (2013) Front Aging Neurosci , vol.5 , pp. 38
    • Götz, J.1    Lim, Y.A.2    Eckert, A.3
  • 41
    • 28444466516 scopus 로고    scopus 로고
    • High-fat diets, insulin resistance and declining cognitive function
    • Greenwood, C.E., Winocur, G. (2005). High-fat diets, insulin resistance and declining cognitive function. Neurobiol. Aging. 26 Suppl 1, 42-45.
    • (2005) Neurobiol. Aging. , vol.26 , pp. 42-45
    • Greenwood, C.E.1    Winocur, G.2
  • 42
    • 69549126592 scopus 로고    scopus 로고
    • Pancreatic islet amyloidosis, beta-cell apoptosis, and alpha-cell proliferation are determinants of islet remodeling in type-2 diabetic baboons
    • Guardado-Mendoza, R., Davalli, A.M., Chavez, A.O., Hubbard, G.B., Dick, E.J., Majluf-Cruz, A., et al., (2009). Pancreatic islet amyloidosis, beta-cell apoptosis, and alpha-cell proliferation are determinants of islet remodeling in type-2 diabetic baboons. Proc. Natl. Acad. Sci. U S A. 106, 13992-13997.
    • (2009) Proc. Natl. Acad. Sci. U S A. , vol.106 , pp. 13992-13997
    • Guardado-Mendoza, R.1    Davalli, A.M.2    Chavez, A.O.3    Hubbard, G.B.4    Dick, E.J.5    Majluf-Cruz, A.6
  • 43
    • 76149102617 scopus 로고    scopus 로고
    • Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway
    • Gurlo, T., Ryazantsev, S., Huang, C.J., Yeh, M.W., Reber, H.A., Hines, O.J., O'Brien, T.D., Glabe, C.G., Butler, P.C. (2010). Evidence for proteotoxicity in beta cells in type 2 diabetes: toxic islet amyloid polypeptide oligomers form intracellularly in the secretory pathway. Am. J. Pathol. 176, 861-869.
    • (2010) Am. J. Pathol. , vol.176 , pp. 861-869
    • Gurlo, T.1    Ryazantsev, S.2    Huang, C.J.3    Yeh, M.W.4    Reber, H.A.5    Hines, O.J.6    O'Brien, T.D.7    Glabe, C.G.8    Butler, P.C.9
  • 45
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics
    • Hardy, J., Selkoe, D.J. (2002). The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science. 297, 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 46
    • 33644834054 scopus 로고    scopus 로고
    • Role of islet amyloid in type 2 diabetes mellitus
    • Höppener, J.W., Lips, C.J. (2006). Role of islet amyloid in type 2 diabetes mellitus. Int. J. Biochem. Cell Biol. 38, 726-736.
    • (2006) Int. J. Biochem. Cell Biol. , vol.38 , pp. 726-736
    • Höppener, J.W.1    Lips, C.J.2
  • 48
    • 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., Foriers, A., Schuit, F., Pipeleers, D., Van Schravendijk, C. (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    Foriers, A.4    Schuit, F.5    Pipeleers, D.6    Van Schravendijk, C.7
  • 49
    • 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, C.J., Lin, C.Y., Haataja, L., Gurlo, T., Butler, A.E., Rizza, R.A., Butler, P.C. (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    Gurlo, T.4    Butler, A.E.5    Rizza, R.A.6    Butler, P.C.7
  • 52
    • 84890121878 scopus 로고    scopus 로고
    • Amylin deposition in the brain: A second amyloid in Alzheimer disease?
    • Jackson, K., Barisone, G.A., Diaz, E., Jin, L.W., DeCarli, C., Despa, F. (2013). Amylin deposition in the brain: A second amyloid in Alzheimer disease? Ann. Neurol. 74, 517-526.
    • (2013) Ann Neurol , vol.74 , pp. 517-526
    • Jackson, K.1    Barisone, G.A.2    Diaz, E.3    Jin, L.W.4    DeCarli, C.5    Despa, F.6
  • 53
    • 0035969513 scopus 로고    scopus 로고
    • Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology
    • Jaikaran, E.T., Clark, A. (2001). Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology. Biochim. Biophys. Acta. 1537, 179-203.
    • (2001) Biochim. Biophys. Acta. , vol.1537 , pp. 179-203
    • Jaikaran, E.T.1    Clark, A.2
  • 54
    • 0035804936 scopus 로고    scopus 로고
    • Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis
    • Jaikaran, E.T., Higham, C.E., Serpell, L.C., Zurdo, J., Gross, M., Clark, A., Fraser, P.E. (2001) Identification of a novel human islet amyloid polypeptide beta-sheet domain and factors influencing fibrillogenesis. J. Mol. Biol. 308, 515-525.
    • (2001) J. Mol. Biol. , vol.308 , pp. 515-525
    • Jaikaran, E.T.1    Higham, C.E.2    Serpell, L.C.3    Zurdo, J.4    Gross, M.5    Clark, A.6    Fraser, P.E.7
  • 56
    • 0024464611 scopus 로고
    • Impaired glucose tolerance is associated with increased islet amyloid polypeptide (IAPP) immunoreactivity in pancreatic beta cells
    • Johnson, K.H., O'Brien, T.D., Jordan, K., Westermark, P. (1989). Impaired glucose tolerance is associated with increased islet amyloid polypeptide (IAPP) immunoreactivity in pancreatic beta cells. Am. J. Pathol. 135, 245-250.
    • (1989) Am. J. Pathol. , vol.135 , pp. 245-250
    • Johnson, K.H.1    O'Brien, T.D.2    Jordan, K.3    Westermark, P.4
  • 58
    • 84896495719 scopus 로고    scopus 로고
    • Pathophysiology and treatment of type 2 diabetes: perspectives on the past, present, and future
    • Kahn, S.E., Cooper, M.E., Del Prato, S. (2014). Pathophysiology and treatment of type 2 diabetes: perspectives on the past, present, and future. Lancet. 383, 1068-1083.
    • (2014) Lancet , vol.383 , pp. 1068-1083
    • Kahn, S.E.1    Cooper, M.E.2    Del Prato, S.3
  • 60
    • 80052266213 scopus 로고    scopus 로고
    • The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics
    • Karran, E., Mercken, M., De Strooper, B. (2011). The amyloid cascade hypothesis for Alzheimer's disease: an appraisal for the development of therapeutics. Nat. Rev. Drug Discov. 10, 698-712.
    • (2011) Nat. Rev. Drug Discov. , vol.10 , pp. 698-712
    • Karran, E.1    Mercken, M.2    De Strooper, B.3
  • 61
    • 80054800194 scopus 로고    scopus 로고
    • Common cellular and molecular mechanisms in obesity and drug addiction
    • Kenny, P.J. (2011). Common cellular and molecular mechanisms in obesity and drug addiction. Nat. Rev. Neurosci. 12, 638-651.
    • (2011) Nat. Rev. Neurosci. , vol.12 , pp. 638-651
    • Kenny, P.J.1
  • 65
    • 36448936053 scopus 로고    scopus 로고
    • Common pathological processes in Alzheimer disease and type 2 diabetes: a review
    • Li, L., Hölscher, C. (2007). Common pathological processes in Alzheimer disease and type 2 diabetes: a review. Brain Res. Rev. 56, 384-402.
    • (2007) Brain Res. Rev , vol.56 , pp. 384-402
    • Li, L.1    Hölscher, C.2
  • 66
    • 84882248875 scopus 로고    scopus 로고
    • Acidic pH retards the fibrillization of human Islet Amyloid Polypeptide due to electrostatic repulsion of histidines
    • Li, Y., Xu, W., Mu, Y., Zhang, J.Z. (2013). Acidic pH retards the fibrillization of human Islet Amyloid Polypeptide due to electrostatic repulsion of histidines. J. Chem. Phys. 139, 055102.
    • (2013) J. Chem. Phys. , vol.139 , pp. 055102
    • Li, Y.1    Xu, W.2    Mu, Y.3    Zhang, J.Z.4
  • 67
    • 15444362716 scopus 로고    scopus 로고
    • Pancreatic amylin as a centrally acting satiating hormone
    • Lutz, T.A. (2005). Pancreatic amylin as a centrally acting satiating hormone. Curr. Drug Targets. 6, 181-189.
    • (2005) Curr. Drug Targets. , vol.6 , pp. 181-189
    • Lutz, T.A.1
  • 68
    • 64949171578 scopus 로고    scopus 로고
    • Control of food intake and energy expenditure by amylin-therapeutic implications
    • Lutz, T.A. (2009). Control of food intake and energy expenditure by amylin-therapeutic implications. Int. J. Obes. 33 Suppl 1, S24-27.
    • (2009) Int. J. Obes. , vol.33 , pp. S24-27
    • Lutz, T.A.1
  • 69
    • 77952703708 scopus 로고    scopus 로고
    • The role of amylin in the control of energy homeostasis
    • Lutz, T.A. (2010). The role of amylin in the control of energy homeostasis. Am. J. Physiol. Regul. Integr. Comp. Physiol. 298, R1475-1484.
    • (2010) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.298 , pp. R1475-1484
    • Lutz, T.A.1
  • 70
    • 0031745409 scopus 로고    scopus 로고
    • Anorectic effect of amylin is not transmitted by capsaicin-sensitive nerve fibers
    • Lutz, T.A., Althaus, J., Rossi, R., Scharrer, E. (1998a). Anorectic effect of amylin is not transmitted by capsaicin-sensitive nerve fibers. Am. J. Physiol. 274, R1777-1782.
    • (1998) Am. J. Physiol. , vol.274 , pp. R1777-1782
    • Lutz, T.A.1    Althaus, J.2    Rossi, R.3    Scharrer, E.4
  • 71
    • 0029070575 scopus 로고
    • Subdiaphragmatic vagotomy does not influence the anorectic effect of amylin
    • Lutz, T.A., Del Prete, E., Scharrer, E. (1995). Subdiaphragmatic vagotomy does not influence the anorectic effect of amylin. Peptides 16, 457-462.
    • (1995) Peptides , vol.16 , pp. 457-462
    • Lutz, T.A.1    Del Prete, E.2    Scharrer, E.3
  • 73
    • 0034972374 scopus 로고    scopus 로고
    • The anorectic effect of a chronic peripheral infusion of amylin is abolished in area postrema/nucleus of the solitary tract (AP/NTS) lesioned rats
    • Lutz, T.A., Mollet, A., Rushing, P.A., Riediger, T., Scharrer, E. (2001). The anorectic effect of a chronic peripheral infusion of amylin is abolished in area postrema/nucleus of the solitary tract (AP/NTS) lesioned rats. Int. J. Obes. Relat. Metab. Disord. 25, 1005-1011.
    • (2001) Int. J. Obes. Relat. Metab. Disord. , vol.25 , pp. 1005-1011
    • Lutz, T.A.1    Mollet, A.2    Rushing, P.A.3    Riediger, T.4    Scharrer, E.5
  • 74
    • 0027760830 scopus 로고
    • A review of new developments in type 2 diabetes in human beings and cats
    • Lutz, T.A., Rand, J.S. (1993). A review of new developments in type 2 diabetes in human beings and cats. Br. Vet. J. 149, 527-536.
    • (1993) Br. Vet. J. , vol.149 , pp. 527-536
    • Lutz, T.A.1    Rand, J.S.2
  • 75
    • 0032005144 scopus 로고    scopus 로고
    • Lesion of the area postrema/nucleus of the solitary tract (AP/NTS) attenuates the anorectic effects of amylin and calcitonin gene-related peptide (CGRP) in rats
    • Lutz, T.A., Senn, M., Althaus, J., Del Prete, E., Ehrensperger, F., Scharrer, E. (1998b). Lesion of the area postrema/nucleus of the solitary tract (AP/NTS) attenuates the anorectic effects of amylin and calcitonin gene-related peptide (CGRP) in rats. Peptides 19, 309-317.
    • (1998) Peptides , vol.19 , pp. 309-317
    • Lutz, T.A.1    Senn, M.2    Althaus, J.3    Del Prete, E.4    Ehrensperger, F.5    Scharrer, E.6
  • 77
    • 76749086899 scopus 로고    scopus 로고
    • Davalintide (AC2307), a novel amylin-mimetic peptide: enhanced pharmacological properties over native amylin to reduce food intake and body weight
    • Mack, C.M., Soares, C.J., Wilson, J.K., Athanacio, J.R., Turek, V.F., Trevaskis, J.L., et al., (2010). Davalintide (AC2307), a novel amylin-mimetic peptide: enhanced pharmacological properties over native amylin to reduce food intake and body weight. Int. J. Obes. 34, 385-395.
    • (2010) Int. J. Obes. , vol.34 , pp. 385-395
    • Mack, C.M.1    Soares, C.J.2    Wilson, J.K.3    Athanacio, J.R.4    Turek, V.F.5    Trevaskis, J.L.6
  • 78
    • 33749492425 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress signaling in disease
    • Marciniak, S.J., Ron, D. (2006). Endoplasmic reticulum stress signaling in disease. Physiol. Rev. 86, 1133-1149.
    • (2006) Physiol. Rev. , vol.86 , pp. 1133-1149
    • Marciniak, S.J.1    Ron, D.2
  • 79
    • 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, C.B. (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
  • 81
    • 33745586536 scopus 로고    scopus 로고
    • Islet amyloid polypeptide (IAPP) transgenic rodents as models for type 2 diabetes
    • Matveyenko AV, Butler PC. (2006). Islet amyloid polypeptide (IAPP) transgenic rodents as models for type 2 diabetes. ILAR J. 47, 225-233.
    • (2006) ILAR J , vol.47 , pp. 225-233
    • Matveyenko, A.V.1    Butler, P.C.2
  • 82
    • 0036729424 scopus 로고    scopus 로고
    • Multiple combinations of co-factors produce variants of age-related cognitive decline: a theory
    • McDonald, RJ. (2002). Multiple combinations of co-factors produce variants of age-related cognitive decline: a theory. Can. J. Exp. Psychol. 56, 221-239.
    • (2002) Can. J. Exp. Psychol. , vol.56 , pp. 221-239
    • McDonald, R.J.1
  • 83
    • 84916934842 scopus 로고    scopus 로고
    • Amylin activates distributed CNS nuclei to control energy balance
    • Mietlicki-Baase, E.G., Hayes, M.R. (2014). Amylin activates distributed CNS nuclei to control energy balance. Physiol. Behav. 136, 39-46.
    • (2014) Physiol. Behav. , vol.136 , pp. 39-46
    • Mietlicki-Baase, E.G.1    Hayes, M.R.2
  • 85
    • 84880327506 scopus 로고    scopus 로고
    • Amylin receptor signaling in the ventral tegmental area is physiologically relevant for the control of food intake
    • Mietlicki-Baase, E.G., Rupprecht, L.E., Olivos, D.R., Zimmer, D.J., Alter, M.D., Pierce, R.C., et al. (2013). Amylin receptor signaling in the ventral tegmental area is physiologically relevant for the control of food intake. Neuropsychopharmacology 38, 1685-1697.
    • (2013) Neuropsychopharmacology , vol.38 , pp. 1685-1697
    • Mietlicki-Baase, E.G.1    Rupprecht, L.E.2    Olivos, D.R.3    Zimmer, D.J.4    Alter, M.D.5    Pierce, R.C.6
  • 86
    • 1842523038 scopus 로고    scopus 로고
    • Infusion of the amylin antagonist AC 187 into the area postrema increases food intake in rats
    • Mollet, A., Gilg, S., Riediger, T., Lutz, T.A. (2004). Infusion of the amylin antagonist AC 187 into the area postrema increases food intake in rats. Physiol. Behav. 81, 149-155.
    • (2004) Physiol. Behav. , vol.81 , pp. 149-155
    • Mollet, A.1    Gilg, S.2    Riediger, T.3    Lutz, T.A.4
  • 87
    • 0037261581 scopus 로고    scopus 로고
    • Endogenous amylin contributes to the anorectic effects of cholecystokinin and bombesin
    • Mollet, A., Meier, S., Grabler, V., Gilg, S., Scharrer, E., Lutz, T.A. (2003). Endogenous amylin contributes to the anorectic effects of cholecystokinin and bombesin. Peptides 24, 91-98.
    • (2003) Peptides , vol.24 , pp. 91-98
    • Mollet, A.1    Meier, S.2    Grabler, V.3    Gilg, S.4    Scharrer, E.5    Lutz, T.A.6
  • 88
    • 84899141023 scopus 로고    scopus 로고
    • Neuroinflammation in the pathogenesis of Alzheimer's disease A rational framework for the search of novel therapeutic approaches
    • Morales, I., Guzmán-Martínez, L., Cerda-Troncoso, C., Farías, G.A., Maccioni, R.B. (2014). Neuroinflammation in the pathogenesis of Alzheimer's disease. A rational framework for the search of novel therapeutic approaches. Front. Cell. Neurosci. 8, 112.
    • (2014) Front. Cell. Neurosci. , vol.8 , pp. 112
    • Morales, I.1    Guzmán-Martínez, L.2    Cerda-Troncoso, C.3    Farías, G.A.4    Maccioni, R.B.5
  • 89
    • 0032972592 scopus 로고    scopus 로고
    • Effects of sequential proline substitutions on amyloid formation by human amylin20-29
    • Moriarty DF, Raleigh DP. (1999). Effects of sequential proline substitutions on amyloid formation by human amylin20-29. Biochemistry. 38, 1811-1818.
    • (1999) Biochemistry , vol.38 , pp. 1811-1818
    • Moriarty, D.F.1    Raleigh, D.P.2
  • 90
    • 84903729422 scopus 로고    scopus 로고
    • Dietary fat composition and dementia risk
    • Morris, M.C., Tangney, C.C. (2014). Dietary fat composition and dementia risk. Neurobiol. Aging. 35 Suppl 2, S59-64.
    • (2014) Neurobiol. Aging , vol.35 , pp. S59-64
    • Morris, M.C.1    Tangney, C.C.2
  • 91
    • 84913586856 scopus 로고    scopus 로고
    • The browning of white adipose tissue: some burning issues
    • Nedergaard, J., Cannon, B. (2014). The browning of white adipose tissue: some burning issues. Cell Metab. 20, 396-407.
    • (2014) Cell Metab , vol.20 , pp. 396-407
    • Nedergaard, J.1    Cannon, B.2
  • 92
    • 43049107500 scopus 로고    scopus 로고
    • Central and peripheral administration of amylin induces energy expenditure in anesthetized rats
    • Osaka, T., Tsukamoto, A., Koyama, Y., Inoue, S. (2008). Central and peripheral administration of amylin induces energy expenditure in anesthetized rats. Peptides 29, 1028-1035.
    • (2008) Peptides , vol.29 , pp. 1028-1035
    • Osaka, T.1    Tsukamoto, A.2    Koyama, Y.3    Inoue, S.4
  • 93
    • 84925271235 scopus 로고    scopus 로고
    • In vivo seeding and cross-seeding of localized amyloidosis: a molecular link between type 2 diabetes and Alzheimer disease
    • Oskarsson, M.E., Paulsson, J.F., Schultz, S.W., Ingelsson, M., Westermark, P., Westermark, G.T. (2015). In vivo seeding and cross-seeding of localized amyloidosis: a molecular link between type 2 diabetes and Alzheimer disease. Am. J. Pathol. 185, 834-846.
    • (2015) Am. J. Pathol. , vol.185 , pp. 834-846
    • Oskarsson, M.E.1    Paulsson, J.F.2    Schultz, S.W.3    Ingelsson, M.4    Westermark, P.5    Westermark, G.T.6
  • 96
    • 0036022403 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells
    • Oyadomari, S., Araki, E., Mori, M. (2002). Endoplasmic reticulum stress-mediated apoptosis in pancreatic beta-cells. Apoptosis. 7, 335-345.
    • (2002) Apoptosis , vol.7 , pp. 335-345
    • Oyadomari, S.1    Araki, E.2    Mori, M.3
  • 97
    • 0034745636 scopus 로고    scopus 로고
    • Neurotoxic Abeta peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro
    • Parks, J.K., Smith, T.S., Trimmer, P.A., Bennett, J.P. Jr, Parker, W.D. Jr. (2001). Neurotoxic Abeta peptides increase oxidative stress in vivo through NMDA-receptor and nitric-oxide-synthase mechanisms, and inhibit complex IV activity and induce a mitochondrial permeability transition in vitro. J. Neurochem. 76, 1050-1056.
    • (2001) J. Neurochem , vol.76 , pp. 1050-1056
    • Parks, J.K.1    Smith, T.S.2    Trimmer, P.A.3    Bennett, J.P.4    Parker, W.D.5
  • 98
    • 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, J.F., Andersson, A., Westermark, P., Westermark, G.T. (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
  • 99
    • 21344470854 scopus 로고    scopus 로고
    • Aberrant processing of human proislet amyloid polypeptide results in increased amyloid formation
    • Paulsson, J.F., Westermark, G.T. (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
  • 100
    • 0028079090 scopus 로고
    • Direct plasma radioimmunoassay for rat amylin-(1-37): concentrations with acquired and genetic obesity
    • Pieber, T.R., Roitelman, J., Lee, Y., Luskey, K.L., Stein, D.T. (1994). Direct plasma radioimmunoassay for rat amylin-(1-37): concentrations with acquired and genetic obesity. Am. J. Physiol. 267, E156-164.
    • (1994) Am. J. Physiol. , vol.267 , pp. E156-164
    • Pieber, T.R.1    Roitelman, J.2    Lee, Y.3    Luskey, K.L.4    Stein, D.T.5
  • 102
    • 70349871409 scopus 로고    scopus 로고
    • Reduced endoplasmic reticulum (ER)-to-Golgi protein trafficking contributes to ER stress in lipotoxic mouse beta cells by promoting protein overload
    • Preston, A.M., Gurisik, E., Bartley, C., Laybutt, D.R., Biden, T.J. (2009). Reduced endoplasmic reticulum (ER)-to-Golgi protein trafficking contributes to ER stress in lipotoxic mouse beta cells by promoting protein overload. Diabetologia. 52, 2369-2373.
    • (2009) Diabetologia , vol.52 , pp. 2369-2373
    • Preston, A.M.1    Gurisik, E.2    Bartley, C.3    Laybutt, D.R.4    Biden, T.J.5
  • 103
  • 104
    • 84904615046 scopus 로고    scopus 로고
    • Amylin and its analogs: a friend or foe for the treatment of Alzheimer's disease?
    • Qiu, W.Q., Zhu, H. (2014). Amylin and its analogs: a friend or foe for the treatment of Alzheimer's disease? Front. Aging Neurosci. 6, 186.
    • (2014) Front Aging Neurosci , vol.6 , pp. 186
    • Qiu, W.Q.1    Zhu, H.2
  • 105
    • 0036081512 scopus 로고    scopus 로고
    • Effects of amylin- related peptides on food intake, meal patterns, and gastric emptying in rats
    • Reidelberger RD, Kelsey L, and Heimann D. Effects of amylin- related peptides on food intake, meal patterns, and gastric emptying in rats. Am J Physiol Regul Integr Comp Physiol 282: R1395-1404, 2002.
    • (2002) Am J Physiol Regul Integr Comp Physiol , vol.282 , pp. R1395-1404
    • Reidelberger, R.D.1    Kelsey, L.2    Heimann, D.3
  • 107
  • 108
    • 84897954407 scopus 로고    scopus 로고
    • Alzheimer disease: epidemiology, diagnostic criteria, risk factors and biomarkers
    • Reitz, C., Mayeux, R. (2014). Alzheimer disease: epidemiology, diagnostic criteria, risk factors and biomarkers. Biochem. Pharmacol. 88, 640-651.
    • (2014) Biochem. Pharmacol. , vol.88 , pp. 640-651
    • Reitz, C.1    Mayeux, R.2
  • 109
    • 0347988181 scopus 로고    scopus 로고
    • The anorectic hormone amylin contributes to feeding-related changes of neuronal activity in key structures of the gut-brain axis
    • Riediger, T., Zuend, D., Becskei, C., Lutz, T.A. (2004). The anorectic hormone amylin contributes to feeding-related changes of neuronal activity in key structures of the gut-brain axis. Am. J. Physiol. Regul. Integr. Comp. Physiol. 286, R114-122.
    • (2004) Am. J. Physiol. Regul. Integr. Comp. Physiol. , vol.286 , pp. R114-122
    • Riediger, T.1    Zuend, D.2    Becskei, C.3    Lutz, T.A.4
  • 110
    • 84908397502 scopus 로고    scopus 로고
    • Is Alzheimer's disease related to metabolic syndrome? A Wnt signaling conundrum
    • Ríos, J.A., Cisternas, P., Arrese, M., Barja, S., Inestrosa, N.C. (2014). Is Alzheimer's disease related to metabolic syndrome? A Wnt signaling conundrum. Prog. Neurobiol. 121, 125-146.
    • (2014) Prog. Neurobiol , vol.121 , pp. 125-146
    • Ríos, J.A.1    Cisternas, P.2    Arrese, M.3    Barja, S.4    Inestrosa, N.C.5
  • 111
    • 33751509016 scopus 로고    scopus 로고
    • Antiobesity effects of the beta-cell hormone amylin in diet-induced obese rats: effects on food intake, body weight, composition, energy expenditure, and gene expression
    • Roth, J.D., Hughes, H., Kendall, E., Baron, A.D., Anderson, C.M. (2006). Antiobesity effects of the beta-cell hormone amylin in diet-induced obese rats: effects on food intake, body weight, composition, energy expenditure, and gene expression. Endocrinology 147, 5855-5864.
    • (2006) Endocrinology , vol.147 , pp. 5855-5864
    • Roth, J.D.1    Hughes, H.2    Kendall, E.3    Baron, A.D.4    Anderson, C.M.5
  • 112
    • 0030765810 scopus 로고    scopus 로고
    • Comparison of Fos induced in rat brain by GLP-1 and amylin
    • Rowland, N.E., Crews, E.C., Gentry, R.M. (1997). Comparison of Fos induced in rat brain by GLP-1 and amylin. Regul. Pept. 71, 171-174.
    • (1997) Regul. Pept. , vol.71 , pp. 171-174
    • Rowland, N.E.1    Crews, E.C.2    Gentry, R.M.3
  • 114
    • 0036072355 scopus 로고    scopus 로고
    • Acute 3rd-ventricular amylin infusion potently reduces food intake but does not produce aversive consequences
    • Rushing, P.A., Seeley, R.J., Air, E.L., Lutz, T.A., Woods, S.C. (2002). Acute 3rd-ventricular amylin infusion potently reduces food intake but does not produce aversive consequences. Peptides 23, 985-988.
    • (2002) Peptides , vol.23 , pp. 985-988
    • Rushing, P.A.1    Seeley, R.J.2    Air, E.L.3    Lutz, T.A.4    Woods, S.C.5
  • 115
    • 34848920863 scopus 로고    scopus 로고
    • ROS, mitochondria and the regulation of autophagy
    • Scherz-Shouval, R., Elazar, Z. (2007). ROS, mitochondria and the regulation of autophagy. Trends Cell Biol. 17, 422-427.
    • (2007) Trends Cell Biol , vol.17 , pp. 422-427
    • Scherz-Shouval, R.1    Elazar, Z.2
  • 118
    • 84905437740 scopus 로고    scopus 로고
    • Insulin as a bridge between type 2 diabetes and Alzheimer disease - How anti-diabetics could be a solution for dementia
    • Sebastião, I., Candeias, E., Santos, M.S., de Oliveira, C.R., Moreira, P.I., Duarte, A.I. (2014). Insulin as a bridge between type 2 diabetes and Alzheimer disease - How anti-diabetics could be a solution for dementia. Front. Endocrinol. 5, 110.
    • (2014) Front. Endocrinol. , vol.5 , pp. 110
    • Sebastião, I.1    Candeias, E.2    Santos, M.S.3    de Oliveira, C.R.4    Moreira, P.I.5    Duarte, A.I.6
  • 119
    • 80053912909 scopus 로고    scopus 로고
    • Alzheimer's disease: β-amyloid plaque formation in human brain
    • Seeman, P., Seeman, N. (2011). Alzheimer's disease: β-amyloid plaque formation in human brain. Synapse. 65, 1289-1297.
    • (2011) Synapse , vol.65 , pp. 1289-1297
    • Seeman, P.1    Seeman, N.2
  • 120
    • 0027994014 scopus 로고
    • In vitro autoradiographic localization of amylin binding sites in rat brain
    • Sexton, P.M., Paxinos, G., Kenney, M.A., Wookey, P.J., Beaumont, K. (1994). In vitro autoradiographic localization of amylin binding sites in rat brain. Neuroscience 62, 553-567.
    • (1994) Neuroscience , vol.62 , pp. 553-567
    • Sexton, P.M.1    Paxinos, G.2    Kenney, M.A.3    Wookey, P.J.4    Beaumont, K.5
  • 122
    • 84878253079 scopus 로고    scopus 로고
    • The type 2 diabetes-associated gene ide is required for insulin secretion and suppression of α-synuclein levels in β-cells
    • Steneberg, P., Bernardo, L., Edfalk, S., Lundberg, L., Backlund, F., Ostenson, C.G., Edlund, H. (2013). The type 2 diabetes-associated gene ide is required for insulin secretion and suppression of α-synuclein levels in β-cells. Diabetes. 62, 2004-2014.
    • (2013) Diabetes , vol.62 , pp. 2004-2014
    • Steneberg, P.1    Bernardo, L.2    Edfalk, S.3    Lundberg, L.4    Backlund, F.5    Ostenson, C.G.6    Edlund, H.7
  • 123
    • 84904721826 scopus 로고    scopus 로고
    • Autophagy in adipose tissue and the beta cell: implications for obesity and diabetes
    • Stienstra R., Haim, Y., Riahi, Y., Netea, M., Rudich, A., Leibowitz, G. (2014). Autophagy in adipose tissue and the beta cell: implications for obesity and diabetes. Diabetologia. 57, 1505-1516.
    • (2014) Diabetologia , vol.57 , pp. 1505-1516
    • Stienstra, R.1    Haim, Y.2    Riahi, Y.3    Netea, M.4    Rudich, A.5    Leibowitz, G.6
  • 125
    • 84923250107 scopus 로고    scopus 로고
    • Cellular functions of the amyloid precursor protein from development to dementia
    • van der Kant, R., Goldstein, L.S. (2015). Cellular functions of the amyloid precursor protein from development to dementia. Dev. Cell. 32, 502-515.
    • (2015) Dev. Cell. , vol.32 , pp. 502-515
    • van der Kant, R.1    Goldstein, L.S.2
  • 130
    • 84890890049 scopus 로고    scopus 로고
    • Altered autonomic inputs as a cause of pancreatic β-cell amyloid
    • Watve, M., Bodas, A., Diwekar, M. (2014). Altered autonomic inputs as a cause of pancreatic β-cell amyloid. Med. Hypotheses. 82, 49-53.
    • (2014) Med. Hypotheses. , vol.82 , pp. 49-53
    • Watve, M.1    Bodas, A.2    Diwekar, M.3
  • 131
    • 0029330879 scopus 로고
    • Amyloid formation in response to beta cell stress occurs in vitro, but not in vivo, in islets of transgenic mice expressing human islet amyloid polypeptide
    • Westermark, G., Arora, M.B., Fox, N., Carroll, R., Chan, S.J., Westermark, P., Steiner, D.F. (1995a). Amyloid formation in response to beta cell stress occurs in vitro, but not in vivo, in islets of transgenic mice expressing human islet amyloid polypeptide. Mol. Med. 1, 542-553.
    • (1995) Mol. Med. , vol.1 , pp. 542-553
    • Westermark, G.1    Arora, M.B.2    Fox, N.3    Carroll, R.4    Chan, S.J.5    Westermark, P.6    Steiner, D.F.7
  • 133
    • 79954535899 scopus 로고    scopus 로고
    • Islet amyloid polypeptide, islet amyloid, and diabetes mellitus
    • Westermark, P., Andersson, A., Westermark, G.T. (2011). Islet amyloid polypeptide, islet amyloid, and diabetes mellitus. Physiol. Rev. 91, 795-826.
    • (2011) Physiol. Rev. , vol.91 , pp. 795-826
    • Westermark, P.1    Andersson, A.2    Westermark, G.T.3
  • 135
    • 0030025653 scopus 로고    scopus 로고
    • Effects of beta cell granule components on human islet amyloid polypeptide fibril formation
    • Westermark, P., Li, Z.C., Westermark, G.T., Leckström, A., Steiner, D.F. (1996). Effects of beta cell granule components on human islet amyloid polypeptide fibril formation. FEBS Lett. 379, 203-206.
    • (1996) FEBS Lett , vol.379 , pp. 203-206
    • Westermark, P.1    Li, Z.C.2    Westermark, G.T.3    Leckström, A.4    Steiner, D.F.5
  • 136
    • 0028800972 scopus 로고
    • Amylin-induced relaxation of the perfused mesenteric arterial bed: meditation by calcitonin gene-related peptide receptors
    • Westfall, T.C., Curfman-Falvey, M. (1995). Amylin-induced relaxation of the perfused mesenteric arterial bed: meditation by calcitonin gene-related peptide receptors. J. Cardiovasc. Pharmacol. 26, 932-936.
    • (1995) J. Cardiovasc. Pharmacol. , vol.26 , pp. 932-936
    • Westfall, T.C.1    Curfman-Falvey, M.2
  • 137
    • 80052650475 scopus 로고    scopus 로고
    • IL-1 blockade attenuates islet amyloid polypeptide-induced proinflammatory cytokine release and pancreatic islet graft dysfunction
    • Westwell-Roper, C., Dai, D.L., Soukhatcheva, G., Potter, K.J., van Rooijen, N., Ehses, J.A., Verchere, C.B. (2011). IL-1 blockade attenuates islet amyloid polypeptide-induced proinflammatory cytokine release and pancreatic islet graft dysfunction. J. Immunol. 187, 2755-2765.
    • (2011) J. Immunol. , vol.187 , pp. 2755-2765
    • Westwell-Roper, C.1    Dai, D.L.2    Soukhatcheva, G.3    Potter, K.J.4    van Rooijen, N.5    Ehses, J.A.6    Verchere, C.B.7
  • 138
    • 44549084370 scopus 로고    scopus 로고
    • Gastric emptying in response to IAPP and CCK in rats with subdiaphragmatic afferent vagotomy
    • Wickbom, J., Herrington, M.K., Permert, J., Jansson, A., Arnelo, U. (2008). Gastric emptying in response to IAPP and CCK in rats with subdiaphragmatic afferent vagotomy. Regul. Pept. 148, 21-25.
    • (2008) Regul. Pept. , vol.148 , pp. 21-25
    • Wickbom, J.1    Herrington, M.K.2    Permert, J.3    Jansson, A.4    Arnelo, U.5
  • 139
    • 34248647047 scopus 로고    scopus 로고
    • The acute effect of amylin and salmon calcitonin on energy expenditure
    • Wielinga, P.Y., Alder, B., Lutz, T.A. (2007). The acute effect of amylin and salmon calcitonin on energy expenditure. Physiol. Behav. 91, 212-217.
    • (2007) Physiol. Behav. , vol.91 , pp. 212-217
    • Wielinga, P.Y.1    Alder, B.2    Lutz, T.A.3
  • 140
    • 77953914540 scopus 로고    scopus 로고
    • Central amylin acts as an adiposity signal to control body weight and energy expenditure
    • 2010
    • Wielinga, P.Y., Lowenstein, C., Muff, S., Munz, M., Woods, S.C., Lutz, T.A. (2010). Central amylin acts as an adiposity signal to control body weight and energy expenditure. Physiol. Behav. 101, 45-52, 2010.
    • (2010) Physiol. Behav. , vol.101 , pp. 45-52
    • Wielinga, P.Y.1    Lowenstein, C.2    Muff, S.3    Munz, M.4    Woods, S.C.5    Lutz, T.A.6
  • 141
    • 28444459843 scopus 로고    scopus 로고
    • Studies of the effects of high fat diets on cognitive function in a rat model
    • Winocur, G., Greenwood, C.E. (2005). Studies of the effects of high fat diets on cognitive function in a rat model. Neurobiol. Aging. 26 Suppl 1, 46-49.
    • (2005) Neurobiol. Aging , vol.26 , pp. 46-49
    • Winocur, G.1    Greenwood, C.E.2
  • 142
    • 34147119059 scopus 로고    scopus 로고
    • Metabolic syndrome and cognitive decline
    • Yaffe, K. (2007). Metabolic syndrome and cognitive decline. Curr. Alzheimer Res. 4, 123-126.
    • (2007) Curr. Alzheimer Res. , vol.4 , pp. 123-126
    • Yaffe, K.1
  • 143
    • 0028936025 scopus 로고
    • Formation of islet amyloid fibrils in beta-secretory granules of transgenic mice expressing human islet amyloid polypeptide/amylin
    • Yagui, K., Yamaguchi, T., Kanatsuka, A., Shimada, F., Huang, C.I., Tokuyama, Y., et al. (1995). Formation of islet amyloid fibrils in beta-secretory granules of transgenic mice expressing human islet amyloid polypeptide/amylin. Eur. J.Endocrinol. 132, 487-496.
    • (1995) Eur. J.Endocrinol. , vol.132 , pp. 487-496
    • Yagui, K.1    Yamaguchi, T.2    Kanatsuka, A.3    Shimada, F.4    Huang, C.I.5    Tokuyama, Y.6
  • 144
    • 0031779868 scopus 로고    scopus 로고
    • Roles of amylin in diabetes and in regulation of nutrient load
    • Young, A., Denaro, M. (1998). Roles of amylin in diabetes and in regulation of nutrient load. Nutrition. 14, 524-527.
    • (1998) Nutrition , vol.14 , pp. 524-527
    • Young, A.1    Denaro, M.2
  • 145
    • 84919729803 scopus 로고    scopus 로고
    • The pathogenic mechanism of diabetes varies with the degree of overexpression and oligomerization of human amylin in the pancreatic islet β cells
    • Zhang, S., Liu, H., Chuang, C.L., Li, X., Au, M., Zhang, L., Phillips, A.R., Scott, D.W., Cooper, G.J. (2014). The pathogenic mechanism of diabetes varies with the degree of overexpression and oligomerization of human amylin in the pancreatic islet β cells. FASEB J. 28, 5083-5096.
    • (2014) FASEB J , vol.28 , pp. 5083-5096
    • Zhang, S.1    Liu, H.2    Chuang, C.L.3    Li, X.4    Au, M.5    Zhang, L.6    Phillips, A.R.7    Scott, D.W.8    Cooper, G.J.9
  • 146
    • 79953204299 scopus 로고    scopus 로고
    • Neuronal receptor activity-modifying protein 1 promotes energy expenditure in mice
    • Zhang, Z., Liu, X., Morgan, D.A., Kuburas, A., Thedens, D.R., Russo, A.F., Rahmouni, K. (2011). Neuronal receptor activity-modifying protein 1 promotes energy expenditure in mice. Diabetes. 60, 1063-1071.
    • (2011) Diabetes , vol.60 , pp. 1063-1071
    • Zhang, Z.1    Liu, X.2    Morgan, D.A.3    Kuburas, A.4    Thedens, D.R.5    Russo, A.F.6    Rahmouni, K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.