Мобильная версия

Доступно журналов:

3 288

Доступно статей:

3 891 637

 

Скрыть метаданые

Автор Kretlow, Ariane
Автор Kneipp, Janina
Автор Lasch, Peter
Автор Beekes, Michael
Автор Miller, Lisa
Автор Naumann, Dieter
Дата выпуска 2011
ISBN 978-0-85404-154-1
Формат application.pdf
Издатель Royal Society of Chemistry
Название Chapter 11. Single Cell Analysis of TSE-infected Neurons
Тип other
DOI 10.1039/9781849731997-00315
Print ISSN 2041-9732
Журнал Biomedical Applications of Synchrotron Infrared Microspectroscopy
Первая страница 315
Последняя страница 338
Аффилиация Kretlow Ariane; P25, Robert Koch-Institut; National Synchrotron Light Source
Аффилиация Kneipp Janina; Federal Institute for Materials Research and Testing
Аффилиация Lasch Peter; P25, Robert Koch-Institut
Аффилиация Beekes Michael; P24, Robert Koch-Institut
Аффилиация Miller Lisa; National Synchrotron Light Source
Аффилиация Naumann Dieter; P25, Robert Koch-Institut
Библиографическая ссылка S. B. Prusiner, Prion diseases and the BSE crisis, Science, 1997, 278, 5336, 245, 51
Библиографическая ссылка K. M. Pan, M. Baldwin, J. Nguyen, M. Gasset, A. Serban, D. Groth, I. Mehlhorn, Z. Huang, R. J. Fletterick, F. E. Cohen et al., et al, Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins, Proc. Natl. Acad. Sci. USA, 1993, 90, 23, 10962, 6
Библиографическая ссылка M. Beekes, E. Baldauf, H. Diringer, Sequential appearance and accumulation of pathognomonic markers in the central nervous system of hamsters orally infected with scrapie, J. Gen. Virol., 1996, 77, Pt 8, 1925, 34
Библиографическая ссылка M. Beekes, P. A. McBride, The spread of prions through the body in naturally acquired transmissible spongiform encephalopathies, FEBS J., 2007, 274, 3, 588, 605
Библиографическая ссылка M. Beekes, P. A. McBride, E. Baldauf, Cerebral targeting indicates vagal spread of infection in hamsters fed with scrapie, J. Gen. Virol., 1998, 79, Pt 3, 601, 7
Библиографическая ссылка P. A. McBride, W. J. Schulz-Schaeffer, M. Donaldson, M. Bruce, H. Diringer, H. A. Kretzschmar, M. Beekes, Early spread of scrapie from the gastrointestinal tract to the central nervous system involves autonomic fibers of the splanchnic and vagus nerves, J. Virol., 2001, 75, 19, 9320, 7
Библиографическая ссылка P. A. McBride, M. Beekes, Pathological PrP is abundant in sympathetic and sensory ganglia of hamsters fed with scrapie, Neurosci. Lett., 1999, 265, 2, 135, 8
Библиографическая ссылка W. J. Schulz-Schaeffer, S. Tschoke, N. Kranefuss, W. Drose, D. Hause-Reitner, A. Giese, M. H. Groschup, H. A. Kretzschmar, The paraffin-embedded tissue blot detects PrP(Sc) early in the incubation time in prion diseases, Am. J. Pathol., 2000, 156, 1, 51, 6
Библиографическая ссылка D. L. Wetzel, S. M. LeVine, Imaging molecular chemistry with infrared microscopy, Science, 1999, 285, 5431, 1224, 5
Библиографическая ссылка P. Dumas, N. Jamin, J. L. Teillaud, L. M. Miller, B. Beccard, Imaging capabilities of synchrotron infrared microspectroscopy, Faraday Discuss., 2004, 126, 289, 302, discussion 303-11
Библиографическая ссылка P. Heraud, S. Caine, G. Sanson, R. Gleadow, B. R. Wood, D. McNaughton, Focal plane array infrared imaging: a new way to analyse leaf tissue, New Phytol., 2007, 173, 1, 216, 25
Библиографическая ссылка J. Kneipp, L. M. Miller, M. Joncic, M. Kittel, P. Lasch, M. Beekes, D. Naumann, In situ, Biochim. Biophys., Acta, 2003, 1639, 3, 152, 8
Библиографическая ссылка E. Baldauf, M. Beekes, H. Diringer, Evidence for an alternative direct route of access for the scrapie agent to the brain bypassing the spinal cord, J. Gen. Virol., 1997, 78, Pt 5, 1187, 97
Библиографическая ссылка Q. Wang, A. Kretlow, M. Beekes, D. Naumann, L. Miller, In situ, Vib. Spectrosc., 2005, 38, 61, 69
Библиографическая ссылка A. Dong, P. Huang, W. S. Caughey, Protein secondary structures in water from second-derivative amide I infrared spectra, Biochemistry, 1990, 29, 13, 3303, 8
Библиографическая ссылка A. Barth, C. Zscherp, What vibrations tell us about proteins, Quart. Rev. Biophys., 2002, 35, 4, 369, 430
Библиографическая ссылка J. Buijs, W. Norde, J. W. T. Lichtenbelt, Changes in the Secondary Structure of Adsorbed IgG and F(abâ ²)2 studied by FTIR Spectroscopy, Langmuir, 1996, 12, 1605, 13
Библиографическая ссылка N. Toyran, B. Turan, F. Severcan, Selenium alters the lipid content and protein profile of rat heart: an FTIR microspectroscopic study, Arch. Biochem. Biophys., 2007, 458, 2, 184, 93
Библиографическая ссылка K. K. Chittur, FTIR/ATR for protein adsorption to biomaterial surfaces, Biomaterials, 1998, 19, 4-5, 357, 69
Библиографическая ссылка A. Troullier, D. Reinstadler, Y. Dupont, D. Naumann, V. Forge, Transient non-native secondary structures during the refolding of alpha-lactalbumin detected by infrared spectroscopy, Nat. Struct. Biol., 2000, 7, 1, 78, 86
Библиографическая ссылка A. Dong, S. J. Prestrelski, S. D. Allison, J. F. Carpenter, Infrared spectroscopic studies of lyophilization- and temperature-induced protein aggregation, J. Pharm. Sci., 1995, 84, 4, 415, 24
Библиографическая ссылка A. Martinez, J. Haavik, T. Flatmark, J. L. Arrondo, A. Muga, Conformational properties and stability of tyrosine hydroxylase studied by infrared spectroscopy. Effect of iron/catecholamine binding and phosphorylation, J. Biol. Chem., 1996, 271, 33, 19737, 42
Библиографическая ссылка G. Damaschun, H. Damaschun, H. Fabian, K. Gast, R. Krober, M. Wieske, D. Zirwer, Conversion of yeast phosphoglycerate kinase into amyloid-like structure, Proteins, 2000, 39, 3, 204, 11
Библиографическая ссылка U. Dornberger, D. Fandrei, J. Backmann, W. Hubner, K. Rahmelow, K. H. Guhrs, M. Hartmann, B. Schlott, H. Fritzsche, A correlation between thermal stability and structural features of staphylokinase and selected mutants: a Fourier-transform infrared study, Biochim. Biophys. Acta, 1996, 1294, 2, 168, 76
Библиографическая ссылка R. J. Kascsak, R. Rubenstein, P. A. Merz, M. Tonna-DeMasi, R. Fersko, R. I. Carp, H. M. Wisniewski, H. Diringer, Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins, J. Virol., 1987, 61, 12, 3688, 93
Библиографическая ссылка M. Beekes, E. Baldauf, S. Cassens, H. Diringer, P. Keyes, A. C. Scott, G. A. Wells, P. Brown, C. J. Gibbs Jr., D. C. Gajdusek, Western blot mapping of disease-specific amyloid in various animal species and humans with transmissible spongiform encephalopathies using a high-yield purification method, J. Gen. Virol., 1995, 76, Pt 10, 2567, 76
Библиографическая ссылка J. F. Diedrich, P. E. Bendheim, Y. S. Kim, R. I. Carp, A. T. Haase, Scrapie-associated prion protein accumulates in astrocytes during scrapie infection, Proc. Natl. Acad. Sci. USA, 1991, 88, 2, 375, 9
Библиографическая ссылка J. F. Diedrich, R. I. Carp, A. T. Haase, Increased expression of heat shock protein, transferrin, and beta 2-microglobulin in astrocytes during scrapie, Microb. Pathog., 1993, 15, 1, 1, 6
Библиографическая ссылка M. Fusek, V. Vetvicka, Dual role of cathepsin D: ligand and protease, Biomed. Pap. Med. Fac. Univ. Palacky Olomouc Czech Repub., 2005, 149, 1, 43, 50
Библиографическая ссылка T. Lah, M. Drobnic-Kosorok, V. Turk, R. H. Pain, D. Cathepsin, Biochem J., 1984, 218, 2, 601, 608
Библиографическая ссылка M. Okon, P. Bray, D. Vucelic, 1H NMR assignments and secondary structure of human beta 2-microglobulin in solution, Biochemistry, 1992, 31, 37, 8906, 15
Библиографическая ссылка E. L. Oleszak, G. Murdoch, L. Manuelidis, E. E. Manuelidis, Growth factor production by Creutzfeldt-Jakob disease cell lines, J. Virol., 1988, 62, 9, 3103, 8
Библиографическая ссылка J. Pammer, W. Weninger, E. Tschachler, in vitro, Am. J. Pathol., 1998, 153, 5, 1353, 8
Библиографическая ссылка G. Li, D. C. Bolton, A novel hamster prion protein mRNA contains an extra exon: increased expression in scrapie, Brain Res., 1997, 751, 2, 265, 74
Библиографическая ссылка S. Halliday, F. Houston, N. Hunter, Expression of PrPC on cellular components of sheep blood, J. Gen. Virol., 2005, 86, Pt 5, 1571, 9
Библиографическая ссылка I. Ferrer, R. Blanco, M. Carmona, B. Puig, R. Ribera, M. J. Rey, T. Ribalta, Prion protein expression in senile plaques in Alzheimer's disease, Acta Neuropathol., 2001, 101, 1, 49, 56
Библиографическая ссылка C. Robertson, S. A. Booth, D. R. Beniac, M. B. Coulthart, T. F. Booth, A. McNicol, Cellular prion protein is released on exosomes from activated platelets, Blood, 2006, 107, 10, 3907, 11
Библиографическая ссылка I. Porto-Carreiro, B. Fevrier, S. Paquet, D. Vilette, G. Raposo, Prions and exosomes: from PrPc trafficking to PrPsc propagation, Blood Cells Mol. Dis., 2005, 35, 2, 143, 8
Библиографическая ссылка B. Fevrier, D. Vilette, F. Archer, D. Loew, W. Faigle, M. Vidal, H. Laude, G. Raposo, Cells release prions in association with exosomes, Proceedings of the National Academy of Sciences of the United States of America, 2004, 101, 26, 9683, 8
Библиографическая ссылка B. Fevrier, D. Vilette, H. Laude, G. Raposo, Exosomes: a bubble ride for prions, Traffic, 2005, 6, 1, 10, 7
Библиографическая ссылка A. Mironov Jr., D. Latawiec, H. Wille, E. Bouzamondo-Bernstein, G. Legname, R. A. Williamson, D. Burton, S. J. DeArmond, S. B. Prusiner, P. J. Peters, Cytosolic prion protein in neurons, J. Neurosci., 2003, 23, 18, 7183, 93
Библиографическая ссылка M. A. Prado, J. Alves-Silva, A. C. Magalhaes, V. F. Prado, R. Linden, V. R. Martins, R. R. Brentani, PrPc on the road: trafficking of the cellular prion protein, J. Neurochem., 2004, 88, 4, 769, 81
Библиографическая ссылка A. Taraboulos, D. Serban, S. B. Prusiner, Scrapie prion proteins accumulate in the cytoplasm of persistently infected cultured cells, J. Cell Biol., 1990, 110, 6, 2117, 32
Библиографическая ссылка M. P. McKinley, A. Taraboulos, L. Kenaga, D. Serban, A. Stieber, S. J. DeArmond, S. B. Prusiner, N. Gonatas, Ultrastructural localization of scrapie prion proteins in cytoplasmic vesicles of infected cultured cells, Lab. Invest., 1991, 65, 6, 622, 30
Библиографическая ссылка A. Taraboulos, M. Scott, A. Semenov, D. Avrahami, S. B. Prusiner, Biosynthesis of the prion proteins in scrapie-infected cells in culture, Braz. J. Med. Biol. Res., 1994, 27, 2, 303, 7
Библиографическая ссылка J. A. Johnston, C. L. Ward, R. R. Kopito, Aggresomes: a cellular response to misfolded proteins, J. Cell Biol., 1998, 143, 7, 1883, 98
Библиографическая ссылка E. Cohen, A. Taraboulos, Scrapie-like prion protein accumulates in aggresomes of cyclosporin A-treated cells, EMBO J., 2003, 22, 3, 404, 17
Библиографическая ссылка A. Mange, C. Crozet, S. Lehmann, F. Beranger, Scrapie-like prion protein is translocated to the nuclei of infected cells independently of proteasome inhibition and interacts with chromatin, J. Cell Sci., 2004, 117, Pt 11, 2411, 6
Библиографическая ссылка J. Ma, R. Wollmann, S. Lindquist, Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol, Science, 2002, 298, 5599, 1781, 5
Библиографическая ссылка B. Caughey, G. J. Raymond, The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive, J. Biol. Chem., 1991, 266, 27, 18217, 23
Библиографическая ссылка S. Lehmann, D. A. Harris, Mutant and infectious prion proteins display common biochemical properties in cultured cells, J. Biol. Chem., 1996, 271, 3, 1633, 7
Библиографическая ссылка L. J. van Keulen, B. E. Schreuder, R. H. Meloen, M. Poelen-van den Berg, G. Mooij-Harkes, M. E. Vromans, J. P. Langeveld, Immunohistochemical detection and localization of prion protein in brain tissue of sheep with natural scrapie, Vet. Pathol., 1995, 32, 3, 299, 308
Библиографическая ссылка M. Jeffrey, C. M. Goodsir, M. E. Bruce, P. A. McBride, N. Fowler, J. R. Scott, in vivo, Neurosci. Lett., 1994, 174, 1, 39, 42
Библиографическая ссылка M. Jeffrey, C. M. Goodsir, M. E. Bruce, P. A. McBride, J. R. Scott, Infection-specific prion protein (PrP) accumulates on neuronal plasmalemma in scrapie-infected mice, Ann. N. Y. Acad. Sci., 1994, 724, 327, 30
Библиографическая ссылка F. Archer, C. Bachelin, O. Andreoletti, N. Besnard, G. Perrot, C. Langevin, A. Le Dur, D. Vilette, A. Baron-Van Evercooren, J. L. Vilotte, H. Laude, Cultured peripheral neuroglial cells are highly permissive to sheep prion infection, J. Virol., 2004, 78, 1, 482, 90
Библиографическая ссылка M. H. Groschup, M. Beekes, P. A. McBride, M. Hardt, J. A. Hainfellner, H. Budka, Deposition of disease-associated prion protein involves the peripheral nervous system in experimental scrapie, Acta Neuropathol. (Berl.), 1999, 98, 5, 453, 7
Библиографическая ссылка S. Booth, C. Bowman, R. Baumgartner, G. Sorensen, C. Robertson, M. Coulthart, C. Phillipson, R. L. Somorjai, Identification of central nervous system genes involved in the host response to the scrapie agent during preclinical and clinical infection, J. Gen. Virol., 2004, 85, Pt 11, 3459, 71
Библиографическая ссылка R. Chiesa, B. Drisaldi, E. Quaglio, A. Migheli, P. Piccardo, B. Ghetti, D. A. Harris, Accumulation of protease-resistant prion protein (PrP) and apoptosis of cerebellar granule cells in transgenic mice expressing a PrP insertional mutation, Proc. Natl. Acad. Sci. USA, 2000, 97, 10, 5574, 9
Библиографическая ссылка Y. Zhang, E. Spiess, M. H. Groschup, A. Burkle, Up-regulation of cathepsin B and cathepsin L activities in scrapie-infected mouse Neuro2a cells, J. Gen. Virol., 2003, 84, Pt 8, 2279, 83
Библиографическая ссылка C. Hetz, M. Russelakis-Carneiro, K. Maundrell, J. Castilla, C. Soto, Caspase-12 and endoplasmic reticulum stress mediate neurotoxicity of pathological prion protein, EMBO J., 2003, 22, 20, 5435, 45
Библиографическая ссылка X. Ye, H. C. Meeker, P. Kozlowski, R. I. Carp, Increased c-Fos protein in the brains of scrapie-infected SAMP8, SAMR1, AKR and C57BL mice, Neuropathol. Appl. Neurobiol., 2002, 28, 5, 358, 66
Библиографическая ссылка S. K. Park, S. I. Choi, J. K. Jin, E. K. Choi, J. I. Kim, R. I. Carp, Y. S. Kim, Differential expression of Bax and Bcl-2 in the brains of hamsters infected with 263K scrapie agent, Neuroreport, 2000, 11, 8, 1677, 82
Библиографическая ссылка N. Jamin, L. Miller, J. Moncuit, W. H. Fridman, P. Dumas, J. L. Teillaud, Chemical heterogeneity in cell death: combined synchrotron IR and fluorescence microscopy studies of single apoptotic and necrotic cells, Biopolymers, 2003, 72, 5, 366, 73
Библиографическая ссылка H. Fabian, C. Schultz, Fourier Transform Infrared Spectroscopy in Peptide and Protein Analysis, Encyclop. Anal. Chem., 2000, 5779, 5803
Библиографическая ссылка C. Yu, J. Irudayaraj, Spectroscopic characterization of microorganisms by Fourier transform infrared microspectroscopy, Biopolymers, 2005, 77, 6, 368, 77

Скрыть метаданые