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2006
Campidelli Stéphane, Klumpp Cédric, Bianco Alberto, Guldi Dirk M, Prato Maurizio
Functionalization of CNT: synthesis and applications in photovoltaics and biology Journal Article
In: Journal of Physical Organic Chemistry, vol. 19, no. 8-9, pp. 531–539, 2006, ISSN: 1099-1395.
Abstract | Links | BibTeX | Tags: Carbon nanotubes, Cells, Drug delivery, electron transfer, Functionalization, I2CT, Peptides, photovoltaic, Team-Bianco, Toxicity, Vectors
@article{campidelli_functionalization_2006,
title = {Functionalization of CNT: synthesis and applications in photovoltaics and biology},
author = {Stéphane Campidelli and Cédric Klumpp and Alberto Bianco and Dirk M Guldi and Maurizio Prato},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/poc.1052},
doi = {10.1002/poc.1052},
issn = {1099-1395},
year = {2006},
date = {2006-01-01},
urldate = {2020-03-31},
journal = {Journal of Physical Organic Chemistry},
volume = {19},
number = {8-9},
pages = {531--539},
abstract = {Here, we review part of the work carried out in our laboratories on carbon nanotube functionalization. Both covalent (sidewall derivatization) and non-covalent (using π-π interactions) functionalization have been used to solubilize carbon nanotubes (NTs). The combination of NTs with various electron donors, mainly using the supramolecular approach, led to a new generation of donor-acceptor nanohybrids which can be used for the development of carbon-based photovoltaic cells. Covalent functionalization has been successfully applied for preparation of water soluble nanotubes and further derivatization of the nanotubes with bioactive molecules hold great promise for application in drug, vaccine and gene delivery. Copyright © 2006 John Wiley & Sons, Ltd.},
keywords = {Carbon nanotubes, Cells, Drug delivery, electron transfer, Functionalization, I2CT, Peptides, photovoltaic, Team-Bianco, Toxicity, Vectors},
pubstate = {published},
tppubtype = {article}
}
Here, we review part of the work carried out in our laboratories on carbon nanotube functionalization. Both covalent (sidewall derivatization) and non-covalent (using π-π interactions) functionalization have been used to solubilize carbon nanotubes (NTs). The combination of NTs with various electron donors, mainly using the supramolecular approach, led to a new generation of donor-acceptor nanohybrids which can be used for the development of carbon-based photovoltaic cells. Covalent functionalization has been successfully applied for preparation of water soluble nanotubes and further derivatization of the nanotubes with bioactive molecules hold great promise for application in drug, vaccine and gene delivery. Copyright © 2006 John Wiley & Sons, Ltd.
2004
Martineau Y., Bec C. Le, Monbrun L., Allo V., Chiu I. M., Danos O., Moine H., Prats H., Prats A. C.
Internal ribosome entry site structural motifs conserved among mammalian fibroblast growth factor 1 alternatively spliced mRNAs Journal Article
In: Mol Cell Biol, vol. 24, no. 17, pp. 7622-35, 2004, (0270-7306 Journal Article).
Abstract | BibTeX | Tags: (Genetics), *5', *Alternative, *Nucleic, *Promoter, 1/*genetics, Acid, Alignment, Animals, Base, Cell, Conformation, Data, EHRESMANN, Factor, Fibroblast, Gene, Genes, Genetic, Gov't, Growth, Human, Line, Messenger/chemistry/*genetics/metabolism, Mice, Molecular, Muscle, Mutagenesis, Non-U.S., Regions, Ribosomes/*metabolism, RNA, Sequence, Site-Directed, Skeletal/cytology/physiology, Splicing, Structural/genetics, Support, Techniques, Transfer, Untranslated, Vectors
@article{,
title = {Internal ribosome entry site structural motifs conserved among mammalian fibroblast growth factor 1 alternatively spliced mRNAs},
author = { Y. Martineau and C. Le Bec and L. Monbrun and V. Allo and I. M. Chiu and O. Danos and H. Moine and H. Prats and A. C. Prats},
year = {2004},
date = {2004-01-01},
journal = {Mol Cell Biol},
volume = {24},
number = {17},
pages = {7622-35},
abstract = {Fibroblast growth factor 1 (FGF-1) is a powerful angiogenic factor whose gene structure contains four promoters, giving rise to a process of alternative splicing resulting in four mRNAs with alternative 5' untranslated regions (5' UTRs). Here we have identified, by using double luciferase bicistronic vectors, the presence of internal ribosome entry sites (IRESs) in the human FGF-1 5' UTRs, particularly in leaders A and C, with distinct activities in mammalian cells. DNA electrotransfer in mouse muscle revealed that the IRES present in the FGF-1 leader A has a high activity in vivo. We have developed a new regulatable TET OFF bicistronic system, which allowed us to rule out the possibility of any cryptic promoter in the FGF-1 leaders. FGF-1 IRESs A and C, which were mapped in fragments of 118 and 103 nucleotides, respectively, are flexible in regard to the position of the initiation codon, making them interesting from a biotechnological point of view. Furthermore, we show that FGF-1 IRESs A of murine and human origins show similar IRES activity profiles. Enzymatic and chemical probing of the FGF-1 IRES A RNA revealed a structural domain conserved among mammals at both the nucleotide sequence and RNA structure levels. The functional role of this structural motif has been demonstrated by point mutagenesis, including compensatory mutations. These data favor an important role of IRESs in the control of FGF-1 expression and provide a new IRES structural motif that could help IRES prediction in 5' UTR databases.},
note = {0270-7306
Journal Article},
keywords = {(Genetics), *5', *Alternative, *Nucleic, *Promoter, 1/*genetics, Acid, Alignment, Animals, Base, Cell, Conformation, Data, EHRESMANN, Factor, Fibroblast, Gene, Genes, Genetic, Gov't, Growth, Human, Line, Messenger/chemistry/*genetics/metabolism, Mice, Molecular, Muscle, Mutagenesis, Non-U.S., Regions, Ribosomes/*metabolism, RNA, Sequence, Site-Directed, Skeletal/cytology/physiology, Splicing, Structural/genetics, Support, Techniques, Transfer, Untranslated, Vectors},
pubstate = {published},
tppubtype = {article}
}
Fibroblast growth factor 1 (FGF-1) is a powerful angiogenic factor whose gene structure contains four promoters, giving rise to a process of alternative splicing resulting in four mRNAs with alternative 5' untranslated regions (5' UTRs). Here we have identified, by using double luciferase bicistronic vectors, the presence of internal ribosome entry sites (IRESs) in the human FGF-1 5' UTRs, particularly in leaders A and C, with distinct activities in mammalian cells. DNA electrotransfer in mouse muscle revealed that the IRES present in the FGF-1 leader A has a high activity in vivo. We have developed a new regulatable TET OFF bicistronic system, which allowed us to rule out the possibility of any cryptic promoter in the FGF-1 leaders. FGF-1 IRESs A and C, which were mapped in fragments of 118 and 103 nucleotides, respectively, are flexible in regard to the position of the initiation codon, making them interesting from a biotechnological point of view. Furthermore, we show that FGF-1 IRESs A of murine and human origins show similar IRES activity profiles. Enzymatic and chemical probing of the FGF-1 IRES A RNA revealed a structural domain conserved among mammals at both the nucleotide sequence and RNA structure levels. The functional role of this structural motif has been demonstrated by point mutagenesis, including compensatory mutations. These data favor an important role of IRESs in the control of FGF-1 expression and provide a new IRES structural motif that could help IRES prediction in 5' UTR databases.
