메뉴 건너뛰기




Volumn 27, Issue 6, 2011, Pages 1768-1776

Amyloid fibril formation from crude protein mixtures

Author keywords

Amyloid fibril; Bionanomaterials; Morphology; Protein assembly

Indexed keywords

AMYLOID FIBRIL; AMYLOID FIBRIL FORMATION; BIONANOMATERIALS; CARBOXYMETHYLATION; CRUDE PROTEINS; FIBRILLAR STRUCTURES; HETEROGENEOUS MIXTURES; HIGHER ORDER; INSULIN AMYLOID FIBRILS; PROTEIN ASSEMBLY; PROTEIN FIBRILS; PROTEIN STRUCTURES; PURIFIED PROTEIN; RATE OF REACTION; THIOFLAVIN T; TRYPSIN DIGESTION;

EID: 82955233853     PISSN: 87567938     EISSN: 15206033     Source Type: Journal    
DOI: 10.1002/btpr.693     Document Type: Article
Times cited : (3)

References (37)
  • 1
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F, Dobson CM. Protein misfolding, functional amyloid, and human disease. Ann Rev Biochem. 2006; 75: 333-366.
    • (2006) Ann Rev Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 3
    • 0034683126 scopus 로고    scopus 로고
    • Amyloids protect the silkmoth oocyte and embryo
    • Iconomidou VA, Vriend G, Hamodrakas SJ. Amyloids protect the silkmoth oocyte and embryo. FEBS Lett. 2000; 479: 141-145.
    • (2000) FEBS Lett. , vol.479 , pp. 141-145
    • Iconomidou, V.A.1    Vriend, G.2    Hamodrakas, S.J.3
  • 5
    • 34249739081 scopus 로고    scopus 로고
    • Amyloid fibrils: from disease to design. New biomaterial applications for self-assembling cross-beta fibrils
    • Gras SL. Amyloid fibrils: from disease to design. New biomaterial applications for self-assembling cross-beta fibrils. Aust J Chem. 2007; 60: 333-342.
    • (2007) Aust J Chem. , vol.60 , pp. 333-342
    • Gras, S.L.1
  • 6
    • 47049100201 scopus 로고    scopus 로고
    • Amyloids: not only pathological agents but also ordered nanomaterials
    • Cherny, I, Gazit, E. Amyloids: not only pathological agents but also ordered nanomaterials. Angew Chem Int Ed. 2008; 47: 4062-4069.
    • (2008) Angew Chem Int Ed. , vol.47 , pp. 4062-4069
    • Cherny, I.1    Gazit, E.2
  • 7
    • 2942744730 scopus 로고    scopus 로고
    • Amyloid fibrils in bionanotechnology
    • Waterhouse, SH, Gerrard, JA. Amyloid fibrils in bionanotechnology. Aust J Chem. 2004; 57: 519-523.
    • (2004) Aust J Chem. , vol.57 , pp. 519-523
    • Waterhouse, S.H.1    Gerrard, J.A.2
  • 10
    • 0035158241 scopus 로고    scopus 로고
    • Studies of the structure of insulin fibrils by Fourier transform infrared (FTIR) spectroscopy and electron microscopy
    • Nielsen L, Frokjaer S, Carpenter JF, Brange J. Studies of the structure of insulin fibrils by Fourier transform infrared (FTIR) spectroscopy and electron microscopy. J Pharm Sci. 2001; 90: 29-37.
    • (2001) J Pharm Sci. , vol.90 , pp. 29-37
    • Nielsen, L.1    Frokjaer, S.2    Carpenter, J.F.3    Brange, J.4
  • 11
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism
    • Nielsen L, Khurana R, Coats A, Frokjaer S, Brange J, Vyas S, Uversky VN, Fink AL. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry. 2001; 40: 6036-6046.
    • (2001) Biochemistry. , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 12
    • 77956751025 scopus 로고
    • Insulin: the structure in the crystal and its reflection in chemistry and biology
    • Blundell TL, Dodson GG, Hodgkin DC, Mercola DA. Insulin: the structure in the crystal and its reflection in chemistry and biology. Adv Prot Chem. 1972; 26: 379-402.
    • (1972) Adv Prot Chem. , vol.26 , pp. 379-402
    • Blundell, T.L.1    Dodson, G.G.2    Hodgkin, D.C.3    Mercola, D.A.4
  • 13
    • 0000237715 scopus 로고
    • An X-ray diffraction investigation of selected type of insulin fibrils
    • Koltun WL, Waugh DF, Bear RS. An X-ray diffraction investigation of selected type of insulin fibrils. J Am Chem Soc. 1954; 76: 413-417.
    • (1954) J Am Chem Soc. , vol.76 , pp. 413-417
    • Koltun, W.L.1    Waugh, D.F.2    Bear, R.S.3
  • 14
    • 0026625689 scopus 로고
    • Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping
    • Suckau D, Mak M, Przybylski M. Protein surface topology-probing by selective chemical modification and mass spectrometric peptide mapping. Proc Natl Acad Sci USA. 1992; 89: 5630-5634.
    • (1992) Proc Natl Acad Sci USA. , vol.89 , pp. 5630-5634
    • Suckau, D.1    Mak, M.2    Przybylski, M.3
  • 15
    • 0015272069 scopus 로고
    • Molecular basis of insulin action: contributions of chemical modifications and synthetic approaches
    • Zahn H, Brandenburg D, Hans-Gregor G. Molecular basis of insulin action: contributions of chemical modifications and synthetic approaches. Diabetes. 1972; 21: 468-475.
    • (1972) Diabetes. , vol.21 , pp. 468-475
    • Zahn, H.1    Brandenburg, D.2    Hans-Gregor, G.3
  • 18
    • 0015899953 scopus 로고
    • Selective reduction of cystine I-VI11 in α-lactalbumin of bovine milk
    • Shechter Y, Patchornik A, Burstein Y. Selective reduction of cystine I-VI11 in α-lactalbumin of bovine milk. Biochemistry. 1973; 12: 3407-3413.
    • (1973) Biochemistry. , vol.12 , pp. 3407-3413
    • Shechter, Y.1    Patchornik, A.2    Burstein, Y.3
  • 19
    • 82955200159 scopus 로고    scopus 로고
    • Sigma-Aldrich. Trypsin, Proteomics Grade, Sigma: Product Code T 6567. Technical Bulletin. .
    • Sigma-Aldrich. Trypsin, Proteomics Grade, Sigma: Product Code T 6567. Technical Bulletin. 2007.
    • (2007)
  • 20
    • 0000857494 scopus 로고
    • An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • Eng JK, McCormack AL, Yates JR III. An approach to correlate tandem mass spectral data of peptides with amino acid sequences in a protein database. J Am Soc Mass Spectrom. 1994; 5: 976-989.
    • (1994) J Am Soc Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates III, J.R.3
  • 21
    • 0027502784 scopus 로고
    • Thioflavin T interaction with synthetic Alzheimer's disease α-amyloid peptides: detection of amyloid aggregation in solution
    • LeVine H III. Thioflavin T interaction with synthetic Alzheimer's disease α-amyloid peptides: detection of amyloid aggregation in solution. Protein Sci. 1993; 2: 404-410.
    • (1993) Protein Sci. , vol.2 , pp. 404-410
    • LeVine III, H.1
  • 22
    • 0015517217 scopus 로고
    • Cross-p protein structures. I. Insulin fibrils
    • Burke MJ, Rougvie MA. Cross-p protein structures. I. Insulin fibrils. Biochemistry. 1972; 11: 2435-2439.
    • (1972) Biochemistry. , vol.11 , pp. 2435-2439
    • Burke, M.J.1    Rougvie, M.A.2
  • 24
    • 0343730383 scopus 로고
    • Electrolytic reduction of the disulfide bonds of insulin
    • Markus G. Electrolytic reduction of the disulfide bonds of insulin. J Biol Chem. 1964; 239: 4163-4170.
    • (1964) J Biol Chem. , vol.239 , pp. 4163-4170
    • Markus, G.1
  • 25
    • 0019881763 scopus 로고
    • Disulphide bridges in globular proteins
    • Thornton JM. Disulphide bridges in globular proteins. J Mol Biol. 1981; 151: 261-287.
    • (1981) J Mol Biol. , vol.151 , pp. 261-287
    • Thornton, J.M.1
  • 26
    • 0001005525 scopus 로고
    • Regeneration of insulin from insulin fibrils by the action of alkali
    • Waugh DF. Regeneration of insulin from insulin fibrils by the action of alkali. J Am Chem Soc. 1948; 70: 1850-1857.
    • (1948) J Am Chem Soc. , vol.70 , pp. 1850-1857
    • Waugh, D.F.1
  • 27
    • 0018932451 scopus 로고
    • Calorimetric study of the reduction of the disulfide bonds in insulin
    • Fukada H, Takahashi K. Calorimetric study of the reduction of the disulfide bonds in insulin. J Biochem (Tokyo). 1980; 87: 1111-1117.
    • (1980) J Biochem (Tokyo). , vol.87 , pp. 1111-1117
    • Fukada, H.1    Takahashi, K.2
  • 28
    • 29244479548 scopus 로고    scopus 로고
    • Independent heterologous fibrillation of insulin and its b chain peptide
    • Hong D-P, Fink AL. Independent heterologous fibrillation of insulin and its b chain peptide. Biochemistry. 2005; 44: 16701-16709.
    • (2005) Biochemistry. , vol.44 , pp. 16701-16709
    • Hong, D.-P.1    Fink, A.L.2
  • 29
    • 33746648618 scopus 로고    scopus 로고
    • Fibrillation of human insulin a and b chains
    • Hong D-P, Ahmad A, Fink AL. Fibrillation of human insulin a and b chains. Biochemistry. 2006; 45: 9342-9353.
    • (2006) Biochemistry. , vol.45 , pp. 9342-9353
    • Hong, D.-P.1    Ahmad, A.2    Fink, A.L.3
  • 30
    • 76649138290 scopus 로고    scopus 로고
    • Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status
    • Groenning M. Binding mode of Thioflavin T and other molecular probes in the context of amyloid fibrils-current status. J Chem Biol. 2010; 3: 1-18.
    • (2010) J Chem Biol. , vol.3 , pp. 1-18
    • Groenning, M.1
  • 32
    • 0030907673 scopus 로고    scopus 로고
    • A model of insulin fibrils derived from the X-ray crystal structure of a monomeric insulin (despentapeptide insulin)
    • Brange J, Dodson GG, Edwards DJ, Holden PH, Whittingham JL. A model of insulin fibrils derived from the X-ray crystal structure of a monomeric insulin (despentapeptide insulin). Proteins. 1997; 27: 507-516.
    • (1997) Proteins. , vol.27 , pp. 507-516
    • Brange, J.1    Dodson, G.G.2    Edwards, D.J.3    Holden, P.H.4    Whittingham, J.L.5
  • 33
    • 33646468916 scopus 로고    scopus 로고
    • Unique milk protein based nanotubes: food and nanotechnology meet
    • Graveland-Bikker JF, de Kruif CG. Unique milk protein based nanotubes: food and nanotechnology meet. Trends Food Sci Technol. 2006; 17: 196-203.
    • (2006) Trends Food Sci Technol. , vol.17 , pp. 196-203
    • Graveland-Bikker, J.F.1    de Kruif, C.G.2
  • 34
    • 0031172143 scopus 로고    scopus 로고
    • The mechanical properties of simulated collagen fibrils
    • Parkinson J, Brass A, Canova G, Brechet Y. The mechanical properties of simulated collagen fibrils. J Biomech. 1997; 30: 549-554.
    • (1997) J Biomech. , vol.30 , pp. 549-554
    • Parkinson, J.1    Brass, A.2    Canova, G.3    Brechet, Y.4
  • 36
    • 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, Sakono M, Hashimoto N, Ihara M, Maeda M. Bovine insulin filaments induced by reducing disulfide bonds show a different morphology, secondary structure, and cell toxicity from intact insulin amyloid fibrils. Biophys J. 2009; 96: 3331-3340.
    • (2009) Biophys J. , vol.96 , pp. 3331-3340
    • Zako, T.1    Sakono, M.2    Hashimoto, N.3    Ihara, M.4    Maeda, M.5
  • 37
    • 37549031260 scopus 로고    scopus 로고
    • Amyloid a state in many guises: survival of the fittest fibril fold
    • Pedersen JS, Otzen DE. Amyloid a state in many guises: survival of the fittest fibril fold. Prot Sci. 2008; 17: 2-10.
    • (2008) Prot Sci. , vol.17 , pp. 2-10
    • Pedersen, J.S.1    Otzen, D.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.