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Volumn 5, Issue , 2015, Pages

Inhibition of insulin fibrillation by osmolytes: Mechanistic Insights

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; BETAINE; INSULIN; PROLINE; PROTEIN BINDING; SORBITOL;

EID: 84948807964     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep17599     Document Type: Article
Times cited : (78)

References (124)
  • 1
    • 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.75, 333-366 (2006).
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 2
    • 46749117136 scopus 로고    scopus 로고
    • Molecular and cellular aspects of protein misfolding and disease
    • Herczenik, E. & Gebbink, M. F. Molecular and cellular aspects of protein misfolding and disease. FASEB J. 22, 2115-2133 (2008).
    • (2008) FASEB J. , vol.22 , pp. 2115-2133
    • Herczenik, E.1    Gebbink, M.F.2
  • 3
    • 0031592945 scopus 로고    scopus 로고
    • The common core structure of amyloid fibrils by synchrotron X-ray diffraction
    • Sunde, M. et al. The common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Bio. 273, 729-739 (1997).
    • (1997) J. Mol. Bio. , vol.273 , pp. 729-739
    • Sunde, M.1
  • 5
    • 70349503591 scopus 로고    scopus 로고
    • Biophysics of Parkinsons disease: Structure and aggregation of alpha-synuclein
    • Uversky, V. N. & Eliezer, D. Biophysics of Parkinsons disease: structure and aggregation of alpha-synuclein. Curr. Prot. Pept. Sci. 5, 483-499 (2009).
    • (2009) Curr. Prot. Pept. Sci. , vol.5 , pp. 483-499
    • Uversky, V.N.1    Eliezer, D.2
  • 6
    • 0029994633 scopus 로고    scopus 로고
    • Arrest of beta-amyloid fibril formation by apenta peptide ligand
    • Tjernberg, L. O. et al. Arrest of beta-amyloid fibril formation by apenta peptide ligand. J. Biol. Chem. 271, 8545-8548 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 8545-8548
    • Tjernberg, L.O.1
  • 7
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway, K. A., Rochet, J. C., Bieganski, R. M. & Lansbury, P. T. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 294, 1346-1349 (2001).
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury, P.T.4
  • 8
    • 0034987618 scopus 로고    scopus 로고
    • Interpreting the effects of small uncharged solutes on protein- folding equilibria
    • Davis-Searles, P. R. et al. Interpreting the effects of small uncharged solutes on protein- folding equilibria. Ann. Rev. Biophys. Biomol. Struct. 30, 271-306 (2001).
    • (2001) Ann. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 271-306
    • Davis-Searles, P.R.1
  • 9
    • 0034035899 scopus 로고    scopus 로고
    • Probing protein- sugar interactions
    • Ebel, C., Eisenberg, H. & Ghirlando, R. Probing protein- sugar interactions. Biophys J. 78, 385-393 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 385-393
    • Ebel, C.1    Eisenberg, H.2    Ghirlando, R.3
  • 10
    • 4644335636 scopus 로고    scopus 로고
    • Reduced protein adsorption at solid interfaces by sugar excipients
    • Wendorf, J. R., Radke, C. J. & Blanch, H. W. Reduced protein adsorption at solid interfaces by sugar excipients. Biotechnol. Bioeng. 87, 565-573 (2004).
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 565-573
    • Wendorf, J.R.1    Radke, C.J.2    Blanch, H.W.3
  • 11
    • 0035237232 scopus 로고    scopus 로고
    • Protein stabilization by naturally occurring osmolytes
    • Bolen, D. W. Protein stabilization by naturally occurring osmolytes. Methods Mol. Biol. 168, 17-36 (2001).
    • (2001) Methods Mol. Biol. , vol.168 , pp. 17-36
    • Bolen, D.W.1
  • 12
    • 33947730947 scopus 로고    scopus 로고
    • An analysis of the molecular origin of osmolytes-dependent protein stability
    • Rosgen, J., Pettitt, B. M. & Bolen, D. W. An analysis of the molecular origin of osmolytes-dependent protein stability. Prot. Sci.16, 733-743 (2007).
    • (2007) Prot. Sci. , vol.16 , pp. 733-743
    • Rosgen, J.1    Pettitt, B.M.2    Bolen, D.W.3
  • 13
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff, S. N. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 51, 355-432 (1998).
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 14
    • 0032564420 scopus 로고    scopus 로고
    • A transient expansion of the native state precedes aggregation of recombinant human interferon-c
    • Kendrick, B. S., Carpenter, J. F., Cleland, J. L. & Randolph, T. W. A transient expansion of the native state precedes aggregation of recombinant human interferon-c. Proc. Natl. Acad. Sci. USA. 95, 14142-14146 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA. , vol.95 , pp. 14142-14146
    • Kendrick, B.S.1    Carpenter, J.F.2    Cleland, J.L.3    Randolph, T.W.4
  • 15
    • 84885083599 scopus 로고    scopus 로고
    • Effect of osmolytes on the fibrillation of Hyp F-N
    • Bhavsar, R. D., Prasad, S. & Roy, I. Effect of osmolytes on the fibrillation of Hyp F-N. Biochimie, 95, 2190-2193 (2013).
    • (2013) Biochimie , vol.95 , pp. 2190-2193
    • Bhavsar, R.D.1    Prasad, S.2    Roy, I.3
  • 16
    • 34547590372 scopus 로고    scopus 로고
    • Effects of osmolytes on hexokinase kinetics combined with macromolecular crowding: Test of the osmolyte compatibility hypothesis towards crowded systems
    • Olsen,S. N., Ramlov, H. & Westh, P. Effects of osmolytes on hexokinase kinetics combined with macromolecular crowding: Test of the osmolyte compatibility hypothesis towards crowded systems. Comp. Biochem. Phys. A: Mol. Integr. Physiol. 148, 339-345 (2007).
    • (2007) Comp. Biochem. Phys. A: Mol. Integr. Physiol. , vol.148 , pp. 339-345
    • Olsens, N.1    Ramlov, H.2    Westh, P.3
  • 17
    • 84904470984 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation of hen egg white lysozyme by trimethylamine N-oxide at low pH
    • Wawer, J. et al. Inhibition of amyloid fibril formation of hen egg white lysozyme by trimethylamine N-oxide at low pH. Int. J. Biol. Macromol. 70, 214-221(2014).
    • (2014) Int. J. Biol. Macromol. , vol.70 , pp. 214-221
    • Wawer, J.1
  • 19
    • 1842850631 scopus 로고    scopus 로고
    • Inhibition of insulin amyloid formation by small stress molecules
    • Arora, A., Hab, C. & Park, C. B. Inhibition of insulin amyloid formation by small stress molecules. FEBS Lett. 564, 121-125 (2004).
    • (2004) FEBS Lett. , vol.564 , pp. 121-125
    • Arora, A.1    Hab, C.2    Park, C.B.3
  • 20
    • 0026598013 scopus 로고
    • Enzyme stabilization by ectoine-type compatible solutes: Protection against heating, freezing and drying
    • Lippert, K. & Galinski, E. A. Enzyme stabilization by ectoine-type compatible solutes: protection against heating, freezing and drying. Appl. Micro. boil. Biotechnol. 37, 61-65(1992).
    • (1992) Appl. Micro. Boil. Biotechnol. , vol.37 , pp. 61-65
    • Lippert, K.1    Galinski, E.A.2
  • 21
    • 0039801358 scopus 로고    scopus 로고
    • Protection of a model enzyme (lactate dehydrogenase) against heat, urea and freeze-thaw treatment by compatible solute additive
    • Goller, K. & Galinski, E. A. Protection of a model enzyme (lactate dehydrogenase) against heat, urea and freeze-thaw treatment by compatible solute additive. J. Mol. Catal. B Enzym. 7, 37-45 (1999).
    • (1999) J. Mol. Catal. B Enzym. , vol.7 , pp. 37-45
    • Goller, K.1    Galinski, E.A.2
  • 22
    • 0038374325 scopus 로고    scopus 로고
    • Why is trehalose an exceptional protein stabilizer?
    • Kaushik, J. K. & Bhat, R. Why is trehalose an exceptional protein stabilizer? J. Biol. Chem.278, 26458-26465 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 26458-26465
    • Kaushik, J.K.1    Bhat, R.2
  • 23
    • 0035941144 scopus 로고    scopus 로고
    • Citrulline, a novel compatible solute in drought- tolerant wild watermelon leaves, is an efficient hydroxyl radical scavenger
    • Akashi, K., Miyake, C. & Yokota, A. Citrulline, a novel compatible solute in drought- tolerant wild watermelon leaves, is an efficient hydroxyl radical scavenger. FEBS Lett. 508, 438-442 (2001).
    • (2001) FEBS Lett. , vol.508 , pp. 438-442
    • Akashi, K.1    Miyake, C.2    Yokota, A.3
  • 25
    • 24044449002 scopus 로고    scopus 로고
    • Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimers β-amyloid
    • Kanapathipillaia, M., Lentzenb, G., Sierksa, M. & Park, C. B. Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimers β-amyloid. FEBS Lett. 579, 4775-4780 (2005).
    • (2005) FEBS Lett. , vol.579 , pp. 4775-4780
    • Kanapathipillaia, M.1    Lentzenb, G.2    Sierksa, M.3    Park, C.B.4
  • 26
    • 0028278931 scopus 로고
    • The insulin receptor: Structure, function and signalling
    • Lee, J. & Pilch, P. F. The insulin receptor: structure, function and signalling. Am. J. Physiol. 266, C319-C334 (1994).
    • (1994) Am. J. Physiol. , vol.266 , pp. C319-C334
    • Lee, J.1    Pilch, P.F.2
  • 27
    • 0015517217 scopus 로고
    • Cross-β protein structures.I. Insulin fibrils
    • Burke, M. J. & Rougvie, M. A. Cross-β protein structures.I. Insulin fibrils. Biochemistry 11, 2435-2439 (1972).
    • (1972) Biochemistry , vol.11 , pp. 2435-2439
    • Burke, M.J.1    Rougvie, M.A.2
  • 28
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • Nielsen, L. et al. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 40, 6036-6046 (2001).
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1
  • 29
    • 0033869084 scopus 로고    scopus 로고
    • Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
    • Nettleton, E. J. et al. Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Biophys. J. 79, 1053-1065 (2000).
    • (2000) Biophys. J. , vol.79 , pp. 1053-1065
    • Nettleton, E.J.1
  • 30
    • 0032054714 scopus 로고    scopus 로고
    • The role of assembly in insulins biosynthesis
    • Dodson, G. G. & Steiner, D. The role of assembly in insulins biosynthesis. Curr. Opin. Struct. Biol. 8, 189-194 (1998).
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 189-194
    • Dodson, G.G.1    Steiner, D.2
  • 31
    • 67549142772 scopus 로고    scopus 로고
    • Localized insulin-derived amyloidosis in patients with diabetes mellitus: A case report
    • Yumlu, S., Barany, R., Eriksson, M. & Rocken, C. Localized insulin-derived amyloidosis in patients with diabetes mellitus: a case report. Hum. Pathol. 40, 1655-1660 (2009).
    • (2009) Hum. Pathol. , vol.40 , pp. 1655-1660
    • Yumlu, S.1    Barany, R.2    Eriksson, M.3    Rocken, C.4
  • 32
    • 77749333254 scopus 로고    scopus 로고
    • Localized amyloidosis at the site of repeated insulin injection in a diabetic patient
    • Shikama, Y. et al. Localized amyloidosis at the site of repeated insulin injection in a diabetic patient. Intern. Med. 49, 397-401 (2010).
    • (2010) Intern. Med. , vol.49 , pp. 397-401
    • Shikama, Y.1
  • 33
    • 0000685268 scopus 로고
    • Studies of the Nucleation and Growth Reactions of Selected Types of Insulin Fibrils
    • Waugh, D. F., Wilhelmson, D. F., Commerford, S. L. & Sackler, M. L. Studies of the Nucleation and Growth Reactions of Selected Types of Insulin Fibrils. J. Am. Chem. Soc. 75, 2592-2600 (1953).
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 2592-2600
    • Waugh, D.F.1    Wilhelmson, D.F.2    Commerford, S.L.3    Sackler, M.L.4
  • 34
    • 30044446633 scopus 로고    scopus 로고
    • Early events in the fibrillation of monomeric insulin
    • Ahmad, A., Uversky, V. N., Hong, D. & Fink, A. L. Early Events in the Fibrillation of Monomeric Insulin. J. Biol. Chem. 280, 42669-42675 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 42669-42675
    • Ahmad, A.1    Uversky, V.N.2    Hong, D.3    Fink, A.L.4
  • 35
    • 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.75, 333-366 (2006).
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 36
    • 46749117136 scopus 로고    scopus 로고
    • Molecular and cellular aspects of protein misfolding and disease
    • Herczenik, E. & Gebbink, M. F. Molecular and cellular aspects of protein misfolding and disease. FASEB J. 22, 2115-2133 (2008).
    • (2008) FASEB J. , vol.22 , pp. 2115-2133
    • Herczenik, E.1    Gebbink, M.F.2
  • 37
    • 0031592945 scopus 로고    scopus 로고
    • The common core structure of amyloid fibrils by synchrotron X-ray diffraction
    • Sunde, M. et al. The common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Bio. 273, 729-739 (1997).
    • (1997) J. Mol. Bio. , vol.273 , pp. 729-739
    • Sunde, M.1
  • 39
    • 70349503591 scopus 로고    scopus 로고
    • Biophysics of Parkinsons disease: Structure and aggregation of alpha-synuclein
    • Uversky, V. N. & Eliezer, D. Biophysics of Parkinsons disease: structure and aggregation of alpha-synuclein. Curr. Prot. Pept. Sci. 5, 483-499 (2009).
    • (2009) Curr. Prot. Pept. Sci. , vol.5 , pp. 483-499
    • Uversky, V.N.1    Eliezer, D.2
  • 40
    • 0029994633 scopus 로고    scopus 로고
    • Arrest of beta-amyloid fibril formation by apentapeptide ligand
    • Tjernberg, L. O. et al. Arrest of beta-amyloid fibril formation by apentapeptide ligand. J. Biol. Chem. 271, 8545-8548 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 8545-8548
    • Tjernberg, L.O.1
  • 41
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway, K. A., Rochet, J. C., Bieganski, R. M. & Lansbury, P. T. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 294, 1346-1349 (2001).
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury, P.T.4
  • 42
    • 0034987618 scopus 로고    scopus 로고
    • Interpreting the effects of small uncharged solutes on protein- folding equilibria
    • Davis-Searles, P. R. et al. Interpreting the effects of small uncharged solutes on protein- folding equilibria. Ann. Rev. Biophys. Biomol. Struct. 30, 271-306 (2001).
    • (2001) Ann. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 271-306
    • Davis-Searles, P.R.1
  • 43
    • 0034035899 scopus 로고    scopus 로고
    • Probing protein- sugar interactions
    • Ebel, C., Eisenberg, H. & Ghirlando, R. Probing protein- sugar interactions. Biophys J. 78, 385-393 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 385-393
    • Ebel, C.1    Eisenberg, H.2    Ghirlando, R.3
  • 44
    • 4644335636 scopus 로고    scopus 로고
    • Reduced protein adsorption at solid interfaces by sugar excipients
    • Wendorf, J. R., Radke, C. J. & Blanch, H. W. Reduced protein adsorption at solid interfaces by sugar excipients. Biotechnol. Bioeng. 87, 565-573 (2004).
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 565-573
    • Wendorf, J.R.1    Radke, C.J.2    Blanch, H.W.3
  • 45
    • 0035237232 scopus 로고    scopus 로고
    • Protein stabilization by naturally occurring osmolytes
    • Bolen, D. W. Protein stabilization by naturally occurring osmolytes. Methods Mol. Biol. 168, 17-36 (2001).
    • (2001) Methods Mol. Biol. , vol.168 , pp. 17-36
    • Bolen, D.W.1
  • 46
    • 33947730947 scopus 로고    scopus 로고
    • An analysis of the molecular origin of osmolytes-dependent protein stability
    • Rosgen, J., Pettitt, B. M. & Bolen, D. W. An analysis of the molecular origin of osmolytes-dependent protein stability. Prot. Sci.16, 733-743 (2007).
    • (2007) Prot. Sci. , vol.16 , pp. 733-743
    • Rosgen, J.1    Pettitt, B.M.2    Bolen, D.W.3
  • 47
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff, S. N. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 51, 355-432 (1998).
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 48
    • 0032564420 scopus 로고    scopus 로고
    • A transient expansion of the native state precedes aggregation of recombinant human interferon-c
    • Kendrick, B. S., Carpenter, J. F., Cleland, J. L. & Randolph, T. W. A transient expansion of the native state precedes aggregation of recombinant human interferon-c. Proc. Natl. Acad. Sci. USA. 95, 14142-14146 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA. , vol.95 , pp. 14142-14146
    • Kendrick, B.S.1    Carpenter, J.F.2    Cleland, J.L.3    Randolph, T.W.4
  • 49
    • 84885083599 scopus 로고    scopus 로고
    • Effect of osmolytes on the fibrillation of HypF-N
    • Bhavsar, R. D., Prasad, S. & Roy, I. Effect of osmolytes on the fibrillation of HypF-N. Biochimie, 95, 2190-2193 (2013).
    • (2013) Biochimie , vol.95 , pp. 2190-2193
    • Bhavsar, R.D.1    Prasad, S.2    Roy, I.3
  • 50
    • 34547590372 scopus 로고    scopus 로고
    • Effects of osmolytes on hexokinase kinetics combined with macromolecular crowding: Test of the osmolyte compatibility hypothesis towards crowded systems
    • Olsen, S. N., Ramlov, H. & Westh, P. Effects of osmolytes on hexokinase kinetics combined with macromolecular crowding: Test of the osmolyte compatibility hypothesis towards crowded systems. Comp. Biochem. Phys. A: Mol. Integr. Physiol. 148, 339-345 (2007).
    • (2007) Comp. Biochem. Phys. A: Mol. Integr. Physiol. , vol.148 , pp. 339-345
    • Olsen, S.N.1    Ramlov, H.2    Westh, P.3
  • 51
    • 84904470984 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation of hen egg white lysozyme by trimethylamine N-oxide at low pH
    • Wawer, J. et al. Inhibition of amyloid fibril formation of hen egg white lysozyme by trimethylamine N-oxide at low pH. Int. J. Biol. Macromol. 70, 214-221(2014).
    • (2014) Int. J. Biol. Macromol. , vol.70 , pp. 214-221
    • Wawer, J.1
  • 53
    • 1842850631 scopus 로고    scopus 로고
    • Inhibition of insulin amyloid formation by small stress molecules
    • Arora, A., Hab, C. & Park, C. B. Inhibition of insulin amyloid formation by small stress molecules. FEBS Lett. 564, 121-125 (2004).
    • (2004) FEBS Lett. , vol.564 , pp. 121-125
    • Arora, A.1    Hab, C.2    Park, C.B.3
  • 54
    • 0026598013 scopus 로고
    • Enzyme stabilization by ectoine-type compatible solutes: Protection against heating, freezing and drying
    • Lippert, K. & Galinski, E. A. Enzyme stabilization by ectoine-type compatible solutes: protection against heating, freezing and drying. Appl. Micro. boil. Biotechnol. 37, 61-65(1992).
    • (1992) Appl. Micro. Boil. Biotechnol. , vol.37 , pp. 61-65
    • Lippert, K.1    Galinski, E.A.2
  • 55
    • 0039801358 scopus 로고    scopus 로고
    • Protection of a model enzyme (lactate dehydrogenase) against heat, urea and freeze-thaw treatment by compatible solute additive
    • Goller, K. & Galinski, E. A. Protection of a model enzyme (lactate dehydrogenase) against heat, urea and freeze-thaw treatment by compatible solute additive. J. Mol. Catal. B Enzym. 7, 37-45 (1999).
    • (1999) J. Mol. Catal. B Enzym. , vol.7 , pp. 37-45
    • Goller, K.1    Galinski, E.A.2
  • 56
    • 0038374325 scopus 로고    scopus 로고
    • Why is trehalose an exceptional protein stabilizer?
    • Kaushik, J. K. & Bhat, R. Why is trehalose an exceptional protein stabilizer? J. Biol. Chem.278, 26458-26465 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 26458-26465
    • Kaushik, J.K.1    Bhat, R.2
  • 57
    • 0035941144 scopus 로고    scopus 로고
    • Citrulline, a novel compatible solute in drought- tolerant wild watermelon leaves, is an efficient hydroxyl radical scavenger
    • Akashi, K., Miyake, C. & Yokota, A. Citrulline, a novel compatible solute in drought- tolerant wild watermelon leaves, is an efficient hydroxyl radical scavenger. FEBS Lett. 508, 438-442 (2001).
    • (2001) FEBS Lett. , vol.508 , pp. 438-442
    • Akashi, K.1    Miyake, C.2    Yokota, A.3
  • 59
    • 24044449002 scopus 로고    scopus 로고
    • Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimers β-amyloid
    • Kanapathipillaia, M., Lentzenb, G., Sierksa, M. & Park, C. B. Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimers β-amyloid. FEBS Lett. 579, 4775-4780 (2005).
    • (2005) FEBS Lett. , vol.579 , pp. 4775-4780
    • Kanapathipillaia, M.1    Lentzenb, G.2    Sierksa, M.3    Park, C.B.4
  • 60
    • 0028278931 scopus 로고
    • The insulin receptor: Structure, function and signalling
    • Lee, J. & Pilch, P. F. The insulin receptor: structure, function and signalling. Am. J. Physiol. 266, C319-C334 (1994).
    • (1994) Am. J. Physiol. , vol.266 , pp. C319-C334
    • Lee, J.1    Pilch, P.F.2
  • 61
    • 0015517217 scopus 로고
    • Cross-β protein structures.I. Insulin fibrils
    • Burke, M. J. & Rougvie, M. A. Cross-β protein structures.I. Insulin fibrils. Biochemistry 11, 2435-2439 (1972).
    • (1972) Biochemistry , vol.11 , pp. 2435-2439
    • Burke, M.J.1    Rougvie, M.A.2
  • 62
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • Nielsen, L. et al. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 40, 6036-6046 (2001).
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1
  • 63
    • 0033869084 scopus 로고    scopus 로고
    • Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
    • Nettleton, E. J. et al. Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Biophys. J. 79, 1053-1065 (2000).
    • (2000) Biophys. J. , vol.79 , pp. 1053-1065
    • Nettleton, E.J.1
  • 64
    • 0032054714 scopus 로고    scopus 로고
    • The role of assembly in insulins biosynthesis
    • Dodson, G. G. & Steiner, D. The role of assembly in insulins biosynthesis. Curr. Opin. Struct. Biol. 8, 189-194 (1998).
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 189-194
    • Dodson, G.G.1    Steiner, D.2
  • 65
    • 67549142772 scopus 로고    scopus 로고
    • Localized insulin-derived amyloidosis in patients with diabetes mellitus: A case report
    • Yumlu, S., Barany, R., Eriksson, M. & Rocken, C. Localized insulin-derived amyloidosis in patients with diabetes mellitus: a case report. Hum. Pathol. 40, 1655-1660 (2009).
    • (2009) Hum. Pathol. , vol.40 , pp. 1655-1660
    • Yumlu, S.1    Barany, R.2    Eriksson, M.3    Rocken, C.4
  • 66
    • 77749333254 scopus 로고    scopus 로고
    • Localized amyloidosis at the site of repeated insulin injection in a diabetic patient
    • Shikama, Y. et al. Localized amyloidosis at the site of repeated insulin injection in a diabetic patient. Intern. Med. 49, 397-401 (2010).
    • (2010) Intern. Med. , vol.49 , pp. 397-401
    • Shikama, Y.1
  • 67
    • 0000685268 scopus 로고
    • Studies of the Nucleation and Growth Reactions of Selected Types of Insulin Fibrils
    • Waugh, D. F., Wilhelmson, D. F., Commerford, S. L. & Sackler, M. L. Studies of the Nucleation and Growth Reactions of Selected Types of Insulin Fibrils. J. Am. Chem. Soc. 75, 2592-2600 (1953).
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 2592-2600
    • Waugh, D.F.1    Wilhelmson, D.F.2    Commerford, S.L.3    Sackler, M.L.4
  • 68
    • 30044446633 scopus 로고    scopus 로고
    • Early events in the fibrillation of monomeric insulin
    • Ahmad, A., Uversky, V. N., Hong, D. & Fink, A. L. Early Events in the Fibrillation of Monomeric Insulin. J. Biol. Chem. 280, 42669-42675 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 42669-42675
    • Ahmad, A.1    Uversky, V.N.2    Hong, D.3    Fink, A.L.4
  • 69
    • 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.75, 333-366 (2006).
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 70
    • 46749117136 scopus 로고    scopus 로고
    • Molecular and cellular aspects of protein misfolding and disease
    • Herczenik, E. & Gebbink, M. F. Molecular and cellular aspects of protein misfolding and disease. FASEB J. 22, 2115-2133 (2008).
    • (2008) FASEB J. , vol.22 , pp. 2115-2133
    • Herczenik, E.1    Gebbink, M.F.2
  • 71
    • 0031592945 scopus 로고    scopus 로고
    • The common core structure of amyloid fibrils by synchrotron X-ray diffraction
    • Sunde, M. et al. The common core structure of amyloid fibrils by synchrotron X-ray diffraction. J. Mol. Bio. 273, 729-739 (1997).
    • (1997) J. Mol. Bio. , vol.273 , pp. 729-739
    • Sunde, M.1
  • 73
    • 70349503591 scopus 로고    scopus 로고
    • Biophysics of Parkinsons disease: Structure and aggregation of alpha-synuclein
    • Uversky, V. N. & Eliezer, D. Biophysics of Parkinsons disease: structure and aggregation of alpha-synuclein. Curr. Prot. Pept. Sci. 5, 483-499 (2009).
    • (2009) Curr. Prot. Pept. Sci. , vol.5 , pp. 483-499
    • Uversky, V.N.1    Eliezer, D.2
  • 74
    • 0029994633 scopus 로고    scopus 로고
    • Arrest of beta-amyloid fibril formation by apentapeptide ligand
    • Tjernberg, L. O. et al. Arrest of beta-amyloid fibril formation by apentapeptide ligand. J. Biol. Chem. 271, 8545-8548 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 8545-8548
    • Tjernberg, L.O.1
  • 75
    • 0035834360 scopus 로고    scopus 로고
    • Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct
    • Conway, K. A., Rochet, J. C., Bieganski, R. M. & Lansbury, P. T. Kinetic stabilization of the alpha-synuclein protofibril by a dopamine-alpha-synuclein adduct. Science 294, 1346-1349 (2001).
    • (2001) Science , vol.294 , pp. 1346-1349
    • Conway, K.A.1    Rochet, J.C.2    Bieganski, R.M.3    Lansbury, P.T.4
  • 76
    • 0034987618 scopus 로고    scopus 로고
    • Interpreting the effects of small uncharged solutes on protein- folding equilibria
    • Davis-Searles, P. R. et al. Interpreting the effects of small uncharged solutes on protein- folding equilibria. Ann. Rev. Biophys. Biomol. Struct. 30, 271-306 (2001).
    • (2001) Ann. Rev. Biophys. Biomol. Struct. , vol.30 , pp. 271-306
    • Davis-Searles, P.R.1
  • 77
    • 0034035899 scopus 로고    scopus 로고
    • Probing protein- sugar interactions
    • Ebel, C., Eisenberg, H. & Ghirlando, R. Probing protein- sugar interactions. Biophys J. 78, 385-393 (2000).
    • (2000) Biophys. J. , vol.78 , pp. 385-393
    • Ebel, C.1    Eisenberg, H.2    Ghirlando, R.3
  • 78
    • 4644335636 scopus 로고    scopus 로고
    • Reduced protein adsorption at solid interfaces by sugar excipients
    • Wendorf, J. R., Radke, C. J. & Blanch, H. W. Reduced protein adsorption at solid interfaces by sugar excipients. Biotechnol. Bioeng. 87, 565-573 (2004).
    • (2004) Biotechnol. Bioeng. , vol.87 , pp. 565-573
    • Wendorf, J.R.1    Radke, C.J.2    Blanch, H.W.3
  • 79
    • 0035237232 scopus 로고    scopus 로고
    • Protein stabilization by naturally occurring osmolytes
    • Bolen, D. W. Protein stabilization by naturally occurring osmolytes. Methods Mol. Biol. 168, 17-36 (2001).
    • (2001) Methods Mol. Biol. , vol.168 , pp. 17-36
    • Bolen, D.W.1
  • 80
    • 33947730947 scopus 로고    scopus 로고
    • An analysis of the molecular origin of osmolytes-dependent protein stability
    • Rosgen, J., Pettitt, B. M. & Bolen, D. W. An analysis of the molecular origin of osmolytes-dependent protein stability. Prot. Sci.16, 733-743 (2007).
    • (2007) Prot. Sci. , vol.16 , pp. 733-743
    • Rosgen, J.1    Pettitt, B.M.2    Bolen, D.W.3
  • 81
    • 0031778590 scopus 로고    scopus 로고
    • Control of protein stability and reactions by weakly interacting cosolvents: The simplicity of the complicated
    • Timasheff, S. N. Control of protein stability and reactions by weakly interacting cosolvents: the simplicity of the complicated. Adv. Protein Chem. 51, 355-432 (1998).
    • (1998) Adv. Protein Chem. , vol.51 , pp. 355-432
    • Timasheff, S.N.1
  • 82
    • 0032564420 scopus 로고    scopus 로고
    • A transient expansion of the native state precedes aggregation of recombinant human interferon-c
    • Kendrick, B. S., Carpenter, J. F., Cleland, J. L. & Randolph, T. W. A transient expansion of the native state precedes aggregation of recombinant human interferon-c. Proc. Natl. Acad. Sci. USA. 95, 14142-14146 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 14142-14146
    • Kendrick, B.S.1    Carpenter, J.F.2    Cleland, J.L.3    Randolph, T.W.4
  • 83
    • 84885083599 scopus 로고    scopus 로고
    • Effect of osmolytes on the fibrillation of HypF-N
    • Bhavsar, R. D., Prasad, S. & Roy, I. Effect of osmolytes on the fibrillation of HypF-N. Biochimie, 95, 2190-2193 (2013).
    • (2013) Biochimie , vol.95 , pp. 2190-2193
    • Bhavsar, R.D.1    Prasad, S.2    Roy, I.3
  • 84
    • 34547590372 scopus 로고    scopus 로고
    • Effects of osmolytes on hexokinase kinetics combined with macromolecular crowding: Test of the osmolyte compatibility hypothesis towards crowded systems
    • Olsen, S. N., Ramlov, H. & Westh, P. Effects of osmolytes on hexokinase kinetics combined with macromolecular crowding: Test of the osmolyte compatibility hypothesis towards crowded systems. Comp. Biochem. Phys. A: Mol. Integr. Physiol. 148, 339-345 (2007).
    • (2007) Comp. Biochem. Phys. A: Mol. Integr. Physiol. , vol.148 , pp. 339-345
    • Olsen, S.N.1    Ramlov, H.2    Westh, P.3
  • 85
    • 84904470984 scopus 로고    scopus 로고
    • Inhibition of amyloid fibril formation of hen egg white lysozyme by trimethylamine N-oxide at low pH
    • Wawer, J. et al. Inhibition of amyloid fibril formation of hen egg white lysozyme by trimethylamine N-oxide at low pH. Int. J. Biol. Macromol. 70, 214-221(2014).
    • (2014) Int. J. Biol. Macromol. , vol.70 , pp. 214-221
    • Wawer, J.1
  • 87
    • 1842850631 scopus 로고    scopus 로고
    • Inhibition of insulin amyloid formation by small stress molecules
    • Arora, A., Hab, C. & Park, C. B. Inhibition of insulin amyloid formation by small stress molecules. FEBS Lett. 564, 121-125 (2004).
    • (2004) FEBS Lett. , vol.564 , pp. 121-125
    • Arora, A.1    Hab, C.2    Park, C.B.3
  • 88
    • 0026598013 scopus 로고
    • Enzyme stabilization by ectoine-type compatible solutes: Protection against heating, freezing and drying
    • Lippert, K. & Galinski, E. A. Enzyme stabilization by ectoine-type compatible solutes: protection against heating, freezing and drying. Appl. Micro. boil. Biotechnol. 37, 61-65(1992).
    • (1992) Appl. Micro. Boil. Biotechnol. , vol.37 , pp. 61-65
    • Lippert, K.1    Galinski, E.A.2
  • 89
    • 0039801358 scopus 로고    scopus 로고
    • Protection of a model enzyme (lactate dehydrogenase) against heat, urea and freeze-thaw treatment by compatible solute additive
    • Goller, K. & Galinski, E. A. Protection of a model enzyme (lactate dehydrogenase) against heat, urea and freeze-thaw treatment by compatible solute additive. J. Mol. Catal. B Enzym. 7, 37-45 (1999).
    • (1999) J. Mol. Catal. B Enzym. , vol.7 , pp. 37-45
    • Goller, K.1    Galinski, E.A.2
  • 90
    • 0038374325 scopus 로고    scopus 로고
    • Why is trehalose an exceptional protein stabilizer?
    • Kaushik, J. K. & Bhat, R. Why is trehalose an exceptional protein stabilizer? J. Biol. Chem.278, 26458-26465 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 26458-26465
    • Kaushik, J.K.1    Bhat, R.2
  • 91
    • 0035941144 scopus 로고    scopus 로고
    • Citrulline, a novel compatible solute in drought- tolerant wild watermelon leaves, is an efficient hydroxyl radical scavenger
    • Akashi, K., Miyake, C. & Yokota, A. Citrulline, a novel compatible solute in drought- tolerant wild watermelon leaves, is an efficient hydroxyl radical scavenger. FEBS Lett. 508, 438-442 (2001).
    • (2001) FEBS Lett. , vol.508 , pp. 438-442
    • Akashi, K.1    Miyake, C.2    Yokota, A.3
  • 93
    • 24044449002 scopus 로고    scopus 로고
    • Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimers β-amyloid
    • Kanapathipillaia, M., Lentzenb, G., Sierksa, M. & Park, C. B. Ectoine and hydroxyectoine inhibit aggregation and neurotoxicity of Alzheimers β-amyloid. FEBS Lett. 579, 4775-4780 (2005).
    • (2005) FEBS Lett. , vol.579 , pp. 4775-4780
    • Kanapathipillaia, M.1    Lentzenb, G.2    Sierksa, M.3    Park, C.B.4
  • 94
    • 0028278931 scopus 로고
    • The insulin receptor: Structure, function and signalling
    • Lee, J. & Pilch, P. F. The insulin receptor: structure, function and signalling. Am. J. Physiol. 266, C319-C334 (1994).
    • (1994) Am. J. Physiol. , vol.266 , pp. C319-C334
    • Lee, J.1    Pilch, P.F.2
  • 95
    • 0015517217 scopus 로고
    • Cross-β protein structures.I. Insulin fibrils
    • Burke, M. J. & Rougvie, M. A. Cross-β protein structures.I. Insulin fibrils. Biochemistry 11, 2435-2439 (1972).
    • (1972) Biochemistry , vol.11 , pp. 2435-2439
    • Burke, M.J.1    Rougvie, M.A.2
  • 96
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: Elucidation of the molecular mechanism
    • Nielsen, L. et al. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 40, 6036-6046 (2001).
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1
  • 97
    • 0033869084 scopus 로고    scopus 로고
    • Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry
    • Nettleton, E. J. et al. Characterization of the oligomeric states of insulin in self-assembly and amyloid fibril formation by mass spectrometry. Biophys. J. 79, 1053-1065 (2000).
    • (2000) Biophys. J. , vol.79 , pp. 1053-1065
    • Nettleton, E.J.1
  • 98
    • 0032054714 scopus 로고    scopus 로고
    • The role of assembly in insulins biosynthesis
    • Dodson, G. G. & Steiner, D. The role of assembly in insulins biosynthesis. Curr. Opin. Struct. Biol. 8, 189-194 (1998).
    • (1998) Curr. Opin. Struct. Biol. , vol.8 , pp. 189-194
    • Dodson, G.G.1    Steiner, D.2
  • 99
    • 67549142772 scopus 로고    scopus 로고
    • Localized insulin-derived amyloidosis in patients with diabetes mellitus: A case report
    • Yumlu, S., Barany, R., Eriksson, M. & Rocken, C. Localized insulin-derived amyloidosis in patients with diabetes mellitus: a case report. Hum. Pathol. 40, 1655-1660 (2009).
    • (2009) Hum. Pathol. , vol.40 , pp. 1655-1660
    • Yumlu, S.1    Barany, R.2    Eriksson, M.3    Rocken, C.4
  • 100
    • 77749333254 scopus 로고    scopus 로고
    • Localized amyloidosis at the site of repeated insulin injection in a diabetic patient
    • Shikama, Y. et al. Localized amyloidosis at the site of repeated insulin injection in a diabetic patient. Intern. Med. 49, 397-401 (2010).
    • (2010) Intern. Med. , vol.49 , pp. 397-401
    • Shikama, Y.1
  • 101
    • 0000685268 scopus 로고
    • Studies of the Nucleation and Growth Reactions of Selected Types of Insulin Fibrils
    • Waugh, D. F., Wilhelmson, D. F., Commerford, S. L. & Sackler, M. L. Studies of the Nucleation and Growth Reactions of Selected Types of Insulin Fibrils. J. Am. Chem. Soc. 75, 2592-2600 (1953).
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 2592-2600
    • Waugh, D.F.1    Wilhelmson, D.F.2    Commerford, S.L.3    Sackler, M.L.4
  • 102
    • 30044446633 scopus 로고    scopus 로고
    • Early Events in the Fibrillation of Monomeric Insulin
    • Ahmad, A., Uversky, V. N., Hong, D. & Fink, A. L. Early Events in the Fibrillation of Monomeric Insulin. J. Biol. Chem. 280, 42669-42675 (2005).
    • (2005) J. Biol. Chem. , vol.280 , pp. 42669-42675
    • Ahmad, A.1    Uversky, V.N.2    Hong, D.3    Fink, A.L.4
  • 103
    • 0036900745 scopus 로고    scopus 로고
    • Insulin delivery systems: Present trends and the future direction
    • Tyagi, P. Insulin delivery systems: present trends and the future direction. Indian J. Pharmacol. 34, 379-389 (2002).
    • (2002) Indian J. Pharmacol. , vol.34 , pp. 379-389
    • Tyagi, P.1
  • 104
    • 84055190997 scopus 로고    scopus 로고
    • Monitoring Insulin Aggregation via Capillary Electrophoresis
    • Pryor, E., Kotarek, J. A., Moss, M. A. & Hestekin, C. N. Monitoring Insulin Aggregation via Capillary Electrophoresis. Int. J. Mol. Sci. 12, 9369-9388 (2011).
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 9369-9388
    • Pryor, E.1    Kotarek, J.A.2    Moss, M.A.3    Hestekin, C.N.4
  • 105
    • 84878137806 scopus 로고    scopus 로고
    • Hierarchical ordering of amyloid fibrils on the mica surface
    • Zhou, X. et al. Hierarchical ordering of amyloid fibrils on the mica surface. Nanoscale 5, 4816-4822 (2013).
    • (2013) Nanoscale , vol.5 , pp. 4816-4822
    • Zhou, X.1
  • 107
    • 72249104137 scopus 로고    scopus 로고
    • Tyrosine Autofluorescence as a Measure of Bovine Insulin Fibrillation
    • Bekard, I. B. & Dunstan, D. E. Tyrosine Autofluorescence as a Measure of Bovine Insulin Fibrillation. Biophys. J. 97, 2521-2531 (2009).
    • (2009) Biophys. J. , vol.97 , pp. 2521-2531
    • Bekard, I.B.1    Dunstan, D.E.2
  • 108
    • 81455125565 scopus 로고    scopus 로고
    • The Mechanism of Enhanced Insulin Amyloid Fibril Formation by NaCl Is Better Explained by a Conformational Change Model
    • Muzaffar, M. & Ahmad, A. The Mechanism of Enhanced Insulin Amyloid Fibril Formation by NaCl Is Better Explained by a Conformational Change Model. PloS One 6, e27906 (2011).
    • (2011) PloS One , vol.6 , pp. e27906
    • Muzaffar, M.1    Ahmad, A.2
  • 109
    • 2342466734 scopus 로고    scopus 로고
    • Global prevalence of diabetes: Estimates for 2000 and projections for 2030
    • Wild, S. et al. Global prevalence of diabetes: estimates for 2000 and projections for 2030. Diabetes Care 27, 1047-1053 (2004).
    • (2004) Diabetes Care , vol.27 , pp. 1047-1053
    • Wild, S.1
  • 110
    • 33646130171 scopus 로고    scopus 로고
    • Inhibition of insulin fibrillogenesis with targeted peptides
    • Gibson, T. J. & Murphy, R. M. Inhibition of insulin fibrillogenesis with targeted peptides. Prot. Sci.15, 1133-1141 (2006).
    • (2006) Prot. Sci. , vol.15 , pp. 1133-1141
    • Gibson, T.J.1    Murphy, R.M.2
  • 112
    • 84884209192 scopus 로고    scopus 로고
    • Stabilization of bovine insulin against agitation-induced aggregation using RNA aptamers
    • Malik, R. & Roy, I. Stabilization of bovine insulin against agitation-induced aggregation using RNA aptamers. Int. J. Pharm. 452, 257-265 (2013).
    • (2013) Int. J. Pharm. , vol.452 , pp. 257-265
    • Malik, R.1    Roy, I.2
  • 113
    • 70350191425 scopus 로고    scopus 로고
    • Osmolyte controlled fibrillation kinetics of insulin: New insight into fibrillation using the preferential exclusion principle
    • Nayak, A., Lee, C. C., McRae, G. J. & Belfort, G. Osmolyte Controlled Fibrillation Kinetics of Insulin: New Insight into Fibrillation Using the Preferential Exclusion Principle. Biotechnol. Prog. 25, 1508-1514 (2009).
    • (2009) Biotechnol. Prog. , vol.25 , pp. 1508-1514
    • Nayak, A.1    Lee, C.C.2    McRae, G.J.3    Belfort, G.4
  • 114
    • 84904168587 scopus 로고    scopus 로고
    • Effects of several quinones on insulin aggregation
    • Gong, H. et al. Effects of several quinones on insulin aggregation. Sci. Rep. 4, 5648 (2014).
    • (2014) Sci. Rep. , vol.4 , pp. 5648
    • Gong, H.1
  • 115
    • 0027502784 scopus 로고
    • Thioflavin T interaction with synthetic Alzheimers disease β amyloid peptides: Detection of amyloid aggregation in solution
    • Levine, H. Thioflavin T interaction with synthetic Alzheimers disease β amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci. 2, 404-410 (1993).
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • Levine, H.1
  • 116
    • 67649397928 scopus 로고    scopus 로고
    • Bovine Insulin Filaments Induced by Reducing Disulfide Bonds Show a Different Morphology, Secondary Structure, and Cell Toxicity from Intact Insulin Amyloid Fibrils
    • Zako, T. et al. Bovine Insulin Filaments Induced by Reducing Disulfide Bonds Show a Different Morphology, Secondary Structure, and Cell Toxicity from Intact Insulin Amyloid Fibrils. Biophys. J. 96, 3331-3340 (2009).
    • (2009) Biophys. J. , vol.96 , pp. 3331-3340
    • Zako, T.1
  • 117
    • 0033777523 scopus 로고    scopus 로고
    • Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy
    • Bouchard, M. et al. Formation of insulin amyloid fibrils followed by FTIR simultaneously with CD and electron microscopy. Protein Sci. 9, 1960-1967 (2000).
    • (2000) Protein Sci. , vol.9 , pp. 1960-1967
    • Bouchard, M.1
  • 118
    • 84928733839 scopus 로고    scopus 로고
    • Addressing mechanism of fibrillization/aggregation and its prevention in presence of osmolytes: Spectroscopic and calorimetric approach
    • Choudhary, S. & Kishore, N. Addressing Mechanism of Fibrillization/Aggregation and Its Prevention in Presence of Osmolytes: Spectroscopic and Calorimetric Approach. PloS One 9, e104600 (2014).
    • (2014) PloS One , vol.9 , pp. e104600
    • Choudhary, S.1    Kishore, N.2
  • 119
    • 0022032982 scopus 로고
    • The stabilization of proteins by osmolytes
    • Arakawa,. T. & Timasheff, S. N. The stabilization of proteins by osmolytes. Biophys. J. 47, 411-414 (1985).
    • (1985) Biophys. J. , vol.47 , pp. 411-414
    • Arakawa, T.1    Timasheff, S.N.2
  • 120
    • 0031737071 scopus 로고    scopus 로고
    • The role of L-proline in the prevention of aggregation during protein folding in vitro
    • Kumar, T. K. S. et al. The role of L-proline in the prevention of aggregation during protein folding in vitro. Biochem. Mol. Biol. Int. 46, 509-517 (1998).
    • (1998) Biochem. Mol. Biol. Int. , vol.46 , pp. 509-517
    • Kumar, T.K.S.1
  • 121
    • 0001461512 scopus 로고
    • Partition chromatography of insulin and other proteins
    • Porter, R. R. Partition Chromatography of Insulin and Other Proteins. Biochem. 53, 320-328 (1953).
    • (1953) Biochem. , vol.53 , pp. 320-328
    • Porter, R.R.1
  • 122
    • 0032830122 scopus 로고    scopus 로고
    • In vitro immunoglobulin light chain fibrillogenesis
    • Wall, J., Murphy, C., L. & Solomon, A. In vitro immunoglobulin light chain fibrillogenesis. Methods Enzymol. 309, 204-217 (1999a).
    • (1999) Methods Enzymol. , vol.309 , pp. 204-217
    • Wall, J.1    Murphy, C.L.2    Solomon, A.3
  • 123
    • 0035918550 scopus 로고    scopus 로고
    • Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism
    • Nielsen, L. et al. Effect of Environmental Factors on the Kinetics of Insulin Fibril Formation: Elucidation of the Molecular Mechanism. Biochemistry 40, 6036-6046 (2001).
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1
  • 124
    • 2342662152 scopus 로고    scopus 로고
    • Negative Staining and Image Classification -Powerful Tools in Modern Electron Microscopy
    • Ohi, M., Li, Y., Cheng, Y. & Walz, T. Negative Staining and Image Classification -Powerful Tools in Modern Electron Microscopy. Biol. Proced. 6, 23-34 (2004).
    • (2004) Biol. Proced. , vol.6 , pp. 23-34
    • Ohi, M.1    Li, Y.2    Cheng, Y.3    Walz, T.4


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