메뉴 건너뛰기




Volumn 14, Issue 4, 2013, Pages 330-337

Islet amyloid polypeptide and diabetes

Author keywords

Amylin; Amyloid; Calcitonin receptor; Fibril; IAPP; Islet amyloid polypeptide; RAMP; Receptor activity modifying proteins; Type 2 diabetes

Indexed keywords

AMYLIN; AMYLIN RECEPTOR; AMYLOID; AMYLOID PROTEIN; CALCITONIN RECEPTOR; RECEPTOR ACTIVITY MODIFYING PROTEIN 1; RECEPTOR ACTIVITY MODIFYING PROTEIN 3; SERUM AMYLOID P;

EID: 84888245583     PISSN: 13892037     EISSN: 18755550     Source Type: Journal    
DOI: 10.2174/13892037113149990050     Document Type: Article
Times cited : (26)

References (84)
  • 1
    • 0023025399 scopus 로고
    • A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas
    • Westermark, P.; Wernstedt, C.; Wilander, E.; Sletten, K. A novel peptide in the calcitonin gene related peptide family as an amyloid fibril protein in the endocrine pancreas. Biochem. Biophys. Res. Commun., 1986, 140, 827-831.
    • (1986) Biochem. Biophys. Res. Commun. , vol.140 , pp. 827-831
    • Westermark, P.1    Wernstedt, C.2    Wilander, E.3    Sletten, K.4
  • 2
    • 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, D.W.; O'Brien, T.D.; Johnson, K.H. 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., 1987, 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
  • 3
    • 0023579739 scopus 로고
    • Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients
    • Cooper, G.J.; Willis, A.C.; Clark, A.; Turner, R.C.; Sim, R.B.; Reid, K.B.M. Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc. Natl. Acad. Sci. USA., 1987, 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.M.6
  • 4
    • 85019282347 scopus 로고
    • On relation of chronic interstitial pancreatitis to the islands of Langerhans and to diabetes mellitus
    • Opie, E.L. On relation of chronic interstitial pancreatitis to the islands of Langerhans and to diabetes mellitus. J Exp Med., 1901, 5, 397-428.
    • (1901) J Exp Med , vol.5 , pp. 397-428
    • Opie, E.L.1
  • 5
    • 0009719314 scopus 로고
    • Zur Kenntnis der feineren Veränderungen des Pankreas bei Diabetes mellitus
    • Weichselbaum, A.; Stangl, E. Zur Kenntnis der feineren Veränderungen des Pankreas bei Diabetes mellitus. Wien klin Wochenschr., 1901, 14, 968-972.
    • (1901) Wien klin Wochenschr , vol.14 , pp. 968-972
    • Weichselbaum, A.1    Stangl, E.2
  • 7
    • 0017226393 scopus 로고
    • Characterization of amyloid fibril proteins from medullary carcinoma of the thyroid
    • Sletten, K.; Westermark, P.; Natvig, J.B. Characterization of amyloid fibril proteins from medullary carcinoma of the thyroid. J. Exp. Med., 1976, 143, 993-998.
    • (1976) J. Exp. Med. , vol.143 , pp. 993-998
    • Sletten, K.1    Westermark, P.2    Natvig, J.B.3
  • 9
    • 79954510553 scopus 로고    scopus 로고
    • Amyloid in the islets of Langerhans: Thoughts and some historical aspects
    • Westermark, P. Amyloid in the islets of Langerhans: Thoughts and some historical aspects. Ups. J. Med. Sci., 2011, 116, 81-89.
    • (2011) Ups. J. Med. Sci. , vol.116 , pp. 81-89
    • Westermark, P.1
  • 12
    • 0024428356 scopus 로고
    • Islet amyloid polypeptide (IAPP): CDNA cloning and identification of an amyloidogenic region associated with species-specific occurrence of age-related diabetes mellitus
    • Betsholtz, C.; Svensson, V.; Rorsman, F.; Engström, U.; Westermark, G.T.; Wilander, E.; Johnson, K.H.; Westermark, P. Islet amyloid polypeptide (IAPP): cDNA cloning and identification of an amyloidogenic region associated with species-specific occurrence of age-related diabetes mellitus. Exp. Cell Res., 1989, 183, 484-493.
    • (1989) Exp. Cell Res. , vol.183 , pp. 484-493
    • Betsholtz, C.1    Svensson, V.2    Rorsman, F.3    Engström, U.4    Westermark, G.T.5    Wilander, E.6    Johnson, K.H.7    Westermark, P.8
  • 13
    • 0024326627 scopus 로고
    • Human islet amyloid polypeptide gene: Complete nucleotide sequence, chromosomal localization, and evolutionary history
    • Nishi, M.; Sanke, T.; Seino, S.; Eddy, R.L.; Fan, Y.-S.; Byers, M.G.; Shows, T.B.; Bell, G.I.; Steiner, D.F. Human islet amyloid polypeptide gene: complete nucleotide sequence, chromosomal localization, and evolutionary history. Mol. Endocrinol., 1989, 3, 1775-1781.
    • (1989) Mol. Endocrinol. , vol.3 , pp. 1775-1781
    • Nishi, M.1    Sanke, T.2    Seino, S.3    Eddy, R.L.4    Fan, Y.-S.5    Byers, M.G.6    Shows, T.B.7    Bell, G.I.8    Steiner, D.F.9
  • 16
    • 0035123349 scopus 로고    scopus 로고
    • The prohormone convertase enzyme 2 (PC2) is essential for processing pro-islet amyloid polypeptide at the NH2-terminal cleavage site
    • Wang, J.; Xu, J.; Finnerty, J.; Furuta, M.; Steiner, D.F.; Verchere, C.B. The prohormone convertase enzyme 2 (PC2) is essential for processing pro-islet amyloid polypeptide at the NH2-terminal cleavage site. Diabetes, 2001, 50, 534-539.
    • (2001) Diabetes , vol.50 , pp. 534-539
    • Wang, J.1    Xu, J.2    Finnerty, J.3    Furuta, M.4    Steiner, D.F.5    Verchere, C.B.6
  • 18
    • 0026775947 scopus 로고
    • The biosynthesis and processing of neuroendocrine peptides: Identification of proprotein convertases involved in intravesicular processing
    • Smeekens, S.P.; Chan, S.J.; Steiner, D.F. The biosynthesis and processing of neuroendocrine peptides: identification of proprotein convertases involved in intravesicular processing. Prog. Brain Res., 1992, 92, 235-246.
    • (1992) Prog. Brain Res. , vol.92 , pp. 235-246
    • Smeekens, S.P.1    Chan, S.J.2    Steiner, D.F.3
  • 20
    • 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. Effects of beta cell granule components on human islet amyloid polypeptide fibril formation. FEBS Lett., 1996, 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
  • 21
    • 79954535899 scopus 로고    scopus 로고
    • Islet amyloid polypeptide, islet amyloid and diabetes mellitus
    • Westermark, P.; Andersson, A.; Westermark, G.T. Islet amyloid polypeptide, islet amyloid and diabetes mellitus. Physiol. Rev., 2011, 91, 795-826.
    • (2011) Physiol. Rev. , vol.91 , pp. 795-826
    • Westermark, P.1    Andersson, A.2    Westermark, G.T.3
  • 26
    • 0034896824 scopus 로고    scopus 로고
    • Effects of calcitonin, amylin, and calcitonin gene-related peptide on osteoclast development
    • Cornish, J.; Callon, K.E.; Bava, U.; Kamona, S.A.; Cooper, G.J.; Reid, I.R. Effects of calcitonin, amylin, and calcitonin gene-related peptide on osteoclast development. Bone, 2001, 29, 162-168.
    • (2001) Bone , vol.29 , pp. 162-168
    • Cornish, J.1    Callon, K.E.2    Bava, U.3    Kamona, S.A.4    Cooper, G.J.5    Reid, I.R.6
  • 28
    • 14544305644 scopus 로고    scopus 로고
    • Osteoclast-like cells express receptor activity modifying protein 2: Application of laser capture microdissection
    • Nakamura, M.; Morimoto, S.; Yang, Q.; Hisamatsu, T.; Hanai, N.; Nakamura, Y.; Mori, I.; Kakudo, K. Osteoclast-like cells express receptor activity modifying protein 2: application of laser capture microdissection. J. Mol. Endocrinol., 2005, 34, 257-261.
    • (2005) J. Mol. Endocrinol. , vol.34 , pp. 257-261
    • Nakamura, M.1    Morimoto, S.2    Yang, Q.3    Hisamatsu, T.4    Hanai, N.5    Nakamura, Y.6    Mori, I.7    Kakudo, K.8
  • 29
    • 33645221141 scopus 로고    scopus 로고
    • Receptor pharmacology
    • Young, A. Receptor pharmacology. Adv. Pharmacol., 2005, 52, 47-65.
    • (2005) Adv. Pharmacol. , vol.52 , pp. 47-65
    • Young, A.1
  • 30
    • 84862138093 scopus 로고    scopus 로고
    • Brainstem sensing of meal-related signals in energy homeostasis
    • Young, A.A. Brainstem sensing of meal-related signals in energy homeostasis. Neuropharmacology, 2012, 63, 31-45.
    • (2012) Neuropharmacology , vol.63 , pp. 31-45
    • Young, A.A.1
  • 32
    • 0035019741 scopus 로고    scopus 로고
    • Comparative effects of amylin and cholecystokinin on food intake and gastric emptying in rats
    • Reidelberger, R.D.; Arnelo, U.; Granqvist, L.; Permert, J. Comparative effects of amylin and cholecystokinin on food intake and gastric emptying in rats. Am. J. Physiol., 2001, 280, R605-R611.
    • (2001) Am. J. Physiol. , vol.280
    • Reidelberger, R.D.1    Arnelo, U.2    Granqvist, L.3    Permert, J.4
  • 33
    • 64349110518 scopus 로고    scopus 로고
    • Impaired hyperglycemia-induced delay in gastric emptying in patients with type 1 diabetes deficient for islet amyloid polypeptide
    • Woerle, H.J.; Albrecht, M.; Linke, R.; Zschau, S.; Neumann, C.; Nicolaus, M.; Gerich, J.E.; Göke, B.; Schirra, J. Impaired hyperglycemia-induced delay in gastric emptying in patients with type 1 diabetes deficient for islet amyloid polypeptide. Diabetes Care, 2008, 31, 2325-2331.
    • (2008) Diabetes Care , vol.31 , pp. 2325-2331
    • Woerle, H.J.1    Albrecht, M.2    Linke, R.3    Zschau, S.4    Neumann, C.5    Nicolaus, M.6    Gerich, J.E.7    Göke, B.8    Schirra, J.9
  • 34
    • 56649101954 scopus 로고    scopus 로고
    • Gastric emptying and postprandial glucose excursions in adolescents with type 1 diabetes
    • Heptulla, R.A.; Rodriguez, L.M.; Mason, K.J.; Haymond, M.W. Gastric emptying and postprandial glucose excursions in adolescents with type 1 diabetes. Pediatr. Diabetes, 2008, 9, 561-566.
    • (2008) Pediatr. Diabetes , vol.9 , pp. 561-566
    • Heptulla, R.A.1    Rodriguez, L.M.2    Mason, K.J.3    Haymond, M.W.4
  • 35
    • 0034463847 scopus 로고    scopus 로고
    • Coexpression of receptors for adrenomedullin, calcitonin generelated peptide, and amylin in pancreatic beta-cells
    • Martínez, A.; Kapas, S.; Miller, M.; Ward, Y.; Cuttitta, F. Coexpression of receptors for adrenomedullin, calcitonin generelated peptide, and amylin in pancreatic beta-cells. Endocrinology, 2000, 141, 406-411.
    • (2000) Endocrinology , vol.141 , pp. 406-411
    • Martínez, A.1    Kapas, S.2    Miller, M.3    Ward, Y.4    Cuttitta, F.5
  • 37
    • 0037471369 scopus 로고    scopus 로고
    • Islet amyloid polypeptide inhibits glucagon release and exerts a dual action on insulin release from isolated islets
    • Åkesson, B.; Panagiotidis, G.; Westermark, P.; Lundquist, I. Islet amyloid polypeptide inhibits glucagon release and exerts a dual action on insulin release from isolated islets. Regul. Pept., 2003, 111, 55-60.
    • (2003) Regul. Pept. , vol.111 , pp. 55-60
    • Åkesson, B.1    Panagiotidis, G.2    Westermark, P.3    Lundquist, I.4
  • 38
    • 84868374880 scopus 로고    scopus 로고
    • Amyloid fibril protein nomenclature: 2012 recommendations from the nomenclature committee of the International Society of Amyloidosis
    • Sipe, J.D.; Benson, M.D.; Buxbaum, J.N.; Ikeda, S.; Merlini, G.; Saraiva, M.J.; Westermark, P. Amyloid fibril protein nomenclature: 2012 recommendations from the nomenclature committee of the International Society of Amyloidosis. Amyloid, 2012, 19, 167-170.
    • (2012) Amyloid , vol.19 , pp. 167-170
    • Sipe, J.D.1    Benson, M.D.2    Buxbaum, J.N.3    Ikeda, S.4    Merlini, G.5    Saraiva, M.J.6    Westermark, P.7
  • 41
    • 0033865052 scopus 로고    scopus 로고
    • Review: Amyloidogenesis-unquestioned answers and unanswered questions
    • Kisilevsky, R. Review: Amyloidogenesis-unquestioned answers and unanswered questions. J. Struct. Biol., 2000, 130, 99-108.
    • (2000) J. Struct. Biol. , vol.130 , pp. 99-108
    • Kisilevsky, R.1
  • 42
    • 77649240855 scopus 로고    scopus 로고
    • Identifying the amylome, proteins capable of forming amyloid-like fibrils
    • Goldschmidt, L.; Teng, P.K.; Riek, R.; Eisenberg, D. Identifying the amylome, proteins capable of forming amyloid-like fibrils. Proc. Natl. Acad. Sci. USA., 2010, 107, 3487-3492.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 3487-3492
    • Goldschmidt, L.1    Teng, P.K.2    Riek, R.3    Eisenberg, D.4
  • 43
    • 84858374665 scopus 로고    scopus 로고
    • The amyloid state of protein in human diseases
    • Eisenberg, D.; Jucker, M. The amyloid state of protein in human diseases. Cell, 2012, 148, 1188-1203.
    • (2012) Cell , vol.148 , pp. 1188-1203
    • Eisenberg, D.1    Jucker, M.2
  • 45
    • 80053610643 scopus 로고    scopus 로고
    • Localized amyloid important in diseases outside the brain: Lessons from the islets of Langerhans and the thoracic aorta
    • Westermark, G.T.; Westermark, P. Localized amyloid important in diseases outside the brain: lessons from the islets of Langerhans and the thoracic aorta. FEBS J., 2011, 278, 3918-3929.
    • (2011) FEBS J. , vol.278 , pp. 3918-3929
    • Westermark, G.T.1    Westermark, P.2
  • 46
    • 1242292280 scopus 로고    scopus 로고
    • Pancreatic [-cell granule peptides form heteromolecular complexes which inhibit islet amyloid polypeptide fibril formation
    • Jaikaran, E.T.A.S.; Nilsson, M.R.; Clark, A. Pancreatic [-cell granule peptides form heteromolecular complexes which inhibit islet amyloid polypeptide fibril formation. Biochem. J., 2004, 377, 709-716.
    • (2004) Biochem. J. , vol.377 , pp. 709-716
    • Jaikaran, E.T.A.S.1    Nilsson, M.R.2    Clark, A.3
  • 47
    • 0031591653 scopus 로고    scopus 로고
    • B cell granule peptides affect human islet amyloid polypeptide (IAPP) fibril formation in vitro
    • Janciauskiene, S.; Eriksson, S.; Carlemalm, E.; Ahrén, B. B cell granule peptides affect human islet amyloid polypeptide (IAPP) fibril formation in vitro. Biochem. Biophys. Res. Commun., 1997, 236, 580-585.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 580-585
    • Janciauskiene, S.1    Eriksson, S.2    Carlemalm, E.3    Ahrén, B.4
  • 48
    • 0344687319 scopus 로고    scopus 로고
    • The mechanism of insulin action on islet amyloid polypeptide fiber formation
    • Larson, J.L.; Miranker, A.D. The mechanism of insulin action on islet amyloid polypeptide fiber formation. J. Mol. Biol., 2004, 335, 221-231.
    • (2004) J. Mol. Biol. , vol.335 , pp. 221-231
    • Larson, J.L.1    Miranker, A.D.2
  • 49
    • 77953710075 scopus 로고    scopus 로고
    • Suppression of IAPP fibrillation at anionic lipid membranes via IAPP-derived amyloid inhibitors and insulin
    • Sellin, D.; Yan, L.M.; Kapurniotu, A.; Winter, R. Suppression of IAPP fibrillation at anionic lipid membranes via IAPP-derived amyloid inhibitors and insulin. Biophys. Chem., 2010, 150, 73-79.
    • (2010) Biophys. Chem. , vol.150 , pp. 73-79
    • Sellin, D.1    Yan, L.M.2    Kapurniotu, A.3    Winter, R.4
  • 50
    • 0003071446 scopus 로고
    • Islet amyloid polypeptide and amyloid in the islets of Langerhans
    • In R.D.G. Leslie and D. Robbins, eds. (Cambridge: Cambridge Press University)
    • Westermark, P. (1995). Islet amyloid polypeptide and amyloid in the islets of Langerhans. In Diabetes: Clinical Science in Practice, R.D.G. Leslie and D. Robbins, eds. (Cambridge: Cambridge Press University), 189-199.
    • (1995) Diabetes: Clinical Science in Practice , pp. 189-199
    • Westermark, P.1
  • 51
    • 0000845316 scopus 로고
    • Hyalinization of the islets of Langerhans in diabetes mellitus
    • Bell, E.T. Hyalinization of the islets of Langerhans in diabetes mellitus. Diabetes. 1952, 1, 341-344.
    • (1952) Diabetes , vol.1 , pp. 341-344
    • Bell, E.T.1
  • 52
    • 72949142071 scopus 로고
    • Amyloidosis of the islets of Langerhans. A restudy of islet hyalin in diabetic and nondiabetic individuals
    • Ehrlich, J.C.; Ratner, I.M. Amyloidosis of the islets of Langerhans. A restudy of islet hyalin in diabetic and nondiabetic individuals. Am. J. Path., 1961, 38, 49-59.
    • (1961) Am. J. Path , vol.38 , pp. 49-59
    • Ehrlich, J.C.1    Ratner, I.M.2
  • 53
    • 0015884138 scopus 로고
    • The pancreatic islet cells in insular amyloidosis in human diabetic and non-diabetic adults
    • Westermark, P.; Grimelius, L. The pancreatic islet cells in insular amyloidosis in human diabetic and non-diabetic adults. Acta Path. Microbiol. Scand. A., 1973, 81, 291-300.
    • (1973) Acta Path. Microbiol. Scand. A , vol.81 , pp. 291-300
    • Westermark, P.1    Grimelius, L.2
  • 55
    • 0015277207 scopus 로고
    • Quantitative studies of amyloid in the islets of Langerhans
    • Westermark, P. Quantitative studies of amyloid in the islets of Langerhans. Upsala J. Med. Sci., 1972, 77, 91-94.
    • (1972) Upsala J. Med. Sci. , vol.77 , pp. 91-94
    • Westermark, P.1
  • 56
    • 0015930676 scopus 로고
    • Fine structure of islets of Langerhans in insular amyloidosis
    • Westermark, P. Fine structure of islets of Langerhans in insular amyloidosis. Virchows Arch. A., 1973, 359, 1-18.
    • (1973) Virchows Arch. A , vol.359 , pp. 1-18
    • Westermark, P.1
  • 57
    • 33646509867 scopus 로고    scopus 로고
    • Intracellular amyloid-like deposits contain unprocessed pro islet amyloid polypeptide (proIAPP) in beta-cells of transgenic mice overexpressing human IAPP and transplanted human islets
    • Paulsson, J.F.; Andersson, A.; Westermark, P.; Westermark, G.T. Intracellular amyloid-like deposits contain unprocessed pro islet amyloid polypeptide (proIAPP) in beta-cells of transgenic mice overexpressing human IAPP and transplanted human islets. Diabetologia, 2006, 49, 1237-1246.
    • (2006) Diabetologia , vol.49 , pp. 1237-1246
    • Paulsson, J.F.1    Andersson, A.2    Westermark, P.3    Westermark, G.T.4
  • 58
    • 31144458770 scopus 로고    scopus 로고
    • Oscillations of cyclic AMP in hormone-stimulated insulin-secreting beta-cells
    • Dyachok, O.; Isakov, Y.; Sågetorp, J.; Tengholm, A. Oscillations of cyclic AMP in hormone-stimulated insulin-secreting beta-cells. Nature, 2006, 439, 349-352.
    • (2006) Nature , vol.439 , pp. 349-352
    • Dyachok, O.1    Isakov, Y.2    Sågetorp, J.3    Tengholm, A.4
  • 59
    • 0034570847 scopus 로고    scopus 로고
    • Islet amyloid development in a mouse strain lacking endogenous islet amyloid polypeptide (IAPP) but expressing human IAPP
    • Westermark, G.T.; Gebre-Medhin, S.; Steiner, D.F.; Westermark, P. Islet amyloid development in a mouse strain lacking endogenous islet amyloid polypeptide (IAPP) but expressing human IAPP. Mol. Med., 2000, 6, 998-1007.
    • (2000) Mol. Med. , vol.6 , pp. 998-1007
    • Westermark, G.T.1    Gebre-Medhin, S.2    Steiner, D.F.3    Westermark, P.4
  • 60
    • 0035969513 scopus 로고    scopus 로고
    • Islet amyloid and type 2 diabetes: From molecular misfolding to islet pathophysiology
    • Jaikaran, E.T.A.S.; Clark, A. Islet amyloid and type 2 diabetes: from molecular misfolding to islet pathophysiology. Biochim. Biophys. Acta., 2001, 1537, 179-203.
    • (2001) Biochim. Biophys. Acta , vol.1537 , pp. 179-203
    • Jaikaran, E.T.A.S.1    Clark, A.2
  • 61
    • 4544365326 scopus 로고    scopus 로고
    • Formation of amyloid in human pancreatic islets transplanted to the liver and spleen of nude mice
    • Westermark, G.T.; Westermark, P.; Nordin, A.; Törnelius, E.; Andersson, A. Formation of amyloid in human pancreatic islets transplanted to the liver and spleen of nude mice. Ups. J. Med. Sci., 2003, 108, 193-204.
    • (2003) Ups. J. Med. Sci. , vol.108 , pp. 193-204
    • Westermark, G.T.1    Westermark, P.2    Nordin, A.3    Törnelius, E.4    Andersson, A.5
  • 64
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F.; Dobson, C.M. Protein misfolding, functional amyloid, and human disease. Annu. Rev. Biochem., 2006, 75, 333-366.
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 65
    • 0018146301 scopus 로고
    • The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus
    • Westermark, P.; Wilander, E. The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus. Diabetologia, 1978, 15, 417-421.
    • (1978) Diabetologia , vol.15 , pp. 417-421
    • Westermark, P.1    Wilander, E.2
  • 66
    • 0034632806 scopus 로고    scopus 로고
    • Islet amyloid and type 2 diabetes mellitus
    • Höppener, J.W.; Ahrén, B.; Lips, C.J. Islet amyloid and type 2 diabetes mellitus. N. Engl. J. Med., 2000, 343, 411-419.
    • (2000) N. Engl. J. Med. , vol.343 , pp. 411-419
    • Höppener, J.W.1    Ahrén, B.2    Lips, C.J.3
  • 67
    • 0842281551 scopus 로고    scopus 로고
    • Principles of protein folding, misfolding and aggregation
    • Dobson, C.M. Principles of protein folding, misfolding and aggregation. Sem. Cell Develop. Biol., 2004, 15, 3-16.
    • (2004) Sem. Cell Develop. Biol. , vol.15 , pp. 3-16
    • Dobson, C.M.1
  • 68
    • 0018627173 scopus 로고
    • Cyclic oscillations of basal plasma glucose and insulin concentrations in human beings
    • Lang, D.A.; Matthews, D.R.; Peto, J.; Turner, R.C. Cyclic oscillations of basal plasma glucose and insulin concentrations in human beings. N. Engl. J. Med., 1979, 301, 1023-1027.
    • (1979) N. Engl. J. Med. , vol.301 , pp. 1023-1027
    • Lang, D.A.1    Matthews, D.R.2    Peto, J.3    Turner, R.C.4
  • 69
    • 33847012626 scopus 로고    scopus 로고
    • Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets
    • Ritzel, R.A.; Meier, J.J.; Lin, C.Y.; Veldhuis, J.D.; Butler, P.C. Human islet amyloid polypeptide oligomers disrupt cell coupling, induce apoptosis, and impair insulin secretion in isolated human islets. Diabetes, 2007, 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
  • 72
    • 0032937607 scopus 로고    scopus 로고
    • Differences in amyloid deposition in islets of transgenic mice expressing human islet amyloid polypeptide versus human islets implanted into nude mice
    • Westermark, G.T.; Westermark, P.; Eizirik, D.; Hellerström, C.; Fox, N.; Steiner, D.F.; Andersson, A. Differences in amyloid deposition in islets of transgenic mice expressing human islet amyloid polypeptide versus human islets implanted into nude mice. Metabolism, 1999, 48, 448-454.
    • (1999) Metabolism , vol.48 , pp. 448-454
    • Westermark, G.T.1    Westermark, P.2    Eizirik, D.3    Hellerström, C.4    Fox, N.5    Steiner, D.F.6    Andersson, A.7
  • 74
    • 84861607456 scopus 로고    scopus 로고
    • Extensive amyloid formation in transplanted microencapsulated mouse and human islets
    • Bohman, S.; Westermark, G.T. Extensive amyloid formation in transplanted microencapsulated mouse and human islets. Amyloid, 2012, 19, 87-93.
    • (2012) Amyloid , vol.19 , pp. 87-93
    • Bohman, S.1    Westermark, G.T.2
  • 75
    • 27244452084 scopus 로고    scopus 로고
    • Is aggregated IAPP a cause of beta-cell failure in transplanted human pancreatic islets?
    • Westermark, P.; Andersson, A.; Westermark, G.T. Is aggregated IAPP a cause of beta-cell failure in transplanted human pancreatic islets? Curr. Diab. Rep., 2005, 5, 184-188.
    • (2005) Curr. Diab. Rep. , vol.5 , pp. 184-188
    • Westermark, P.1    Andersson, A.2    Westermark, G.T.3
  • 76
    • 50449085533 scopus 로고    scopus 로고
    • Widespread amyloid deposition in transplanted human pancreatic islets
    • Westermark, G.T.; Westermark, P.; Berne, C.; Korsgren, O. Widespread amyloid deposition in transplanted human pancreatic islets. N. Engl. J. Med., 2008, 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
  • 79
    • 0037342152 scopus 로고    scopus 로고
    • Gene expression profiles of nondiabetic and diabetic obese mice suggest a role of hepatic lipogenic capacity in diabetes susceptibility
    • Lan, H.; Rabaglia, M.E.; Stoehr, J.P.; Nadler, S.T.; Schueler, K.L.; Zou, F.; Yandell, B.S.; Attie, A.D. Gene expression profiles of nondiabetic and diabetic obese mice suggest a role of hepatic lipogenic capacity in diabetes susceptibility. Diabetes, 2003, 52, 688-700.
    • (2003) Diabetes , vol.52 , pp. 688-700
    • Lan, H.1    Rabaglia, M.E.2    Stoehr, J.P.3    Nadler, S.T.4    Schueler, K.L.5    Zou, F.6    Yandell, B.S.7    Attie, A.D.8
  • 83
    • 0034712910 scopus 로고    scopus 로고
    • Mouse receptor-activity-modifying proteins 1,-2 and-3: Amino acid sequence, expression and function
    • Husmann, K.; Sexton, P.M.; Fischer, J.A.; Born, W. Mouse receptor-activity-modifying proteins 1,-2 and-3: amino acid sequence, expression and function. Mol. Cell. Endocrinol., 2000, 162, 35-43.
    • (2000) Mol. Cell. Endocrinol. , vol.162 , pp. 35-43
    • Husmann, K.1    Sexton, P.M.2    Fischer, J.A.3    Born, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.