메뉴 건너뛰기




Volumn 285, Issue 1, 1999, Pages 33-39

Watching amyloid fibrils grow by time-lapse atomic force microscopy

Author keywords

Amylin; Amyloid; Diabetes; Fibril formation; Time lapse atomic force microscopy

Indexed keywords

AMYLIN; AMYLOID;

EID: 0033534397     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2299     Document Type: Article
Times cited : (308)

References (29)
  • 1
    • 0028800177 scopus 로고
    • Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin
    • Bauer H. H., Aebi U., Haener M., Hermann R., Mueller M., Arvinte T., Merkle H. P. Architecture and polymorphism of fibrillar supramolecular assemblies produced by in vitro aggregation of human calcitonin. J. Struct. Biol. 115:1995;1-15.
    • (1995) J. Struct. Biol. , vol.115 , pp. 1-15
    • Bauer, H.H.1    Aebi, U.2    Haener, M.3    Hermann, R.4    Mueller, M.5    Arvinte, T.6    Merkle, H.P.7
  • 4
    • 0023579739 scopus 로고
    • Purification and characterisation 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., Reid K. B. M. Purification and characterisation of a peptide from amyloid-rich pancreases of type 2 diabetic patients. Proc. Natl Acad. Sci. USA. 84:1987;8628-8632.
    • (1987) Proc. Natl Acad. Sci. USA , 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
  • 6
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes E. D., Glenner G. G. X-ray diffraction studies on amyloid filaments. J. Histochem. Cytochem. 16:1968;673-677.
    • (1968) J. Histochem. Cytochem. , vol.16 , pp. 673-677
    • Eanes, E.D.1    Glenner, G.G.2
  • 9
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's amyloid-beta protein
    • Harper J. D., Lieber C. M., Lansbury P. T. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's amyloid-beta protein. Chem. Biol. 4:1997;951-959.
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury, P.T.3
  • 12
    • 0028303844 scopus 로고
    • Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus
    • Lorenzo A., Razzaboni B., Weir G. C., Yankner B. A. Pancreatic islet cell toxicity of amylin associated with type-2 diabetes mellitus. Nature. 368:1994;756-760.
    • (1994) Nature , vol.368 , pp. 756-760
    • Lorenzo, A.1    Razzaboni, B.2    Weir, G.C.3    Yankner, B.A.4
  • 13
    • 0029935479 scopus 로고    scopus 로고
    • Atomic force microscopy studies of surface morphology and growth kinetics in thaumatin crystallization
    • Malkin A. J., Kuznetsov Y. G., Glantz W., McPherson A. Atomic force microscopy studies of surface morphology and growth kinetics in thaumatin crystallization. Proteins: Struct. Funct. Genet. 24:1996;247-252.
    • (1996) Proteins: Struct. Funct. Genet. , vol.24 , pp. 247-252
    • Malkin, A.J.1    Kuznetsov, Y.G.2    Glantz, W.3    McPherson, A.4
  • 14
    • 0029069245 scopus 로고
    • Atomic force microscopy of cholera toxin B-oligomers bound to bilayers of biologically relevant lipids
    • Mou J., Yang J., Shao S. Atomic force microscopy of cholera toxin B-oligomers bound to bilayers of biologically relevant lipids. J. Mol. Biol. 248:1995;507-512.
    • (1995) J. Mol. Biol. , vol.248 , pp. 507-512
    • Mou, J.1    Yang, J.2    Shao, S.3
  • 15
    • 0037923070 scopus 로고    scopus 로고
    • The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions
    • Müller D. J., Engel A. The height of biomolecules measured with the atomic force microscope depends on electrostatic interactions. Biophys. J. 73:1997;1633-1644.
    • (1997) Biophys. J. , vol.73 , pp. 1633-1644
    • Müller, D.J.1    Engel, A.2
  • 16
    • 0028998339 scopus 로고
    • Force-induced conformational change of bacteriorhodopsin
    • Müller D. J., Büldt G., Engel A. Force-induced conformational change of bacteriorhodopsin. J. Mol. Biol. 249:1995;239-243.
    • (1995) J. Mol. Biol. , vol.249 , pp. 239-243
    • Müller, D.J.1    Büldt, G.2    Engel, A.3
  • 17
    • 0025262297 scopus 로고
    • Amylin secretion from the rat pancreas and its selective loss after streptozotocin treatment
    • Ogawa A., Harris V., McCorkle S. K., Unger R. H., Luskey K. L. Amylin secretion from the rat pancreas and its selective loss after streptozotocin treatment. J. Clin. Invest. 85:1990;973-976.
    • (1990) J. Clin. Invest. , vol.85 , pp. 973-976
    • Ogawa, A.1    Harris, V.2    McCorkle, S.K.3    Unger, R.H.4    Luskey, K.L.5
  • 18
    • 0031880366 scopus 로고    scopus 로고
    • Growth of protein 2-D crystals on supported planar lipid bilayers imaged in situ by AFM
    • Reviakine I., Bergsma-Schutter W., Brisson A. Growth of protein 2-D crystals on supported planar lipid bilayers imaged in situ by AFM. J. Struct. Biol. 121:1998;356-361.
    • (1998) J. Struct. Biol. , vol.121 , pp. 356-361
    • Reviakine, I.1    Bergsma-Schutter, W.2    Brisson, A.3
  • 19
    • 0031011695 scopus 로고    scopus 로고
    • Reversible unfolding of individual titin immunoglobulin domains by AFM
    • Rief M., Gautel M., Oesterhelt F., Fernandez J. M., Gaub H. E. Reversible unfolding of individual titin immunoglobulin domains by AFM. Science. 276:1997;1109-1112.
    • (1997) Science , vol.276 , pp. 1109-1112
    • Rief, M.1    Gautel, M.2    Oesterhelt, F.3    Fernandez, J.M.4    Gaub, H.E.5
  • 22
    • 0031170886 scopus 로고    scopus 로고
    • The toxicity of the Alzheimer's beta amyloid peptide correlates with a distinct fiber morphology
    • Seilheimer B., Bohrmann B., Bondolfi L., Mueller F., Stueber D., Doebeli H. The toxicity of the Alzheimer's beta amyloid peptide correlates with a distinct fiber morphology. J. Struct. Biol. 119:1997;59-71.
    • (1997) J. Struct. Biol. , vol.119 , pp. 59-71
    • Seilheimer, B.1    Bohrmann, B.2    Bondolfi, L.3    Mueller, F.4    Stueber, D.5    Doebeli, H.6
  • 24
    • 0014098295 scopus 로고
    • High resolution electron microscopic analysis of the amyloid fibril
    • Shirahama T., Cohen A. S. High resolution electron microscopic analysis of the amyloid fibril. J. Cell. Biol. 33:1967;679-706.
    • (1967) J. Cell. Biol. , vol.33 , pp. 679-706
    • Shirahama, T.1    Cohen, A.S.2
  • 26
    • 0031983456 scopus 로고    scopus 로고
    • Pathologic amyloid beta-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells
    • Van Nostrand W. E., Melchor J. P., Ruffini L. Pathologic amyloid beta-protein cell surface fibril assembly on cultured human cerebrovascular smooth muscle cells. J. Neurochem. 70:1998;216-223.
    • (1998) J. Neurochem. , vol.70 , pp. 216-223
    • Van Nostrand, W.E.1    Melchor, J.P.2    Ruffini, L.3
  • 27
    • 0023192941 scopus 로고
    • Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells
    • Westermark P., Wernstedt C., Wilander E., Hayden D. W., O'Brien T. D., Johnson K. H. Amyloid fibrils in human insulinoma and islets of Langerhans of the diabetic cat are derived from a neuropeptide-like protein also present in normal islet cells. Proc. Natl Acad. Sci. USA. 84:1987;3881-3885.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 3881-3885
    • Westermark, P.1    Wernstedt, C.2    Wilander, E.3    Hayden, D.W.4    O'Brien, T.D.5    Johnson, K.H.6
  • 29
    • 0032573868 scopus 로고    scopus 로고
    • Carbon nanotube tips: High-resolution probes for imaging biological systems
    • Wong S. S., Harper J. D., Lansbury P. T., Lieber C. M. Carbon nanotube tips: high-resolution probes for imaging biological systems. J. Am. Chem. Soc. 120:1998;603-604.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 603-604
    • Wong, S.S.1    Harper, J.D.2    Lansbury, P.T.3    Lieber, C.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.