WorldCat Identities

Saïb, Ali 19..- ...

Overview
Works: 45 works in 57 publications in 4 languages and 175 library holdings
Genres: Criticism, interpretation, etc  Academic theses 
Roles: Editor, Contributor, Thesis advisor, Author, Scenarist, Scientific advisor, Opponent, Other
Classifications: PJ7755.H3, 579.2
Publication Timeline
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Most widely held works by Ali Saïb
Panorama de la virologie( Book )

1 edition published in 2013 in French and held by 87 WorldCat member libraries worldwide

Docteur Virus et Mister Hyde : mémoires d'un virologiste by Jean Crépu( Visual )

1 edition published in 2006 in French and held by 7 WorldCat member libraries worldwide

Dr. Virus et M. Hyde : mémoires d'un virologiste( Visual )

1 edition published in 2006 in French and held by 6 WorldCat member libraries worldwide

Voilà plus d'un siècle que les scientifiques cherchent à comprendre le monde des virus. Ils furent associés la plupart du temps à des maladies. Le documentaire révèle une face cachée, un rôle positif des virus dans l'organisme
Sharḥ mā fī al-Maqāmāt al-Ḥarīrīyah min al-alfāẓ al-lughawīyah by ʻAbd Allāh ibn al-Ḥusayn ʻUkbarī( Book )

in Arabic and held by 4 WorldCat member libraries worldwide

Etude des modifications post-traductionnelles des protéines du VIH-1, dans les cellules quiescentes, au cours des étapes précoces de la réplication by Audrey Coiffic( Book )

2 editions published in 2011 in French and held by 3 WorldCat member libraries worldwide

In our laboratory we study the hypothesis according to which incoming HIV-1 concentrates and persists at the centrosome in infected quiescent T lymphocytes, in order to be able to hijack the cellular machineries upon cellular reactivation and, especially, following centrosome duplication, to resume its replication cycle. Posttranslational modifications taking place at this site, such as phosphorylation and SUMOylation, could be exploited by the virus and might contribute to the completion/recommencement of viral replication. Components of the SUMOylation machinery have been shown to be necessary for HIV-1 replication, encouraging our study on SUMOylation of integrase (IN) protein during the early steps of HIV-1 infection. By analyzing HIV-1 integrase sequences we identified three SUMOylation consensus sites. HIV-1 I orchestrates the irreversible insertion of the reverse transcribed viral cDNA into the host cell genome, but participates also in other steps of HIV-1 replication. Cellular and viral factors assist IN in performing it multiple functions, and post-translational modifications contribute to modulate its activities. Here, we report that HIV-1 IN is modified by SUMO proteins and that phylogenetically conserved SUMOylation consensu motifs represent the major SUMO-acceptor sites. We also found that viruses harboring SUMOylation defective IN mutants displayed a replication defect that was mapped at an early step(s), before integratioi but after reverse transcription. Since SUMOylation-site IN mutants retained WT catalytic activity, we hypothesize that IN SUMOylation might regulate its affinity for important co-factors, contributing to the optimal execution of an early step(s) of HIV-1 replication
Sharḥ mā fī al-Maqāmāt al-Ḥarīrīyah min al-alfāẓ al-lughawīyah by ʻAbd Allāh ibn al-Ḥusayn ʻUkbarī( Book )

3 editions published in 1975 in Arabic and held by 3 WorldCat member libraries worldwide

Trafic intracellulaire de la protéine Gag du virus Foamy by Noémie Renault( Book )

2 editions published in 2009 in French and held by 3 WorldCat member libraries worldwide

Foamy viruses (FVs) are complex exogenous animal retroviruses that differ in many aspects of their life cycle from the orthoretroviruses such as human immunodefîciency virus (HIV). In particular, in FVvs, Gag and Pol proteins are expressed independently of one another, and both proteins undergo single clivage events. None of the conventional Gag landmarks of exogenous retroviruses, such as the major homology region or Cys-His motifs, are found in this protein. Instead, FV Gag harbors conserved C-terminal basic motifs, referred to as Gly-Arg (GR) boxes. Although the first GR (GRI) box binds viral nucleic acids and is required for viral genome packaging, the second (GRII) harbors a nuclear localization sequence (NLS) at its C-terminus, targeting Gag to the nucleus early after infection. GRII also contains a chromatin binding sequence (CBS) in its N-terminus, tethering the FV incoming pre-integration complex onto host chromosomes.The present work focuses on the structural Gag proteins, in early and late stages of infection. troviral Gag proteins are involved in early stages of infection such as trafficking of incoming viruses nd nuclear import. FV Gag protein uses the microtubule network to reach the nucleus. In cycling cells,FV articles are structured at the centrosome 4 h post-infection. Then, the viral protease helps capsid for ncoating. In quiescent cells, we have shown that viral particles remain structured at the centrosome during everal weeks and that uncoating does not occur : this step is a limiting factor for infection although viral articles are still infectious. Upon cells reactivation, viral capsids undergo proteolysis and disassembly, llowing infection to proceed. During the late stages of infection, Gag undergoes transient nuclear trafficking after it synthesis, before returning back to the cytoplasm for capsid assembly and virus egress. The functional role of this nuclear stage, as well as the molecular mechanisms responsible for Gag nuclear export, are not understood. Here, we identify a leptomycin-sensitive nuclear export sequence (NES) within the N-terminus of the primate foamy virus Gag protein that is absolutely required for the completion of late stages of virus replication. Point mutation of conserved residues within this motif leads to nuclear retention of Gag and dramatically affects viral replication. Moreover, complementation experiments demonstrate that nuclear export-defective Gag mutants negatively interfere with virus release by sequestering wild-type Gag in the nucleus
Trafic intranucléaire du rétrovirus Foamy by Joris Paris( Book )

2 editions published in 2014 in French and held by 2 WorldCat member libraries worldwide

The structural Gag protein hijacks many cellular machineries to fulfill its distinct and fundamental roles in the replication of retroviruses. In the case of the prototype foamy virus (PFV), Gag contains a nuclear export signal (NES) which allows the gRNA-Gag complex to be exported to the cytoplasm prior to capsids assembly and virus egress. We identified a nucleolar localization sequence (NoLS) in the C-terminus of PFV Gag. This NoLS contains two regions, rich in arginine and glycine, which are necessary and sufficient for nucleolar targeting. The methylation of Arginine R540 by PRMT-1 regulates the functions NoLS vs CBS of Gag. To study the nucleolar step of PFV replication, we used different conditions that slow down intracellular trafficking (hypoxia and/or treatment with leptomycin B) and also a molecular trap system to retain Gag into the nucleolus. In both cases, Gag was detected in the nucleolus. We also developed an approach, based on a ribozyme fused to a snoRNA able to cleave specifically PFV gRNA in the nucleolus
A nuclear export signal within the structural Gag protein is required for prototype foamy virus replication by Noemie Renault( )

1 edition published in 2011 in English and held by 2 WorldCat member libraries worldwide

Docteur Virus & Mister Hyde : mémoires d'un virologiste by Jean Crépu( Visual )

2 editions published between 2006 and 2009 in French and held by 2 WorldCat member libraries worldwide

Ǧogrâfîja-je mufaṣṣal-i memâlik-i dewlet-i 'otmanijje eter 'Alî Sa'ib by ʻAlī Ṣāʼib( Book )

1 edition published in 1304 in Undetermined and held by 2 WorldCat member libraries worldwide

Dual inhibition of HIV-1 replication by integrase-LEDGF allosteric inhibitors is predominant at the post-integration stage by Erwann Le Rouzic( )

1 edition published in 2013 in English and held by 2 WorldCat member libraries worldwide

Integrase and integration: biochemical activities of HIV-1 integrase by Olivier Delelis( )

1 edition published in 2008 in English and held by 2 WorldCat member libraries worldwide

Cografya-yi mufassal by ʻAlī Ṣāʼib( Book )

2 editions published in 1886 in Turkish and held by 2 WorldCat member libraries worldwide

Tax ubiquitylation and SUMOylation control the dynamic shuttling of Tax and NEMO between Ubc9 nuclear bodies and the centrosome by Youmna Kfoury( )

1 edition published in 2011 in English and held by 2 WorldCat member libraries worldwide

Etude des mécanismes moléculaires responsables de la persistance des virus foamy by Charles-Henri Lecellier( Book )

2 editions published in 2004 in French and held by 2 WorldCat member libraries worldwide

Early steps of retrovirus replicative cycle by Sébastien Nisole( )

1 edition published in 2004 in English and held by 2 WorldCat member libraries worldwide

Implication des modifications post-traductionnelles des protéines virales dans les étapes précoces du cycle réplicatif du VIH-1 by Guillaume Beauclair( Book )

2 editions published in 2013 in French and held by 2 WorldCat member libraries worldwide

Viruses hijack cellular machineries to replicate. Post-translational modifications pathways are no exception. In the laboratory, we are interested in the interplay between the SUMOylation pathway and HIV-1. SUMOylation involves the covalent binding of SUMO proteins to a lysine residue within a target protein. This post-translational modification plays a key role in many fundamental processes such as transcription and innate immunity. We showed that HIV-1 integrase (IN), the viral enzyme that catalyzes integration of the viral genome into the host cell chromosomes, is SUMOylated and that virions harboring SUMOylation-deficient IN mutants are less infectious than wild-type viruses, indicating that this modification is important for efficient viral replication. To further characterize the interplay between HIV-1 and the SUMOylation pathway, we have investigated in this work the involvement of cellular enzymes responsible of SUMO conjugation. We established that IN interacts and co-localizes with several PIAS family members (E3 SUMO ligases). Among others, PIAS3 was found to enhance IN SUMOylation. We also observed that the amount of endogenous PIAS3 is decreased upon an infection, suggesting a possible role for this protein during the replicative cycle. We also demonstrated the existence of a new splice variant of PIAS3, which has an increase E3 SUMO ligase activity on IN. These results could have many implications since PIAS3 regulates the activity and the functions of STAT3 and RelA/p65. Finally, the experimental work has been complemented by the development of a bioinformatics tool that detects SUMOylation sites and SIM present in proteins
Centrosome and retroviruses: The dangerous liaisons by Philippe V Afonso( )

1 edition published in 2007 in English and held by 2 WorldCat member libraries worldwide

The invariant arginine within the chromatin-binding motif regulates both nucleolar localization and chromatin binding of Foamy virus Gag by Joris Paris( )

1 edition published in 2018 in English and held by 2 WorldCat member libraries worldwide

 
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Audience level: 0.90 (from 0.75 for Sharḥ mā ... to 0.97 for Cografya-y ...)

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