Lancelot Nathalie, Elbayed Karim, Bianco Alberto, Piotto Martial
Measurement of scaled residual dipolar couplings in proteins using variable-angle sample spinning Article de journal
Dans: Journal of biomolecular NMR, vol. 29, no. 3, p. 259–269, 2004, ISSN: 0925-2738.
Résumé | Liens | BibTeX | Étiquettes: anisotropy, I2CT, Magnetic Resonance Spectroscopy, Magnetics, Models, Phospholipid Ethers, Proteins, Statistical, Team-Bianco, Temperature, ubiquitin
@article{lancelot_measurement_2004,
title = {Measurement of scaled residual dipolar couplings in proteins using variable-angle sample spinning},
author = {Nathalie Lancelot and Karim Elbayed and Alberto Bianco and Martial Piotto},
doi = {10.1023/B:JNMR.0000032548.60663.1f},
issn = {0925-2738},
year = {2004},
date = {2004-07-01},
journal = {Journal of biomolecular NMR},
volume = {29},
number = {3},
pages = {259--269},
abstract = {NMR spectra of ubiquitin in the presence of bicelles at a concentration of 25% w/v have been recorded under sample spinning conditions for different angles of rotation. For an axis of rotation equal to the magic angle, the (1)H/(15)N HSQC recorded without any (1)H decoupling in the indirect dimension corresponds to the classical spectrum obtained on a protein in an isotropic solution and allows the measurement of scalar J-couplings (1) J (NH). For an angle of rotation smaller than the magic angle, the bicelles orient with their normal perpendicular to the spinning axis, whereas for an angle of rotation greater than the magic angle the bicelles orient with their normal along the spinning axis. This bicelle alignment creates anisotropic conditions that give rise to the observation of residual dipolar couplings in ubiquitin. The magnitude of these dipolar couplings depends directly on the angle that the rotor makes with the main magnetic field. By changing this angle in a controlled manner, residual dipolar couplings can be either scaled up or down thus offering the possibility to study simultaneously a wide range of dipolar couplings in the same sample.},
keywords = {anisotropy, I2CT, Magnetic Resonance Spectroscopy, Magnetics, Models, Phospholipid Ethers, Proteins, Statistical, Team-Bianco, Temperature, ubiquitin},
pubstate = {published},
tppubtype = {article}
}
Nisole S, Krust B, Callebaut C, Guichard G, Muller S, Briand J P, Hovanessian A G
The anti-HIV pseudopeptide HB-19 forms a complex with the cell-surface-expressed nucleolin independent of heparan sulfate proteoglycans Article de journal
Dans: The Journal of Biological Chemistry, vol. 274, no. 39, p. 27875–27884, 1999, ISSN: 0021-9258.
Résumé | Liens | BibTeX | Étiquettes: Anti-HIV Agents, Binding Sites, CD4-Positive T-Lymphocytes, Cell Line, Cell Membrane, Confocal, Fibroblast Growth Factor 2, Flow Cytometry, Heparan Sulfate Proteoglycans, HIV-1, Humans, Microscopy, Oligopeptides, Peptides, Phospholipid Ethers, Phosphoproteins, Proteins, RNA-Binding Proteins
@article{nisole_anti-hiv_1999,
title = {The anti-HIV pseudopeptide HB-19 forms a complex with the cell-surface-expressed nucleolin independent of heparan sulfate proteoglycans},
author = {S Nisole and B Krust and C Callebaut and G Guichard and S Muller and J P Briand and A G Hovanessian},
doi = {10.1074/jbc.274.39.27875},
issn = {0021-9258},
year = {1999},
date = {1999-09-01},
journal = {The Journal of Biological Chemistry},
volume = {274},
number = {39},
pages = {27875--27884},
abstract = {The HB-19 pseudopeptide 5[Kpsi(CH(2)N)PR]-TASP, psi(CH(2)N) for reduced peptide bond, is a specific inhibitor of human immunodeficiency virus (HIV) infection in different CD4(+) cell lines and in primary T-lymphocytes and macrophages. Here, by using an experimental CD4(+) cell model to monitor HIV entry and infection, we demonstrate that HB-19 binds the cell surface and inhibits attachment of HIV particles to permissive cells. At concentrations that inhibit HIV attachment, HB-19 binds cells irreversibly, becomes complexed with the cell-surface-expressed nucleolin, and eventually results in its degradation. Accordingly, by confocal immunofluorescence microscopy, we demonstrate the drastic reduction of the cell-surface-expressed nucleolin following treatment of cells with HB-19. HIV particles can prevent the binding of HB-19 to cells and inhibit complex formation with nucleolin. Such a competition between viral particles and HB-19 is consistent with the implication of nucleolin in the process of HIV attachment to target cells. We show that another inhibitor of HIV infection, the fibroblast growth factor-2 (FGF-2) that uses cell-surface-expressed heparan sulfate proteoglycans as low affinity receptors, binds cells and blocks attachment of HIV to permissive cells. FGF-2 does not prevent the binding of HB-19 to cells and to nucleolin, and similarly HB-19 has no apparent effect on the binding of FGF-2 to the cell surface. The lack of competition between these two anti-HIV agents rules out the potential involvement of heparan sulfate proteoglycans in the mechanism of anti-HIV effect of HB-19, thus pointing out that nucleolin is its main target.},
keywords = {Anti-HIV Agents, Binding Sites, CD4-Positive T-Lymphocytes, Cell Line, Cell Membrane, Confocal, Fibroblast Growth Factor 2, Flow Cytometry, Heparan Sulfate Proteoglycans, HIV-1, Humans, Microscopy, Oligopeptides, Peptides, Phospholipid Ethers, Phosphoproteins, Proteins, RNA-Binding Proteins},
pubstate = {published},
tppubtype = {article}
}