Russier Julie, Ménard-Moyon Cécilia, Venturelli Enrica, Gravel Edmond, Marcolongo Gabriele, Meneghetti Moreno, Doris Eric, Bianco Alberto
Oxidative biodegradation of single- and multi-walled carbon nanotubes Article de journal
Dans: Nanoscale, vol. 3, no. 3, p. 893–896, 2011, ISSN: 2040-3372.
Résumé | Liens | BibTeX | Étiquettes: Absorbable Implants, Biocompatible Materials, Body Fluids, carbon, Horseradish Peroxidase, Hydrogen Peroxide, I2CT, Macromolecular Substances, Materials Testing, Molecular Conformation, Nanotubes, Oxidation-Reduction, Particle Size, Surface Properties, Team-Bianco
@article{russier_oxidative_2011,
title = {Oxidative biodegradation of single- and multi-walled carbon nanotubes},
author = {Julie Russier and Cécilia Ménard-Moyon and Enrica Venturelli and Edmond Gravel and Gabriele Marcolongo and Moreno Meneghetti and Eric Doris and Alberto Bianco},
doi = {10.1039/c0nr00779j},
issn = {2040-3372},
year = {2011},
date = {2011-03-01},
journal = {Nanoscale},
volume = {3},
number = {3},
pages = {893--896},
abstract = {In this study we compare the biodegradation of both single-walled (SWCNTs) and multi-walled carbon nanotubes (MWCNTs) using two different oxidative conditions. In particular, we demonstrate that oxidized multi-walled carbon nanotubes are highly degraded, although not to completeness when treated with horseradish peroxidase (HRP) in the presence of hydrogen peroxide.},
keywords = {Absorbable Implants, Biocompatible Materials, Body Fluids, carbon, Horseradish Peroxidase, Hydrogen Peroxide, I2CT, Macromolecular Substances, Materials Testing, Molecular Conformation, Nanotubes, Oxidation-Reduction, Particle Size, Surface Properties, Team-Bianco},
pubstate = {published},
tppubtype = {article}
}
Hipskind R A, Rao V N, Mueller C G, Reddy E S, Nordheim A
Ets-related protein Elk-1 is homologous to the c-fos regulatory factor p62TCF Article de journal
Dans: Nature, vol. 354, no. 6354, p. 531–534, 1991, ISSN: 0028-0836.
Résumé | Liens | BibTeX | Étiquettes: Animals, Antibodies, Base Sequence, Binding Sites, DNA, DNA-Binding Proteins, Epitopes, Escherichia coli, ets-Domain Protein Elk-1, fos, Genes, Genetic, Immune Sera, Macromolecular Substances, Molecular Sequence Data, Mutagenesis, Nucleic Acid, Oligodeoxyribonucleotides, Oncogenic, Promoter Regions, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-ets, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Retroviridae Proteins, Saccharomyces cerevisiae, Sequence Homology, Site-Directed, Team-Mueller, Transcription Factors, Transfection
@article{hipskind_ets-related_1991,
title = {Ets-related protein Elk-1 is homologous to the c-fos regulatory factor p62TCF},
author = {R A Hipskind and V N Rao and C G Mueller and E S Reddy and A Nordheim},
doi = {10.1038/354531a0},
issn = {0028-0836},
year = {1991},
date = {1991-12-01},
journal = {Nature},
volume = {354},
number = {6354},
pages = {531--534},
abstract = {A key event in the response of cells to proliferative signals is the rapid, transient induction of the c-fos proto-oncogene, which is mediated through the serum response element (SRE) in the fos promoter. Genomic footprinting and transfection experiments suggest that this activation occurs through a ternary complex that includes the serum response factor (SRF) and the ternary complex factor p62. Interaction of p62TCF with the SRF-SRE binary complex requires a CAGGA tract immediately upstream of the SRE. Proteins of the ets proto-oncogene family bind to similar sequences and we have found that a member of this family, Elk-1, forms SRF-dependent ternary complexes with the SRE. Elk-1 and p62TCF have the same DNA sequence requirements and antibodies against Elk-1 block the binding of both proteins. Furthermore, we show that like p62TCF, Elk-1 forms complexes with the yeast SRF-homologue MCM1 but not with yeast ARG80. But ARG80 mutants that convey interaction with p62TCF can also form complexes with Elk-1. The similarity, or even identity, between Elk-1 and p62TCF suggests a novel regulatory role for Ets proteins that is effected through interaction with other proteins, such as SRF. Furthermore, the possible involvement of an Ets protein in the control of c-fos has interesting implications for proto-oncogene cooperation in cellular growth control.},
keywords = {Animals, Antibodies, Base Sequence, Binding Sites, DNA, DNA-Binding Proteins, Epitopes, Escherichia coli, ets-Domain Protein Elk-1, fos, Genes, Genetic, Immune Sera, Macromolecular Substances, Molecular Sequence Data, Mutagenesis, Nucleic Acid, Oligodeoxyribonucleotides, Oncogenic, Promoter Regions, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-ets, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Retroviridae Proteins, Saccharomyces cerevisiae, Sequence Homology, Site-Directed, Team-Mueller, Transcription Factors, Transfection},
pubstate = {published},
tppubtype = {article}
}
Schröter H, Mueller C G, Meese K, Nordheim A
Synergism in ternary complex formation between the dimeric glycoprotein p67SRF, polypeptide p62TCF and the c-fos serum response element Article de journal
Dans: The EMBO journal, vol. 9, no. 4, p. 1123–1130, 1990, ISSN: 0261-4189.
Résumé | BibTeX | Étiquettes: Base Sequence, Chloroquine, Gene Expression Regulation, Genetic, Glycosylation, HeLa Cells, Humans, Kinetics, Macromolecular Substances, Molecular Sequence Data, Nuclear Proteins, Oligonucleotide Probes, Plasmids, Polymerase Chain Reaction, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Serum Response Factor, Team-Mueller, Transcription, Transcription Factors
@article{schroter_synergism_1990,
title = {Synergism in ternary complex formation between the dimeric glycoprotein p67SRF, polypeptide p62TCF and the c-fos serum response element},
author = {H Schröter and C G Mueller and K Meese and A Nordheim},
issn = {0261-4189},
year = {1990},
date = {1990-04-01},
journal = {The EMBO journal},
volume = {9},
number = {4},
pages = {1123--1130},
abstract = {Transcriptional regulation of the c-fos proto-oncogene requires the serum response element (SRE) which is complexed by a multi-protein assembly observed both in vitro and in vivo. Two protein factors, p67SRF and p62TCF (previously called p62), are required to interact with the SRE for efficient induction of c-fos by serum. By quantitative band shift electrophoresis we measure at least a 50-fold increase in SRE affinity for p67SRF/p62TCF over p67SRF alone. Stoichiometrically we determine that the ternary complex with p62TCF involves p67SRF in dimeric form. We demonstrate that p67SRF is a glycosylated nuclear transcription factor carrying terminal N-acetylglucosamine (GlcNAc) as a post-translational modification. A proteolytic limit digestion product, approximately 13 kd in size, was generated from the p67SRF-SRE complex. This p67SRF-core domain binds SRE, can dimerize with p67SRF and is still able to form a ternary complex with p62TCF. Therefore, three functional activities can be ascribed to this small p67SRF-core domain: specific DNA binding, dimerization and interaction with p62TCF. We demonstrate that these functions map within the p67SRF core fragment containing the region between amino acids 93 and 222.},
keywords = {Base Sequence, Chloroquine, Gene Expression Regulation, Genetic, Glycosylation, HeLa Cells, Humans, Kinetics, Macromolecular Substances, Molecular Sequence Data, Nuclear Proteins, Oligonucleotide Probes, Plasmids, Polymerase Chain Reaction, Protein-Tyrosine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-fos, Proto-Oncogenes, Serum Response Factor, Team-Mueller, Transcription, Transcription Factors},
pubstate = {published},
tppubtype = {article}
}