메뉴 건너뛰기




Volumn 14, Issue 3, 2013, Pages 1083-1097

Preparation and characterization of PEGylated amylin

Author keywords

amylin; diabetes; islet associated polypeptide; PEGylation; receptor activity modifying protein

Indexed keywords

AMINE; AMINO ACID; AMYLIN; DIMETHYL SULFOXIDE; FLUORESCAMINE; GLUCOSE; LYSINE; MACROGOL DERIVATIVE; METHOXY POLYETHYLENE GLYCOL SUCCINIMIDYL CARBONATE; METHOXY POLYETHYLENE GLYCOL SUCCINIMIDYL PROPIONATE; RECEPTOR ACTIVITY MODIFYING PROTEIN 2; UNCLASSIFIED DRUG;

EID: 84890218967     PISSN: None     EISSN: 15309932     Source Type: Journal    
DOI: 10.1208/s12249-013-9987-4     Document Type: Article
Times cited : (21)

References (74)
  • 1
    • 0025957988 scopus 로고
    • Basal and stimulated plasma levels of pancreatic amylin indicate its co-secretion with insulin in humans
    • 2055340 10.1007/BF00404025 1:CAS:528:DyaK3MXltleiu7Y%3D
    • Hartter E, Svoboda T, Ludvik B, Schuller M, Lell B, Kuenburg E, et al. Basal and stimulated plasma levels of pancreatic amylin indicate its co-secretion with insulin in humans. Diabetologia. 1991;34(1):52-4.
    • (1991) Diabetologia , vol.34 , Issue.1 , pp. 52-54
    • Hartter, E.1    Svoboda, T.2    Ludvik, B.3    Schuller, M.4    Lell, B.5    Kuenburg, E.6
  • 3
    • 84859163527 scopus 로고    scopus 로고
    • Amylin and related proteins: Physiology and pathophysiology
    • L.S. Jefferson A.D. Cherring (eds) Oxford University Press New York
    • Cooper GJS. Amylin and related proteins: physiology and pathophysiology. In: Jefferson LS, Cherring AD, editors. Handbook of physiology. New York: Oxford University Press; 2001.
    • (2001) Handbook of Physiology
    • Cooper, G.J.S.1
  • 4
    • 0026320675 scopus 로고
    • Amylin and insulin co-replacement therapy for insulin-dependent (type I) diabetes mellitus
    • 1787825 10.1016/0306-9877(91)90150-W 1:STN:280:DyaK387lsl2isA%3D%3D
    • Cooper GJ. Amylin and insulin co-replacement therapy for insulin-dependent (type I) diabetes mellitus. Med Hypotheses. 1991;36(3):284-8.
    • (1991) Med Hypotheses , vol.36 , Issue.3 , pp. 284-288
    • Cooper, G.J.1
  • 5
    • 0023579739 scopus 로고
    • Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients
    • 3317417 10.1073/pnas.84.23.8628 1:CAS:528:DyaL1cXpt1GmtA%3D%3D
    • Cooper GJ, Willis AC, Clark A, Turner RC, Sim RB, Reid KB. Purification and characterization of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc Natl Acad Sci USA. 1987;84(23):8628-32.
    • (1987) Proc Natl Acad Sci USA , vol.84 , Issue.23 , 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
  • 7
    • 0023222388 scopus 로고
    • Islet amyloid in type 2 human diabetes mellitus and adult diabetic cats contains a novel putative polypeptide hormone
    • 3296768 1:CAS:528:DyaL2sXlslels7k%3D
    • Westermark P, Wernstedt C, O'Brien TD, Hayden DW, Johnson KH. Islet amyloid in type 2 human diabetes mellitus and adult diabetic cats contains a novel putative polypeptide hormone. Am J Pathol. 1987;127(3):414-7.
    • (1987) Am J Pathol , vol.127 , Issue.3 , pp. 414-417
    • Westermark, P.1    Wernstedt, C.2    O'Brien, T.D.3    Hayden, D.W.4    Johnson, K.H.5
  • 8
    • 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
    • 3035556 10.1073/pnas.84.11.3881 1:CAS:528:DyaL2sXksFKrtr0%3D
    • Westermark P, Wernstedt C, Wilander E, Hayden DW, O'Brien TD, Johnson KH. 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(11):3881-5.
    • (1987) Proc Natl Acad Sci USA , vol.84 , Issue.11 , 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
  • 9
    • 0344638970 scopus 로고
    • Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle
    • 3051005 10.1073/pnas.85.20.7763 1:CAS:528:DyaL1MXls1ej
    • Cooper GJ, Leighton B, Dimitriadis GD, Parry-Billings M, Kowalchuk JM, Howland K, et al. Amylin found in amyloid deposits in human type 2 diabetes mellitus may be a hormone that regulates glycogen metabolism in skeletal muscle. Proc Natl Acad Sci USA. 1988;85(20):7763-6.
    • (1988) Proc Natl Acad Sci USA , vol.85 , Issue.20 , pp. 7763-7766
    • Cooper, G.J.1    Leighton, B.2    Dimitriadis, G.D.3    Parry-Billings, M.4    Kowalchuk, J.M.5    Howland, K.6
  • 10
    • 8944258562 scopus 로고    scopus 로고
    • Preclinical pharmacology of pramlintide in the rat: Comparisons with human and rat amylin
    • 10.1002/(SICI)1098-2299(199604)37:4<231: AID-DDR5>3.0.CO;2-M 1:CAS:528:DyaK28XktFWit7c%3D
    • Young AA, Vine W, Gedulin BR, Pittner R, Janes S, Gaeta LS, et al. Preclinical pharmacology of pramlintide in the rat: comparisons with human and rat amylin. Drug Development Research. 1996;37:231-48.
    • (1996) Drug Development Research , vol.37 , pp. 231-248
    • Young, A.A.1    Vine, W.2    Gedulin, B.R.3    Pittner, R.4    Janes, S.5    Gaeta, L.S.6
  • 11
    • 0025366838 scopus 로고
    • Islet amyloid polypeptide: Pinpointing amino acid residues linked to amyloid fibril formation
    • 2195544 10.1073/pnas.87.13.5036 1:CAS:528:DyaK3cXkslWnsL0%3D
    • Westermark P, Engstrom U, Johnson KH, Westermark GT, Betsholtz C. Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation. Proc Natl Acad Sci USA. 1990;87(13):5036-40.
    • (1990) Proc Natl Acad Sci USA , vol.87 , Issue.13 , pp. 5036-5040
    • Westermark, P.1    Engstrom, U.2    Johnson, K.H.3    Westermark, G.T.4    Betsholtz, C.5
  • 13
    • 0017701219 scopus 로고
    • Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol
    • 405385 1:CAS:528:DyaE2sXksV2it7c%3D
    • Abuchowski A, Van ET, Palczuk NC, Davis FF. Alteration of immunological properties of bovine serum albumin by covalent attachment of polyethylene glycol. J Biol Chem. 1977;252(11):3578-81.
    • (1977) J Biol Chem , vol.252 , Issue.11 , pp. 3578-3581
    • Abuchowski, A.1    Van, E.T.2    Palczuk, N.C.3    Davis, F.F.4
  • 14
    • 0037362655 scopus 로고    scopus 로고
    • Effect of pegylation on pharmaceuticals
    • 12612647 10.1038/nrd1033 1:CAS:528:DC%2BD3sXhsFKrtLs%3D
    • Harris JM, Chess RB. Effect of pegylation on pharmaceuticals. Nat Rev Drug Discov. 2003;2(3):214-21.
    • (2003) Nat Rev Drug Discov , vol.2 , Issue.3 , pp. 214-221
    • Harris, J.M.1    Chess, R.B.2
  • 15
    • 84858228160 scopus 로고    scopus 로고
    • Polymeric conjugates for drug delivery
    • 22707853 10.1021/cm2031569 1:CAS:528:DC%2BC38XivVequg%3D%3D
    • Larson N, Ghandehari H. Polymeric conjugates for drug delivery. Chem Mater. 2012;24(5):840-53.
    • (2012) Chem Mater , vol.24 , Issue.5 , pp. 840-853
    • Larson, N.1    Ghandehari, H.2
  • 16
    • 33846874991 scopus 로고    scopus 로고
    • High-yield production of biologically active mono-PEGylated salmon calcitonin by site-specific PEGylation
    • 17207880 10.1016/j.jconrel.2006.11.013 1:CAS:528:DC%2BD2sXhsFCgtb0%3D
    • Youn YS, Na DH, Lee KC. High-yield production of biologically active mono-PEGylated salmon calcitonin by site-specific PEGylation. J Control Release. 2007;117(3):371-9.
    • (2007) J Control Release , vol.117 , Issue.3 , pp. 371-379
    • Youn, Y.S.1    Na, D.H.2    Lee, K.C.3
  • 17
    • 26944452043 scopus 로고    scopus 로고
    • PEGylation, successful approach to drug delivery
    • 16243265 10.1016/S1359-6446(05)03575-0 1:CAS:528:DC%2BD2MXhtFers7rF
    • Veronese FM, Pasut G. PEGylation, successful approach to drug delivery. Drug Discov Today. 2005;10(21):1451-8.
    • (2005) Drug Discov Today , vol.10 , Issue.21 , pp. 1451-1458
    • Veronese, F.M.1    Pasut, G.2
  • 18
    • 77952224043 scopus 로고    scopus 로고
    • Protein conjugates purification and characterization
    • F.M. Veronese (eds) 1 Birkhäuser Basel 10.1007/978-3-7643-8679-5-7
    • Fee CJ. Protein conjugates purification and characterization. In: Veronese FM, editor. PEGylated protein drugs: basic science and clinical applications. 1st ed. Basel: Birkhäuser; 2009. p. 113-25.
    • (2009) PEGylated Protein Drugs: Basic Science and Clinical Applications , pp. 113-125
    • Fee, C.J.1
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 5432063 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli UK. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970;227(259):680-5.
    • (1970) Nature , vol.227 , Issue.259 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 77952745485 scopus 로고    scopus 로고
    • Biochemical and biophysical characterization of lysozyme modified by PEGylation
    • 10.1016/j.ijpharm.2010.03.036 1:CAS:528:DC%2BC3cXmtVGku7c%3D
    • Freitas DS, Abrahao NJ. Biochemical and biophysical characterization of lysozyme modified by PEGylation. International Journal of Pharmaceutics. 2010;392:111-7.
    • (2010) International Journal of Pharmaceutics , vol.392 , pp. 111-117
    • Freitas, D.S.1    Abrahao, N.J.2
  • 21
    • 84870239118 scopus 로고    scopus 로고
    • A new site-specific monoPEGylated filgrastim derivative prepared by enzymatic conjugation: Production and physicochemical characterization
    • 22735238 10.1016/j.jconrel.2012.06.026 1:CAS:528:DC%2BC38XhtVWisb3L
    • Scaramuzza S, Tonon G, Olianas A, Messana I, Schrepfer R, Orsini G, et al. A new site-specific monoPEGylated filgrastim derivative prepared by enzymatic conjugation: production and physicochemical characterization. J Control Release. 2012;164(3):355-63.
    • (2012) J Control Release , vol.164 , Issue.3 , pp. 355-363
    • Scaramuzza, S.1    Tonon, G.2    Olianas, A.3    Messana, I.4    Schrepfer, R.5    Orsini, G.6
  • 22
    • 84863205849 scopus 로고    scopus 로고
    • NIH image to ImageJ: 25 years of image analysis
    • 22930834 10.1038/nmeth.2089 1:CAS:528:DC%2BC38XhtVKntb7P
    • Schneider CA, Rasband WS, Eliceiri KW. NIH image to ImageJ: 25 years of image analysis. Nature Methods. 2012;9:671-5.
    • (2012) Nature Methods , vol.9 , pp. 671-675
    • Schneider, C.A.1    Rasband, W.S.2    Eliceiri, K.W.3
  • 23
    • 77957356491 scopus 로고    scopus 로고
    • Fityk: A general-purpose peak fitting program
    • 10.1107/S0021889810030499 1:CAS:528:DC%2BC3cXhtFOqsbbK
    • Wojdyr M. Fityk: a general-purpose peak fitting program. Journal of Applied Crystallography. 2010;43:1126-8.
    • (2010) Journal of Applied Crystallography , vol.43 , pp. 1126-1128
    • Wojdyr, M.1
  • 24
    • 0015522277 scopus 로고
    • Fluorescamine: A reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range
    • 5085985 10.1126/science.178.4063.871 1:CAS:528:DyaE3sXis1ShsA%3D%3D
    • Udenfriend S, Stein S, Bohlen P, Dairman W, Leimgruber W, Weigele M. Fluorescamine: a reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range. Science. 1972;178(63):871-2.
    • (1972) Science , vol.178 , Issue.63 , pp. 871-872
    • Udenfriend, S.1    Stein, S.2    Bohlen, P.3    Dairman, W.4    Leimgruber, W.5    Weigele, M.6
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 942051 10.1016/0003-2697(76)90527-3 1:CAS:528:DyaE28XksVehtrY%3D
    • Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analyt Biochem. 1976;72:248-54.
    • (1976) Analyt Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 41149140769 scopus 로고    scopus 로고
    • MMass data miner: An open source alternative for mass spectrometric data analysis
    • 18293430 10.1002/rcm.3444
    • Strohalm M, Hassman M, Kosata B, Kodicek M. mMass data miner: an open source alternative for mass spectrometric data analysis. Rapid Communications in Mass Spectrometry. 2008;22(6):905-8.
    • (2008) Rapid Communications in Mass Spectrometry , vol.22 , Issue.6 , pp. 905-908
    • Strohalm, M.1    Hassman, M.2    Kosata, B.3    Kodicek, M.4
  • 27
    • 84856185720 scopus 로고    scopus 로고
    • Structural basis for extracellular interactions between calcitonin receptor-like receptor and receptor activity-modifying protein 2 for adrenomedullin-specific binding
    • 22102369 10.1002/pro.2003 1:CAS:528:DC%2BC38Xpslyqtw%3D%3D
    • Kusano S, Kukimoto-Niino M, Hino N, Ohsawa N, Okuda K, Sakamoto K, et al. Structural basis for extracellular interactions between calcitonin receptor-like receptor and receptor activity-modifying protein 2 for adrenomedullin-specific binding. Protein Sci. 2012;21(2):199-210.
    • (2012) Protein Sci , vol.21 , Issue.2 , pp. 199-210
    • Kusano, S.1    Kukimoto-Niino, M.2    Hino, N.3    Ohsawa, N.4    Okuda, K.5    Sakamoto, K.6
  • 28
    • 34250350054 scopus 로고    scopus 로고
    • Low-resolution structure and fluorescence anisotropy analysis of protein tyrosine phosphatase eta catalytic domain
    • 17400699 10.1529/biophysj.106.094961 1:CAS:528:DC%2BD2sXmsFektrs%3D
    • Matozo HC, Santos MAM, Neto MD, Bleicher L, Lima LMTR, Iuliano R, et al. Low-resolution structure and fluorescence anisotropy analysis of protein tyrosine phosphatase eta catalytic domain. Biophys J. 2007;92(12):4424-32.
    • (2007) Biophys J , vol.92 , Issue.12 , pp. 4424-4432
    • Matozo, H.C.1    Santos, M.A.M.2    Neto, M.D.3    Bleicher, L.4    Lima, L.5    Iuliano, R.6
  • 29
    • 0027104852 scopus 로고
    • Homologous islet amyloid polypeptide: Effects on plasma levels of glucagon, insulin and glucose in the mouse
    • 1337737 10.1016/0168-8227(92)90142-E 1:CAS:528:DyaK3sXisVyju7g%3D
    • Panagiotidis G, Salehi AA, Westermark P, Lundquist I. Homologous islet amyloid polypeptide: effects on plasma levels of glucagon, insulin and glucose in the mouse. Diabetes Res Clin Pract. 1992;18(3):167-71.
    • (1992) Diabetes Res Clin Pract , vol.18 , Issue.3 , pp. 167-171
    • Panagiotidis, G.1    Salehi, A.A.2    Westermark, P.3    Lundquist, I.4
  • 31
    • 77956534963 scopus 로고    scopus 로고
    • Standard operating procedures for describing and performing metabolic tests of glucose homeostasis in mice
    • 20713647 10.1242/dmm.006239 1:CAS:528:DC%2BC3MXhvVertLg%3D
    • Ayala JE, Samuel VT, Morton GJ, Obici S, Croniger CM, Shulman GI, et al. Standard operating procedures for describing and performing metabolic tests of glucose homeostasis in mice. Dis Model Mech. 2010;3(9-10):525-34.
    • (2010) Dis Model Mech , vol.3 , Issue.9-10 , pp. 525-534
    • Ayala, J.E.1    Samuel, V.T.2    Morton, G.J.3    Obici, S.4    Croniger, C.M.5    Shulman, G.I.6
  • 32
    • 0028237050 scopus 로고
    • Identification and characterization of O-biotinylated hydroxy amino acid residues in peptides
    • 8080081 10.1006/abio.1994.1263 1:CAS:528:DyaK2cXktlSntbk%3D
    • Miller BT, Rogers ME, Smith JS, Kurosky A. Identification and characterization of O-biotinylated hydroxy amino acid residues in peptides. Analyt Biochem. 1994;219(2):240-8.
    • (1994) Analyt Biochem , vol.219 , Issue.2 , pp. 240-248
    • Miller, B.T.1    Rogers, M.E.2    Smith, J.S.3    Kurosky, A.4
  • 33
    • 0027421928 scopus 로고
    • Elevated intrinsic reactivity of seryl hydroxyl groups within the linear peptide triads His-Xaa-Ser or Ser-Xaa-His
    • 8216328 10.1006/bbrc.1993.2272 1:CAS:528:DyaK2cXhtVOksrg%3D
    • Miller BT, Kurosky A. Elevated intrinsic reactivity of seryl hydroxyl groups within the linear peptide triads His-Xaa-Ser or Ser-Xaa-His. Biochem Biophys Res Commun. 1993;196(1):461-7.
    • (1993) Biochem Biophys Res Commun , vol.196 , Issue.1 , pp. 461-467
    • Miller, B.T.1    Kurosky, A.2
  • 34
    • 0029339452 scopus 로고
    • Comparison of three common amine reactive fluorescent probes used for conjugation to biomolecules by capillary zone electrophoresis
    • 7578365 10.1021/bc00034a015 1:CAS:528:DyaK2MXms1GnsL8%3D
    • Banks PR, Paquette DM. Comparison of three common amine reactive fluorescent probes used for conjugation to biomolecules by capillary zone electrophoresis. Bioconjug Chem. 1995;6(4):447-58.
    • (1995) Bioconjug Chem , vol.6 , Issue.4 , pp. 447-458
    • Banks, P.R.1    Paquette, D.M.2
  • 35
    • 0037124506 scopus 로고    scopus 로고
    • Chemistry for peptide and protein PEGylation
    • 12052709 10.1016/S0169-409X(02)00022-4 1:CAS:528:DC%2BD38XktFKiu7g%3D
    • Roberts MJ, Bentley MD, Harris JM. Chemistry for peptide and protein PEGylation. Adv Drug Deliv Rev. 2002;54(4):459-76.
    • (2002) Adv Drug Deliv Rev , vol.54 , Issue.4 , pp. 459-476
    • Roberts, M.J.1    Bentley, M.D.2    Harris, J.M.3
  • 36
    • 33749830133 scopus 로고    scopus 로고
    • Molecular mapping of the recognition interface between the islet amyloid polypeptide and insulin
    • 16960910 10.1002/anie.200602034 1:CAS:528:DC%2BD28XhtFWgsr3P
    • Gilead S, Wolfenson H, Gazit E. Molecular mapping of the recognition interface between the islet amyloid polypeptide and insulin. Angew Chem Int Ed Engl. 2006;45(39):6476-80.
    • (2006) Angew Chem Int Ed Engl , vol.45 , Issue.39 , pp. 6476-6480
    • Gilead, S.1    Wolfenson, H.2    Gazit, E.3
  • 37
    • 33750302461 scopus 로고    scopus 로고
    • Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism
    • 17051221 10.1038/nature05143 1:CAS:528:DC%2BD28XhtVyktbjO
    • Shen Y, Joachimiak A, Rosner MR, Tang WJ. Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism. Nature. 2006;443(7113):870-4.
    • (2006) Nature , vol.443 , Issue.7113 , pp. 870-874
    • Shen, Y.1    Joachimiak, A.2    Rosner, M.R.3    Tang, W.J.4
  • 38
    • 0034667661 scopus 로고    scopus 로고
    • Receptor-activity-modifying protein 1 forms heterodimers with two G-protein-coupled receptors to define ligand recognition
    • 11023820 10.1042/0264-6021:3510347 1:CAS:528:DC%2BD3cXnvFSqt7Y%3D
    • Leuthauser K, Gujer R, Aldecoa A, McKinney RA, Muff R, Fischer JA, et al. Receptor-activity-modifying protein 1 forms heterodimers with two G-protein-coupled receptors to define ligand recognition. Biochem J. 2000;351(Pt 2):347-51.
    • (2000) Biochem J , vol.351 , Issue.PART 2 , pp. 347-351
    • Leuthauser, K.1    Gujer, R.2    Aldecoa, A.3    McKinney, R.A.4    Muff, R.5    Fischer, J.A.6
  • 39
    • 0033932339 scopus 로고    scopus 로고
    • Amylin receptor phenotypes derived from human calcitonin receptor/RAMP coexpression exhibit pharmacological differences dependent on receptor isoform and host cell environment
    • 10871296 1:CAS:528:DC%2BD3cXksFyht7w%3D
    • Tilakaratne N, Christopoulos G, Zumpe ET, Foord SM, Sexton PM. Amylin receptor phenotypes derived from human calcitonin receptor/RAMP coexpression exhibit pharmacological differences dependent on receptor isoform and host cell environment. J Pharmacol Exp Ther. 2000;294(1):61-72.
    • (2000) J Pharmacol Exp Ther , vol.294 , Issue.1 , pp. 61-72
    • Tilakaratne, N.1    Christopoulos, G.2    Zumpe, E.T.3    Foord, S.M.4    Sexton, P.M.5
  • 40
    • 17844365264 scopus 로고    scopus 로고
    • Pharmacological discrimination of calcitonin receptor: Receptor activity-modifying protein complexes
    • 15692146 10.1124/mol.104.008615 1:CAS:528:DC%2BD2MXktFegt7o%3D
    • Hay DL, Christopoulos G, Christopoulos A, Poyner DR, Sexton PM. Pharmacological discrimination of calcitonin receptor: receptor activity-modifying protein complexes. Mol Pharmacol. 2005;67(5):1655-65.
    • (2005) Mol Pharmacol , vol.67 , Issue.5 , pp. 1655-1665
    • Hay, D.L.1    Christopoulos, G.2    Christopoulos, A.3    Poyner, D.R.4    Sexton, P.M.5
  • 41
    • 33746393683 scopus 로고    scopus 로고
    • Complexing receptor pharmacology: Modulation of family B G protein-coupled receptor function by RAMPs
    • 16888151 10.1196/annals.1317.076 1:CAS:528:DC%2BD28XpvVehsLY%3D
    • Sexton PM, Morfis M, Tilakaratne N, Hay DL, Udawela M, Christopoulos G, et al. Complexing receptor pharmacology: modulation of family B G protein-coupled receptor function by RAMPs. Ann N Y Acad Sci. 2006;1070:90-104.
    • (2006) Ann N y Acad Sci , vol.1070 , pp. 90-104
    • Sexton, P.M.1    Morfis, M.2    Tilakaratne, N.3    Hay, D.L.4    Udawela, M.5    Christopoulos, G.6
  • 42
    • 0033039911 scopus 로고    scopus 로고
    • Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product
    • 10385705 1:CAS:528:DyaK1MXksFOmtLY%3D
    • Christopoulos G, Perry KJ, Morfis M, Tilakaratne N, Gao Y, Fraser NJ, et al. Multiple amylin receptors arise from receptor activity-modifying protein interaction with the calcitonin receptor gene product. Mol Pharmacol. 1999;56(1):235-42.
    • (1999) Mol Pharmacol , vol.56 , Issue.1 , pp. 235-242
    • Christopoulos, G.1    Perry, K.J.2    Morfis, M.3    Tilakaratne, N.4    Gao, Y.5    Fraser, N.J.6
  • 44
    • 80052721057 scopus 로고    scopus 로고
    • More than insulin
    • 21904314 10.1038/nbt.1967 1:CAS:528:DC%2BC3MXhtFCnt7nM
    • Eisenstein M. More than insulin. Nat Biotechnol. 2011;29(9):782-5.
    • (2011) Nat Biotechnol , vol.29 , Issue.9 , pp. 782-785
    • Eisenstein, M.1
  • 45
    • 2942635897 scopus 로고    scopus 로고
    • First Brazilian pancreatic islet transplantation in a patient with type 1 diabetes mellitus
    • 15194388 10.1016/j.transproceed.2004.04.065 1:STN:280: DC%2BD2c3psVWhtg%3D%3D
    • Eliaschewitz FG, Aita CA, Genzini T, Noronha IL, Lojudice FH, Labriola L, et al. First Brazilian pancreatic islet transplantation in a patient with type 1 diabetes mellitus. Transplant Proc. 2004;36(4):1117-8.
    • (2004) Transplant Proc , vol.36 , Issue.4 , pp. 1117-1118
    • Eliaschewitz, F.G.1    Aita, C.A.2    Genzini, T.3    Noronha, I.L.4    Lojudice, F.H.5    Labriola, L.6
  • 46
    • 77951611220 scopus 로고    scopus 로고
    • Conversion of adult pancreatic alpha-cells to beta-cells after extreme beta-cell loss
    • 20364121 10.1038/nature08894 1:CAS:528:DC%2BC3cXkt1aqtLc%3D
    • Thorel F, Nepote V, Avril I, Kohno K, Desgraz R, Chera S, et al. Conversion of adult pancreatic alpha-cells to beta-cells after extreme beta-cell loss. Nature. 2010;464(7292):1149-54.
    • (2010) Nature , vol.464 , Issue.7292 , pp. 1149-1154
    • Thorel, F.1    Nepote, V.2    Avril, I.3    Kohno, K.4    Desgraz, R.5    Chera, S.6
  • 47
    • 77952703708 scopus 로고    scopus 로고
    • The role of amylin in the control of energy homeostasis
    • 20357016 10.1152/ajpregu.00703.2009 1:CAS:528:DC%2BC3cXnslCnsrk%3D
    • Lutz TA. The role of amylin in the control of energy homeostasis. Am J Physiol Regul Integr Comp Physiol. 2010;298(6):R1475-84.
    • (2010) Am J Physiol Regul Integr Comp Physiol , vol.298 , Issue.6
    • Lutz, T.A.1
  • 48
    • 0025004669 scopus 로고
    • Effects of amylin on glucose metabolism and glycogenolysis in vivo and in vitro
    • 2399978 1:CAS:528:DyaK3cXmtVGisbc%3D
    • Young DA, Deems RO, Deacon RW, McIntosh RH, Foley JE. Effects of amylin on glucose metabolism and glycogenolysis in vivo and in vitro. Am J Physiol. 1990;259(3 Pt 1):E457-61.
    • (1990) Am J Physiol , vol.259 , Issue.3 PART 1
    • Young, D.A.1    Deems, R.O.2    Deacon, R.W.3    McIntosh, R.H.4    Foley, J.E.5
  • 49
    • 64849096689 scopus 로고    scopus 로고
    • Residual structure in islet amyloid polypeptide mediates its interactions with soluble insulin
    • 19146426 10.1021/bi802097b 1:CAS:528:DC%2BD1MXisFelsrg%3D
    • Wei L, Jiang P, Yau YH, Summer H, Shochat SG, Mu Y, et al. Residual structure in islet amyloid polypeptide mediates its interactions with soluble insulin. Biochemistry. 2009;48(11):2368-76.
    • (2009) Biochemistry , vol.48 , Issue.11 , pp. 2368-2376
    • Wei, L.1    Jiang, P.2    Yau, Y.H.3    Summer, H.4    Shochat, S.G.5    Mu, Y.6
  • 50
    • 77955321505 scopus 로고    scopus 로고
    • PH-Dependent interactions of human islet amyloid polypeptide segments with insulin studied by replica exchange molecular dynamics simulations
    • 20684641 10.1021/jp101811u 1:CAS:528:DC%2BC3cXptFOqurY%3D
    • Jiang P, Wei L, Pervushin K, Mu Y. pH-Dependent interactions of human islet amyloid polypeptide segments with insulin studied by replica exchange molecular dynamics simulations. J Phys Chem B. 2010;114(31):10176-83.
    • (2010) J Phys Chem B , vol.114 , Issue.31 , pp. 10176-10183
    • Jiang, P.1    Wei, L.2    Pervushin, K.3    Mu, Y.4
  • 52
    • 0024539595 scopus 로고
    • Synthesis of palmitoyl derivatives of insulin and their biological activities
    • 2668914 10.1023/A:1015992828666 1:CAS:528:DyaL1MXhsl2gt7k%3D
    • Hashimoto M, Takada K, Kiso Y, Muranishi S. Synthesis of palmitoyl derivatives of insulin and their biological activities. Pharm Res. 1989;6(2):171-6.
    • (1989) Pharm Res , vol.6 , Issue.2 , pp. 171-176
    • Hashimoto, M.1    Takada, K.2    Kiso, Y.3    Muranishi, S.4
  • 54
    • 9044226136 scopus 로고    scopus 로고
    • Soluble, fatty acid acylated insulins bind to albumin and show protracted action in pigs
    • 8721773 10.1007/BF00418343 1:CAS:528:DyaK28XitlaisLw%3D
    • Markussen J, Havelund S, Kurtzhals P, Andersen AS, Halstrom J, Hasselager E, et al. Soluble, fatty acid acylated insulins bind to albumin and show protracted action in pigs. Diabetologia. 1996;39(3):281-8.
    • (1996) Diabetologia , vol.39 , Issue.3 , pp. 281-288
    • Markussen, J.1    Havelund, S.2    Kurtzhals, P.3    Andersen, A.S.4    Halstrom, J.5    Hasselager, E.6
  • 55
    • 22644432886 scopus 로고    scopus 로고
    • Synthesis and evaluation of insulin-human serum albumin conjugates
    • 16029043 10.1021/bc050102k 1:CAS:528:DC%2BD2MXlsV2rtrc%3D
    • Thibaudeau K, Leger R, Huang XC, Robitaille M, Quraishi O, Soucy C, et al. Synthesis and evaluation of insulin-human serum albumin conjugates. Bioconjugate Chemistry. 2005;16(4):1000-8.
    • (2005) Bioconjugate Chemistry , vol.16 , Issue.4 , pp. 1000-1008
    • Thibaudeau, K.1    Leger, R.2    Huang, X.C.3    Robitaille, M.4    Quraishi, O.5    Soucy, C.6
  • 58
    • 33746910579 scopus 로고    scopus 로고
    • Time-action profile of insulin detemir and NPH insulin in patients with type 2 diabetes from different ethnic groups
    • 16918592 10.1111/j.1463-1326.2006.00643.x 1:CAS:528:DC%2BD28XhtFSis7rP
    • Hompesch M, Troupin B, Heise T, Elbroend B, Endahl L, Haahr H, et al. Time-action profile of insulin detemir and NPH insulin in patients with type 2 diabetes from different ethnic groups. Diabetes Obes Metab. 2006;8(5):568-73.
    • (2006) Diabetes Obes Metab , vol.8 , Issue.5 , pp. 568-573
    • Hompesch, M.1    Troupin, B.2    Heise, T.3    Elbroend, B.4    Endahl, L.5    Haahr, H.6
  • 59
    • 0034609586 scopus 로고    scopus 로고
    • Identification of the major positional isomer of pegylated interferon alpha-2b
    • 10978146 10.1021/bi000617t 1:CAS:528:DC%2BD3cXlsVShurY%3D
    • Wang YS, Youngster S, Bausch J, Zhang R, McNemar C, Wyss DF. Identification of the major positional isomer of pegylated interferon alpha-2b. Biochemistry. 2000;39(35):10634-40.
    • (2000) Biochemistry , vol.39 , Issue.35 , pp. 10634-10640
    • Wang, Y.S.1    Youngster, S.2    Bausch, J.3    Zhang, R.4    McNemar, C.5    Wyss, D.F.6
  • 60
    • 33645282778 scopus 로고    scopus 로고
    • Recovery and purification of highly aggregation-prone disulfide-containing peptides: Application to islet amyloid polypeptide
    • 16406209 10.1016/j.ab.2005.11.029 1:CAS:528:DC%2BD28XivVaqu7Y%3D
    • Abedini A, Singh G, Raleigh DP. Recovery and purification of highly aggregation-prone disulfide-containing peptides: application to islet amyloid polypeptide. Analyt Biochem. 2006;351(2):181-6.
    • (2006) Analyt Biochem , vol.351 , Issue.2 , pp. 181-186
    • Abedini, A.1    Singh, G.2    Raleigh, D.P.3
  • 61
    • 84870679109 scopus 로고    scopus 로고
    • Fibril formation and toxicity of the non-amyloidogenic rat amylin peptide
    • 22854213 10.1016/j.micron.2012.07.001 1:CAS:528:DC%2BC38XhvVajt7fL
    • Milton NG, Harris JR. Fibril formation and toxicity of the non-amyloidogenic rat amylin peptide. Micron. 2013;44:246-53.
    • (2013) Micron , vol.44 , pp. 246-253
    • Milton, N.G.1    Harris, J.R.2
  • 62
    • 0033579545 scopus 로고    scopus 로고
    • Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin
    • 10600392 10.1006/jmbi.1999.3286 1:CAS:528:DyaK1MXnvFaru7Y%3D
    • Nilsson MR, Raleigh DP. Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin. J Mol Biol. 1999;294(5):1375-85.
    • (1999) J Mol Biol , vol.294 , Issue.5 , pp. 1375-1385
    • Nilsson, M.R.1    Raleigh, D.P.2
  • 63
    • 0035161120 scopus 로고    scopus 로고
    • Synthesis and purification of amyloidogenic peptides
    • 11141308 10.1006/abio.2000.4887 1:CAS:528:DC%2BD3MXhtF2ktQ%3D%3D
    • Nilsson MR, Nguyen LL, Raleigh DP. Synthesis and purification of amyloidogenic peptides. Analyt Biochem. 2001;288(1):76-82.
    • (2001) Analyt Biochem , vol.288 , Issue.1 , pp. 76-82
    • Nilsson, M.R.1    Nguyen, L.L.2    Raleigh, D.P.3
  • 64
    • 33645210308 scopus 로고    scopus 로고
    • Clinical studies
    • 16492555 10.1016/S1054-3589(05)52018-0 1:CAS:528:DC%2BD1cXitlahsL8%3D
    • Young A. Clinical studies. Adv Pharmacol. 2005;52:289-320.
    • (2005) Adv Pharmacol , vol.52 , pp. 289-320
    • Young, A.1
  • 65
    • 66449087200 scopus 로고    scopus 로고
    • Dynamic alpha-helix structure of micelle-bound human amylin
    • 19244249 10.1074/jbc.M809085200 1:CAS:528:DC%2BD1MXltVCmtLY%3D
    • Patil SM, Xu S, Sheftic SR, Alexandrescu AT. Dynamic alpha-helix structure of micelle-bound human amylin. J Biol Chem. 2009;284(18):11982-91.
    • (2009) J Biol Chem , vol.284 , Issue.18 , pp. 11982-11991
    • Patil, S.M.1    Xu, S.2    Sheftic, S.R.3    Alexandrescu, A.T.4
  • 66
    • 67650533782 scopus 로고    scopus 로고
    • Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy
    • 19456151 10.1021/ja9010095 1:CAS:528:DC%2BD1MXmtFKitb0%3D
    • Nanga RP, Brender JR, Xu J, Hartman K, Subramanian V, Ramamoorthy A. Three-dimensional structure and orientation of rat islet amyloid polypeptide protein in a membrane environment by solution NMR spectroscopy. J Am Chem Soc. 2009;131(23):8252-61.
    • (2009) J Am Chem Soc , vol.131 , Issue.23 , pp. 8252-8261
    • Nanga, R.P.1    Brender, J.R.2    Xu, J.3    Hartman, K.4    Subramanian, V.5    Ramamoorthy, A.6
  • 67
    • 55949114507 scopus 로고    scopus 로고
    • Peptide aggregation in finite systems
    • 18621830 10.1529/biophysj.108.136226 1:CAS:528:DC%2BD1cXht1Srs7nJ
    • Singh G, Brovchenko I, Oleinikova A, Winter R. Peptide aggregation in finite systems. Biophys J. 2008;95(7):3208-21.
    • (2008) Biophys J , vol.95 , Issue.7 , pp. 3208-3221
    • Singh, G.1    Brovchenko, I.2    Oleinikova, A.3    Winter, R.4
  • 68
    • 0344687319 scopus 로고    scopus 로고
    • The mechanism of insulin action on islet amyloid polypeptide fiber formation
    • 14659752 10.1016/j.jmb.2003.10.045 1:CAS:528:DC%2BD3sXpsVSgurg%3D
    • Larson JL, Miranker AD. The mechanism of insulin action on islet amyloid polypeptide fiber formation. J Mol Biol. 2004;335(1):221-31.
    • (2004) J Mol Biol , vol.335 , Issue.1 , pp. 221-231
    • Larson, J.L.1    Miranker, A.D.2
  • 69
    • 52949132646 scopus 로고    scopus 로고
    • Interaction of membrane-bound islet amyloid polypeptide with soluble and crystalline insulin
    • 18765820 10.1110/ps.036350.108 1:CAS:528:DC%2BD1cXht1Cit7vP
    • Knight JD, Williamson JA, Miranker AD. Interaction of membrane-bound islet amyloid polypeptide with soluble and crystalline insulin. Protein Sci. 2008;17(10):1850-6.
    • (2008) Protein Sci , vol.17 , Issue.10 , pp. 1850-1856
    • Knight, J.D.1    Williamson, J.A.2    Miranker, A.D.3
  • 70
    • 67650022868 scopus 로고    scopus 로고
    • Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process
    • 19475663 10.1002/pro.145 1:CAS:528:DC%2BD1MXnvVChsLs%3D
    • Wiltzius JJ, Sievers SA, Sawaya MR, Eisenberg D. Atomic structures of IAPP (amylin) fusions suggest a mechanism for fibrillation and the role of insulin in the process. Protein Sci. 2009;18(7):1521-30.
    • (2009) Protein Sci , vol.18 , Issue.7 , pp. 1521-1530
    • Wiltzius, J.J.1    Sievers, S.A.2    Sawaya, M.R.3    Eisenberg, D.4
  • 71
    • 51849084313 scopus 로고    scopus 로고
    • Amylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state
    • 18710262 10.1021/bi800828u 1:CAS:528:DC%2BD1cXpvFyktrc%3D
    • Yonemoto IT, Kroon GJ, Dyson HJ, Balch WE, Kelly JW. Amylin proprotein processing generates progressively more amyloidogenic peptides that initially sample the helical state. Biochemistry. 2008;47(37):9900-10.
    • (2008) Biochemistry , vol.47 , Issue.37 , pp. 9900-9910
    • Yonemoto, I.T.1    Kroon, G.J.2    Dyson, H.J.3    Balch, W.E.4    Kelly, J.W.5
  • 72
    • 77749320957 scopus 로고    scopus 로고
    • Inhibition of IAPP and IAPP(20-29) fibrillation by polymeric nanoparticles
    • 20017535 10.1021/la902980d 1:CAS:528:DC%2BD1MXhsFOisrvE
    • Cabaleiro-Lago C, Lynch I, Dawson KA, Linse S. Inhibition of IAPP and IAPP(20-29) fibrillation by polymeric nanoparticles. Langmuir. 2010;26(5):3453-61.
    • (2010) Langmuir , vol.26 , Issue.5 , pp. 3453-3461
    • Cabaleiro-Lago, C.1    Lynch, I.2    Dawson, K.A.3    Linse, S.4
  • 73
    • 0037120160 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides
    • 12298020 10.1002/1521-3765(20020916)8:18<4285: AID-CHEM4285>3.0. CO;2-0 1:CAS:528:DC%2BD38XnsFentbc%3D
    • Rijkers DT, Hoppener JW, Posthuma G, Lips CJ, Liskamp RM. Inhibition of amyloid fibril formation of human amylin by N-alkylated amino acid and alpha-hydroxy acid residue containing peptides. Chemistry. 2002;8(18):4285-91.
    • (2002) Chemistry , vol.8 , Issue.18 , pp. 4285-4291
    • Rijkers, D.T.1    Hoppener, J.W.2    Posthuma, G.3    Lips, C.J.4    Liskamp, R.M.5
  • 74
    • 75649097839 scopus 로고    scopus 로고
    • Aggregation properties of the peptide fragments derived from the 17-29 region of the human and rat IAPP: A comparative study with two PEG-conjugated variants of the human sequence
    • 20039665 10.1021/jp908436s 1:CAS:528:DC%2BD1MXhs1alurzI
    • Mazzaglia A, Micali N, Scolaro LM, Attanasio F, Magri A, Pappalardo G, et al. Aggregation properties of the peptide fragments derived from the 17-29 region of the human and rat IAPP: a comparative study with two PEG-conjugated variants of the human sequence. J Phys Chem B. 2010;114(2):705-13.
    • (2010) J Phys Chem B , vol.114 , Issue.2 , pp. 705-713
    • Mazzaglia, A.1    Micali, N.2    Scolaro, L.M.3    Attanasio, F.4    Magri, A.5    Pappalardo, G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.