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Volumn 44, Issue 49, 2005, Pages 16284-16291

The role of His-18 in amyloid formation by human islet amyloid polypeptide

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; ENZYMES; HISTOLOGY; MONOMERS; MORPHOLOGY; PH EFFECTS;

EID: 28944446580     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi051432v     Document Type: Article
Times cited : (147)

References (34)
  • 1
    • 0035856920 scopus 로고    scopus 로고
    • Global and societal implications of the diabetes epidemic
    • Zimmet, P., Alberti, K. G. M. M., and Shaw, J. (2001) Global and societal implications of the diabetes epidemic, Nature 414, 782-787.
    • (2001) Nature , vol.414 , pp. 782-787
    • Zimmet, P.1    Alberti, K.G.M.M.2    Shaw, J.3
  • 2
    • 0009781763 scopus 로고    scopus 로고
    • Insulin secretion in type-2 diabetes mellitus
    • Diabetes and Obesity, Humana Press, Totowa, NJ
    • Kudva, Y. C., and Butler, P. C. (1997) Insulin secretion in type-2 diabetes mellitus, In Clinical Research in Diabetes and Obesity, Vol. 2, Diabetes and Obesity, Humana Press, Totowa, NJ.
    • (1997) Clinical Research in Diabetes and Obesity , vol.2
    • Kudva, Y.C.1    Butler, P.C.2
  • 3
    • 0024026298 scopus 로고
    • Lilly Lecture 1987: The triumvirate: Cell, muscle, liver: A collusion responsible for NIDDM
    • DeFronzo, R. A. (1988) Lilly Lecture 1987: The triumvirate: Cell, muscle, liver: A collusion responsible for NIDDM, Diabetes 37, 667-687.
    • (1988) Diabetes , vol.37 , pp. 667-687
    • DeFronzo, R.A.1
  • 4
    • 0026452254 scopus 로고
    • Immunohistology of islet amyloid polypeptide in diabetes mellitus: Semiquantitative studies in a post-mortem series
    • Rocken, C., Linke, R. P., and Saeger, W. (1992) Immunohistology of islet amyloid polypeptide in diabetes mellitus: Semiquantitative studies in a post-mortem series, Virchows Arch. A Pathol. Anat. Histopathol. 421, 339-344.
    • (1992) Virchows Arch. a Pathol. Anat. Histopathol. , vol.421 , pp. 339-344
    • Rocken, C.1    Linke, R.P.2    Saeger, W.3
  • 5
    • 0018856283 scopus 로고
    • Das Amyloid der Langerhansschen Inseln und seine Beziehung zum Diabetes mellitus
    • Schneider, H. M., Storkel, S., and Will, W. (1980) Das Amyloid der Langerhansschen Inseln und seine Beziehung zum Diabetes mellitus, Dtsch. Med. Wochenschr. 105, 1143-1147.
    • (1980) Dtsch. Med. Wochenschr. , vol.105 , pp. 1143-1147
    • Schneider, H.M.1    Storkel, S.2    Will, W.3
  • 6
    • 0032969276 scopus 로고    scopus 로고
    • Islet amyloid: A long-recognied but underappreciated pathological feature of type 2 diabetes
    • Kahn, S. E., Andrikopoulos, S., and Verchere, C. B. (1999) Islet amyloid: A long-recognied 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
  • 8
    • 0028303844 scopus 로고
    • Pancreatic islet cell toxicity of amylin associated with type 2 diabetes mellitus
    • Lorenzo, A., Razzaboni, B., Weir, G., and Yankner, B. (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.3    Yankner, B.4
  • 10
    • 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., and Johnson, K. H. (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. U.S.A. 84, 3881-3885.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , 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
  • 11
    • 0023579739 scopus 로고
    • Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients
    • Cooper, G. J. S., Willis, A. C., Clark, A., Turner, R. C., Sim, R. B., and Reid, K. B. M. (1987) Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients, Proc. Natl. Acad. Sci. U.S.A. 84, 8628-8632.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 8628-8632
    • Cooper, G.J.S.1    Willis, A.C.2    Clark, A.3    Turner, R.C.4    Sim, R.B.5    Reid, K.B.M.6
  • 13
    • 0025967810 scopus 로고
    • Plasma islet amyloid polypeptide (amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients
    • Sanke, T., T., H., Nakano, Y., Oki, C., Okai, K., Nishimura, S., Kondo, M., and Nanjo, K. (1991) Plasma islet amyloid polypeptide (amylin) levels and their responses to oral glucose in type 2 (non-insulin-dependent) diabetic patients, Diabetologia 34, 129-132.
    • (1991) Diabetologia , vol.34 , pp. 129-132
    • Sanke, T.T.H.1    Nakano, Y.2    Oki, C.3    Okai, K.4    Nishimura, S.5    Kondo, M.6    Nanjo, K.7
  • 14
    • 0025287442 scopus 로고
    • Effects of meal ingestion on plasma amylin concentration in NIDDM and non-diabetic humans
    • Butler, P. C., Chou, J., Carter, W. B., Wang, Y. N., Bu, B. H., Chang, D., Chang, J. K., and Rizza, R. A. (1990) Effects of meal ingestion on plasma amylin concentration in NIDDM and non-diabetic humans, Diabetes 39, 752-756.
    • (1990) Diabetes , vol.39 , pp. 752-756
    • Butler, P.C.1    Chou, J.2    Carter, W.B.3    Wang, Y.N.4    Bu, B.H.5    Chang, D.6    Chang, J.K.7    Rizza, R.A.8
  • 15
    • 0024307859 scopus 로고
    • The insulin secretory granule
    • Hutton, J. C. (1989) The insulin secretory granule, Diabetologia 32, 271-281.
    • (1989) Diabetologia , vol.32 , pp. 271-281
    • Hutton, J.C.1
  • 17
    • 0031769349 scopus 로고    scopus 로고
    • Transgenic overexpression of human islet amyloid polypeptide inhibits insulin secretion and glucose elimination after gastric glucose gavage in mice
    • Ahren, B., Oosterwijk, C., Lips, C. J., and Hoppener, J. W. (1998) Transgenic overexpression of human islet amyloid polypeptide inhibits insulin secretion and glucose elimination after gastric glucose gavage in mice, Diabetologia 41, 1374-1380.
    • (1998) Diabetologia , vol.41 , pp. 1374-1380
    • Ahren, B.1    Oosterwijk, C.2    Lips, C.J.3    Hoppener, J.W.4
  • 19
    • 0033534397 scopus 로고    scopus 로고
    • Watching amyloid fibrils grow by time-lapse atomic force microscopy
    • Goldsbury, C. S., Kistler, J., Aebi, U., Arvinte, T., and Cooper, G. J. S. (1999) Watching amyloid fibrils grow by time-lapse atomic force microscopy, J. Mol. Biol. 285, 33-39.
    • (1999) J. Mol. Biol. , vol.285 , pp. 33-39
    • Goldsbury, C.S.1    Kistler, J.2    Aebi, U.3    Arvinte, T.4    Cooper, G.J.S.5
  • 21
    • 10844254749 scopus 로고    scopus 로고
    • The role of aromatic interactions in amyloid formation by polypeptides: Analysis of peptides derived from human amylin
    • Tracz, S. M., Abedini, A., Driscoll, M., and Raleigh, D. P. (2004) The role of aromatic interactions in amyloid formation by polypeptides: Analysis of peptides derived from human amylin, Biochemistry 43, 15901-15908.
    • (2004) Biochemistry , vol.43 , pp. 15901-15908
    • Tracz, S.M.1    Abedini, A.2    Driscoll, M.3    Raleigh, D.P.4
  • 23
    • 0018937820 scopus 로고
    • Role of zinc in insulin biosynthesis. Some possible zinc-insulin interactions in the pancreatic cell
    • Emdin, S. O., Dobson, G. G., Cutfield, J. M., and Cutfield, S. M. (1980) Role of zinc in insulin biosynthesis. Some possible zinc-insulin interactions in the pancreatic cell, Diabetologia 19, 174-182.
    • (1980) Diabetologia , vol.19 , pp. 174-182
    • Emdin, S.O.1    Dobson, G.G.2    Cutfield, J.M.3    Cutfield, S.M.4
  • 24
    • 0028886748 scopus 로고
    • Effect of pH and insulin on fibrillogenesis of islet amyloid polypeptide in vitro
    • Charge, S. B. P., de Koning, E. J. P., and Clark, A. (1995) Effect of pH and insulin on fibrillogenesis of islet amyloid polypeptide in vitro, Biochemistry 34, 14588-14593.
    • (1995) Biochemistry , vol.34 , pp. 14588-14593
    • Charge, S.B.P.1    De Koning, E.J.P.2    Clark, A.3
  • 25
    • 0027502784 scopus 로고
    • Thioflavin-T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine, H. (1993) Thioflavin-T interaction with synthetic Alzheimer's disease β-amyloid peptides: Detection of amyloid aggregation in solution, Protein Sci. 2, 404-410.
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • LeVine, H.1
  • 26
    • 0032079387 scopus 로고    scopus 로고
    • A novel assay in vitro of human islet amyloid polypeptide amyloidogenesis and effects of insulin secretory vesicle peptides on amyloid formation
    • Kudva, Y. C., Mueske, C., Butler, P. C., and Eberhardt, N. L. (1998) A novel assay in vitro of human islet amyloid polypeptide amyloidogenesis and effects of insulin secretory vesicle peptides on amyloid formation, Biochem. J. 331, 809-813.
    • (1998) Biochem. J. , vol.331 , pp. 809-813
    • Kudva, Y.C.1    Mueske, C.2    Butler, P.C.3    Eberhardt, N.L.4
  • 28
    • 0035804936 scopus 로고    scopus 로고
    • Identification of a novel human islet amyloid polypeptide β-sheet domain and factors influencing fibrillogenesis
    • Jaikaran, E. T. A. S., Higham, C. E., Serpell, L. C., Zurdo, J., Gross, M., Clark, A., and Fraser, P. E. (2001) Identification of a novel human islet amyloid polypeptide β-sheet domain and factors influencing fibrillogenesis, J. Mol. Biol. 308, 515-525.
    • (2001) J. Mol. Biol. , vol.308 , pp. 515-525
    • Jaikaran, E.T.A.S.1    Higham, C.E.2    Serpell, L.C.3    Zurdo, J.4    Gross, M.5    Clark, A.6    Fraser, P.E.7
  • 29
    • 16244376187 scopus 로고    scopus 로고
    • The parallel superpleated β-structure as a model for amyloid fibrils of human amylin
    • Kajava, A. V., Aebi, U., and Steven, A. C. (2005) The parallel superpleated β-structure as a model for amyloid fibrils of human amylin, J. Mol. Biol. 348, 247-252.
    • (2005) J. Mol. Biol. , vol.348 , pp. 247-252
    • Kajava, A.V.1    Aebi, U.2    Steven, A.C.3
  • 30
    • 0141746349 scopus 로고    scopus 로고
    • The role of protein stability, solubility, and net charge in amyloid fibril formation
    • Schmittschmitt, J. P., and Schotz, J. M. (2003) The role of protein stability, solubility, and net charge in amyloid fibril formation, Protein Sci. 12, 2378-2378.
    • (2003) Protein Sci , vol.12 , pp. 2378-2378
    • Schmittschmitt, J.P.1    Schotz, J.M.2
  • 31
    • 0030025653 scopus 로고    scopus 로고
    • Effects of β-cell granule components on human islet amyloid polypeptide fibril formation
    • Westermark, P., Li, Z. C., Westermark, G. T., Leckstrom, A., and Steiner, D. F. (1996) Effects of β-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    Leckstrom, A.4    Steiner, D.F.5
  • 32
    • 0031591653 scopus 로고    scopus 로고
    • β-cell granule peptides affect human islet amyloid polypeptide (IAPP) fibril formation in vitro
    • Janciauskiene, S., Eriksson, S., Carlemalm, E., and Ahren, B. (1997) β-Cell granule peptides affect human islet amyloid polypeptide (IAPP) fibril formation in vitro, Biochem. Biophys. Res. Commun. 236, 580-585.
    • (1997) Biochem. Biophys. Res. Commun. , vol.236 , pp. 580-585
    • Janciauskiene, S.1    Eriksson, S.2    Carlemalm, E.3    Ahren, B.4
  • 33
    • 1242292280 scopus 로고    scopus 로고
    • Pancreatic β-cell granule peptides form heteromolecular complexes which inhibit islet amyloid polypeptide fibril formation
    • Jaikaran, E. T. A. S., Nilsson, M. R., and Clark, A. (2004) Pancreatic β-cell granule peptides form heteromolecular complexes which inhibit islet amyloid polypeptide fibril formation, Biochem. J. 377, 709-716.
    • (2004) Biochem. J. , vol.377 , pp. 709-716
    • Jaikaran, E.T.A.S.1    Nilsson, M.R.2    Clark, A.3
  • 34
    • 0344687319 scopus 로고    scopus 로고
    • The mechanism of insulin action on islet amyloid polypeptide fiber formation
    • Larson, J. L., and Miranker, A. D. (2004) The mechanism of insulin action on islet amyloid polypeptide fiber formation, J. Mol. Biol. 335, 221-231.
    • (2004) J. Mol. Biol. , vol.335 , pp. 221-231
    • Larson, J.L.1    Miranker, A.D.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.