KeyNo Authors Year Pages Journal Journal2 Title Abstract Keywords Times Cited Cited Reference Count: cit

1 Mattson, M P, Haddon, R. C., Rao, A. M. 2000 175-182 J. Mol. Neurosci. J Mol Neurosci Molecular functionalization of carbon nanotubes and use as substrates for neuronal growth Carbon nanotubes are strong, flexible, conduct electrical current, and can be functionalized with different molecules, properties that may be useful in basic and applied neuroscience research. We report the first application of carbon nanotube technology to neuroscience research. Methods were developed for growing embryonic rat-brain neurons on multiwalled carbon nanotubes. On unmodified nanotubes, neurons extend only one or two neurites, which exhibit very few branches. In contrast, neurons grown on nanotubes coated with the bioactive molecule 4-hydroxynonenal elaborate multiple neurites, which exhibit extensive branching. These findings establish the feasability of using nanotubes as substrates for nerve cell growth and as probes of neuronal function at the nanometer scale. brain, growth cones, hippocampus, hydroxynonenal, nanotechnology, cone guidance, lipid-peroxidation, calcium regulation, chemistry, proteins, product 279 27      Hamon MA, 1999, ADV MATER, V11, P834, DOI 10.1002/(SICI)1521-4095(199907)11:10<834::AID-ADMA834>3.0.CO      Song HJ, 1999, CURR OPIN NEUROBIOL, V9, P355, DOI 10.1016/S0959-4388(99)80052-X      Andrews R, 1999, CHEM PHYS LETT, V303, P467, DOI 10.1016/S0009-2614(99)00282-1      Mattson MP, 1999, J NEUROSCI RES, V56, P8, DOI 10.1002/(SICI)1097-4547(19990401)56:1<8::AID-JNR2>3.3.CO 2-lug      Fan SS, 1999, SCIENCE, V283, P512, DOI 10.1126/science.283.5401.512      Ren ZF, 1998, SCIENCE, V282, P1105, DOI 10.1126/science.282.5391.1105      Chen J, 1998, SCIENCE, V282, P95, DOI 10.1126/science.282.5386.95      Wong SS, 1998, NATURE, V394, P52      Tans SJ, 1998, NATURE, V393, P49      Suter DM, 1998, CURR OPIN NEUROBIOL, V8, P106, DOI 10.1016/S0959-4388(98)80014-7      Wong EW, 1997, SCIENCE, V277, P1971, DOI 10.1126/science.277.5334.1971      Journet C, 1997, NATURE, V388, P756      Mattson MP, 1997, NEUROREPORT, V8, P2275, DOI 10.1097/00001756-199707070-00036      Rao AM, 1997, SCIENCE, V275, P187, DOI 10.1126/science.275.5297.187      Mark RJ, 1997, J NEUROCHEM, V68, P255      Thess A, 1996, SCIENCE, V273, P483, DOI 10.1126/science.273.5274.483      Carini R, 1996, BIOCHEM BIOPH RES CO, V218, P772, DOI 10.1006/bbrc.1996.0137      Waeg G, 1996, FREE RADICAL RES, V25, P149, DOI 10.3109/10715769609149920      Goodman CS, 1996, ANNU REV NEUROSCI, V19, P341, DOI 10.1146/annurev.neuro.19.1.341      UCHIDA K, 1992, P NATL ACAD SCI USA, V89, P4544, DOI 10.1073/pnas.89.10.4544      LUSTGARTEN JH, 1991, J BIOMECH ENG-T ASME, V113, P184, DOI 10.1115/1.2891232      ESTERBAUER H, 1991, FREE RADICAL BIO MED, V11, P81, DOI 10.1016/0891-5849(91)90192-6      MATTSON MP, 1988, J NEUROSCI RES, V21, P447, DOI 10.1002/jnr.490210236      KATER SB, 1988, TRENDS NEUROSCI, V11, P315, DOI 10.1016/0166-2236(88)90094-X      MATTSON MP, 1988, J NEUROSCI, V8, P2087      MATTSON MP, 1988, BRAIN RES REV, V13, P179, DOI 10.1016/0165-0173(88)90020-3      MATTSON MP, 1987, J NEUROSCI, V7, P4034

2 Akiyoshi, K, Itaya, A., Nomura, S. M., Ono, N., Yoshikawa, K. 2003 33-38 FEBS Lett. FEBS Lett Induction of neuron-like tubes and liposome networks by cooperative effect of gangliosides and phospholipids Although there is a rather large abundance of gangliosides in neurons, their functional role is still unclear. We focused on a physicochemical role of gangliosides in the formation of tubular structures, such as axons or dendrites in neurons. When a ganglioside, GM3, was added to cell-size liposomes that consisted of dioleoylphosphatidyl-choline, tubular structures were induced and liposome networks connected by the tubes were observed by differential interference microscopy and fluorescence microscopy. The potential for various gangliosides to induce tubes was dependent on the structures of their hydrophilic head group. With a large excess of gangliosides, the tubes are destabilized and small fragments, or micelles, are generated. The phenomenon was suggested by physical model calculation. Gangliosides may play a role as building material in neural unique tubular structures. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved. ganglioside, neuron, giant liposome, nanotube, network structure, microscopic observation, lipid tubules, containers, nanotubes, membranes, cells 36 29      Shimizu T, 2002, MACROMOL RAPID COMM, V23, P311, DOI 10.1002/1521-3927(20020401)23:5/6<311::AID-MARC311>3.0.CO      Szostak JW, 2001, NATURE, V409, P387, DOI 10.1038/35053176      Karlsson A, 2001, NATURE, V409, P150, DOI 10.1038/35051656      Karlsson M, 2000, ANAL CHEM, V72, P5857, DOI 10.1021/ac0003246      LUISI PL, 2000, PERSPECTIVE SUPRAMOL, V6      Prinetti A, 1999, J BIOL CHEM, V274, P20916, DOI 10.1074/jbc.274.30.20916      Chiu DT, 1999, SCIENCE, V283, P1892, DOI 10.1126/science.283.5409.1892      ZIGMOND MJ, 1999, FUNDAMENTAL NEUROSCI, P519      Bucher P, 1998, LANGMUIR, V14, P2712, DOI 10.1021/la971318g      Simons K, 1997, NATURE, V387, P569, DOI 10.1038/42408      Magome N, 1997, CHEM LETT, P205, DOI 10.1246/cl.1997.205      Evans E, 1996, SCIENCE, V273, P933, DOI 10.1126/science.273.5277.933      Kulkarni VS, 1995, BIOPHYS J, V69, P1976      RAHMANN H, 1995, BEHAV BRAIN RES, V66, P105, DOI 10.1016/0166-4328(94)00131-X      SCHNUR JM, 1994, SCIENCE, V264, P945, DOI 10.1126/science.264.5161.945      SONNINO S, 1994, CHEM PHYS LIPIDS, V71, P21, DOI 10.1016/0009-3084(94)02304-2      SCHNUR JM, 1993, SCIENCE, V262, P1669, DOI 10.1126/science.262.5140.1669      LASIC DD, 1993, LIPOSOMES PHYSICS AP      ARCHIBALD DD, 1992, BIOCHEMISTRY-US, V31, P9045, DOI 10.1021/bi00152a048      KUNITAKE T, 1992, ANGEW CHEM INT EDIT, V31, P709, DOI 10.1002/anie.199207091      Israelachvili JN., 1992, INTERMOLECULAR SURFA      SCHENGRUND CL, 1990, BRAIN RES BULL, V24, P131, DOI 10.1016/0361-9230(90)90297-D      CANNELLA MS, 1988, DEV BRAIN RES, V39, P137, DOI 10.1016/0165-3806(88)90075-2      CURATOLO W, 1986, J BIOL CHEM, V261, P7177      HOTANI H, 1984, J MOL BIOL, V178, P113, DOI 10.1016/0022-2836(84)90234-1      LEDEEN RW, 1984, J NEUROSCI RES, V12, P147, DOI 10.1002/jnr.490120204      TSUJI S, 1983, J BIOCHEM-TOKYO, V94, P303      FORMISANO S, 1979, BIOCHEMISTRY-US, V18, P1119, DOI 10.1021/bi00573a028      HELFRICH W, 1973, Z NATURFORSCH C, VC 28, P693

3 Cans, A S, Wittenberg, N., Karlsson, R., Sombers, L., Karlsson, M., Orwar, O., Ewing, A. 2003 400-404 Proc. Natl. Acad. Sci. U. S. A. P NATL ACAD SCI USA Artificial cells: Unique insights into exocytosis using liposomes and lipid nanotubes Exocytosis is the fundamental process underlying neuronal communication. This process involves fusion of a small neurotransmitter-containing vesicle with the plasma membrane of a cell to release minute amounts of transmitter molecules. Exocytosis is thought to go through an intermediate step involving formation of a small lipid nanotube or fusion pore, followed by expansion of the pore to the final stage of exocytosis. The process of exocytosis has been studied by various methods, however, when living cells are used it is difficult to discriminate between the molecular effects of membrane proteins relative to the mechanics of lipid-membrane-driven processes and to manipulate system parameters (e.g., membrane composition, pH, ion concentration, temperature, etc.). We describe the use of liposome-lipid nanotube networks to create an artificial cell model that undergoes the later stages of exocytosis. This model shows that membrane mechanics, without protein intervention, can drive expansion of the fusion pore to the final stage of exocytosis and can affect the rate of transmitter release through the fusion pore. adrenal chromaffin cells, pores connecting membranes, fusion pore, different tensions, vesicle fusion, release, events, secretion, dynamics, pheochromocytoma 64 33      Karlsson R, 2002, LANGMUIR, V18, P4186, DOI 10.1021/la025533v      Cho SJ, 2002, CELL BIOL INT, V26, P35, DOI 10.1006/cbir.2001.0849      Bruns Dieter, 2002, Pfluegers Archiv European Journal of Physiology, V443, P333, DOI 10.1007/s00424-001-0742-4      Kahya N, 2001, BIOPHYS J, V81, P1464      Karlsson A, 2001, NATURE, V409, P150, DOI 10.1038/35051656      Karlsson M, 2000, ANAL CHEM, V72, P5857, DOI 10.1021/ac0003246      Chizmadzhev YA, 2000, BIOPHYS J, V78, P2241      Amatore C, 2000, BIOCHIMIE, V82, P481, DOI 10.1016/S0300-9084(00)00213-3      Amatore C, 1999, CHEM-EUR J, V5, P2151, DOI 10.1002/(SICI)1521-3765(19990702)5:7<2151::AID-CHEM2151>3.3.CO      Chizmadzhev YA, 1999, BIOPHYS J, V76, P2951, DOI 10.1016/S0006-3495(99)77450-3      Angleson JK, 1999, NAT NEUROSCI, V2, P440      Woodbury Dixon J., 1999, Cell Biochemistry and Biophysics, V30, P303, DOI 10.1007/BF02738117      Kozminski KD, 1998, ANAL CHEM, V70, P3123, DOI 10.1021/ac980129f      Takei K, 1998, CELL, V94, P131, DOI 10.1016/S0092-8674(00)81228-3      Chanturiya A, 1997, P NATL ACAD SCI USA, V94, P14423, DOI 10.1073/pnas.94.26.14423      Steyer JA, 1997, NATURE, V388, P474      Khanin R, 1997, BIOPHYS J, V72, P507      Evans E, 1996, SCIENCE, V273, P933, DOI 10.1126/science.273.5277.933      Monck JR, 1996, CURR OPIN CELL BIOL, V8, P524, DOI 10.1016/S0955-0674(96)80031-7      Finnegan JM, 1996, J NEUROCHEM, V66, P1914      Calakos N, 1996, PHYSIOL REV, V76, P1      Chizmadzhev YA, 1995, BIOPHYS J, V69, P2489      WIGHTMAN RM, 1995, BIOPHYS J, V68, P383      MONCK JR, 1995, MOL MEMBR BIOL, V12, P151, DOI 10.3109/09687689509038511      DETOLEDO GA, 1993, NATURE, V363, P554, DOI 10.1038/363554a0      CHOW RH, 1992, NATURE, V356, P60, DOI 10.1038/356060a0      WIGHTMAN RM, 1991, P NATL ACAD SCI USA, V88, P10754, DOI 10.1073/pnas.88.23.10754      MONCK JR, 1990, P NATL ACAD SCI USA, V87, P7804, DOI 10.1073/pnas.87.20.7804      HOEKSTRA D, 1990, HEPATOLOGY, V12, pS61      SCHMIDT W, 1983, EUR J CELL BIOL, V32, P31      NEHER E, 1982, P NATL ACAD SCI-BIOL, V79, P6712, DOI 10.1073/pnas.79.21.6712      ZIMMERBERG J, 1980, J GEN PHYSIOL, V75, P241, DOI 10.1085/jgp.75.3.241      CHANDLER DE, 1980, J CELL BIOL, V86, P666, DOI 10.1083/jcb.86.2.666

4 Elam, J S, Taylor, A. B., Strange, R., Antonyuk, S., Doucette, P. A., Rodriguez, J. A., Hasnain, S. S., Hayward, L. J., Valentine, J. S., Yeates, T. O., Hart, P. J. 2003 461-467 Nat. Struct. Biol. Nat Struct Biol Amyloid-like filaments and water-filled nanotubes formed by SOD1 mutant proteins linked to familial ALS Mutations in the SOD1 gene cause the autosomal dominant, neurodegenerative disorder familial amyotrophic lateral sclerosis (FALS). In spinal cord neurons of human FALS patients and in transgenic mice expressing these mutant proteins, aggregates containing FALS SOD1 are observed. Accumulation of SOD1 aggregates is believed to interfere with axonal transport, protein degradation and anti-apoptotic functions of the neuronal cellular machinery. Here we show that metal-deficient, pathogenic SOD1 mutant proteins crystallize in three different crystal forms, all of which reveal higher-order assemblies of aligned beta-sheets. Amyloid-like filaments and water-filled nanotubes arise through extensive interactions between loop and beta-barrel elements of neighboring mutant SOD1 molecules. In all cases, non-native conformational changes permit a gain of interaction between dimers that leads to higher-order arrays. Normal beta-sheet containing proteins avoid such self-association by preventing their edge strands from making intermolecular interactions. 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