Stupfler B, Verriez C, Gallois-Montbrun S, Marquet R, Paillart J C
Degradation-independent inhibition of APOBEC3G by HIV-1 Vif protein Journal Article
In: Viruses, vol. 13, no. 4, pp. 617, 2021.
Abstract | Links | BibTeX | Tags: APOBEC3G, deamination, encapsidation, HIV, MARQUET, PAILLART, proteasome, RNP granules, Translation, ubiquitin, Unité ARN, vif
@article{Stupfler2021,
title = {Degradation-independent inhibition of APOBEC3G by HIV-1 Vif protein},
author = {B Stupfler and C Verriez and S Gallois-Montbrun and R Marquet and J C Paillart},
url = {https://www.mdpi.com/1999-4915/13/4/617},
doi = {10.3390/v13040617},
year = {2021},
date = {2021-01-01},
journal = {Viruses},
volume = {13},
number = {4},
pages = {617},
abstract = {The ubiquitinproteasome system plays an important role in the cell under normal physiological conditions but also during viral infections. Indeed, many auxiliary proteins from the (HIV-1) divert this system to its own advantage, notably to induce the degradation of cellular restriction factors. For instance, the HIV-1 viral infectivity factor (Vif) has been shown to specifically counteract several cellular deaminases belonging to the apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like (APOBEC3 or A3) family (A3A to A3H) by recruiting an E3-ubiquitin ligase complex and inducing their polyubiquitination and degradation through the proteasome. Although this pathway has been extensively characterized so far, Vif has also been shown to impede A3s through degradation-independent processes, but research on this matter remains limited. In this review, we describe our current knowledge regarding the degradation-independent inhibition of A3s, and A3G in particular, by the HIV-1 Vif protein, the molecular mechanisms involved, and highlight important properties of this small viral protein.},
keywords = {APOBEC3G, deamination, encapsidation, HIV, MARQUET, PAILLART, proteasome, RNP granules, Translation, ubiquitin, Unité ARN, vif},
pubstate = {published},
tppubtype = {article}
}
Koltun Bella, Shackelford Eliza, Bonnay François, Matt Nicolas, Reichhart Jean-Marc, Orian Amir
The SUMO-targeted ubiquitin ligase, Dgrn, is essential for Drosophila innate immunity Journal Article
In: The International Journal of Developmental Biology, vol. 61, no. 3-4-5, pp. 319–327, 2017, ISSN: 0214-6282.
Links | BibTeX | Tags: Dgrn, Drosophila, innate immunity, Ligase, M3i, matt, reichhart, SUMO, target, ubiquitin
@article{koltun_sumo-targeted_2017,
title = {The SUMO-targeted ubiquitin ligase, Dgrn, is essential for Drosophila innate immunity},
author = {Bella Koltun and Eliza Shackelford and François Bonnay and Nicolas Matt and Jean-Marc Reichhart and Amir Orian},
url = {http://www.intjdevbiol.com/paper.php?doi=160250ao},
doi = {10.1387/ijdb.160250ao},
issn = {0214-6282},
year = {2017},
date = {2017-01-01},
urldate = {2017-07-12},
journal = {The International Journal of Developmental Biology},
volume = {61},
number = {3-4-5},
pages = {319--327},
keywords = {Dgrn, Drosophila, innate immunity, Ligase, M3i, matt, reichhart, SUMO, target, ubiquitin},
pubstate = {published},
tppubtype = {article}
}
Ferrandon Dominique
Ubiquitin-proteasome: pallbearer carries the deceased to the grave Journal Article
In: Immunity, vol. 27, no. 4, pp. 541–544, 2007, ISSN: 1074-7613.
Abstract | Links | BibTeX | Tags: *Models, Animals, Apoptosis, Apoptosis/*physiology, ferrandon, Immunological, M3i, Macrophages, Macrophages/immunology/metabolism, Models, Phagocytosis, Phagocytosis/*physiology, Proteasome Endopeptidase Complex, Proteasome Endopeptidase Complex/*metabolism, ubiquitin, Ubiquitin/*metabolism
@article{ferrandon_ubiquitin-proteasome:_2007b,
title = {Ubiquitin-proteasome: pallbearer carries the deceased to the grave},
author = {Dominique Ferrandon},
doi = {10.1016/j.immuni.2007.10.003},
issn = {1074-7613},
year = {2007},
date = {2007-10-01},
journal = {Immunity},
volume = {27},
number = {4},
pages = {541--544},
abstract = {Phagocytosis is a complex process that involves multiple cellular functions. In this issue of Immunity, Silva et al. (2007) report that a protein ubiquitylation complex and the proteasome are required for the clearance of apoptotic cells in Drosophila.},
keywords = {*Models, Animals, Apoptosis, Apoptosis/*physiology, ferrandon, Immunological, M3i, Macrophages, Macrophages/immunology/metabolism, Models, Phagocytosis, Phagocytosis/*physiology, Proteasome Endopeptidase Complex, Proteasome Endopeptidase Complex/*metabolism, ubiquitin, Ubiquitin/*metabolism},
pubstate = {published},
tppubtype = {article}
}
Lancelot Nathalie, Elbayed Karim, Bianco Alberto, Piotto Martial
Measurement of scaled residual dipolar couplings in proteins using variable-angle sample spinning Journal Article
In: Journal of biomolecular NMR, vol. 29, no. 3, pp. 259–269, 2004, ISSN: 0925-2738.
Abstract | Links | BibTeX | Tags: 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}
}