Roland Marquet
Onglets principaux
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Publication de Roland Marquet
- Evaluation of anti-HIV-1 mutagenic nucleoside analogues.
- Importance of Modified Nucleotides in Replication of Retroviruses, Plant Pararetroviruses, and Retrotransposons
- Scientific Correspondence
- Empaquetage sélectif du génome des influenzavirus A
- Oligonucleotide-Mediated Inhibition of Genomic RNA Dimerization of HIV-1 Strains MAL and LAI: A Comparative Analysis
- Mutational interference mapping experiment (MIME) for studying RNA structure and function.
- HIV-1 polymerase inhibition by nucleoside analogs: cellular- and kinetic parameters of efficacy, susceptibility and resistance selection.:
- A structure-based approach for targeting the HIV-1 genomic RNA dimerization initiation site
- Selective packaging of the influenza A genome and consequences for genetic reassortment.
- Solution studies of the dimerization initiation site of HIV-1 genomic RNA
- Specific recognition of the HIV-1 genomic RNA by the Gag precursor.
- Synthesis of a Neamine Dimer Targeting the Dimerization Initiation Site of HIV-1 RNA
- In cell mutational interference mapping experiment (in cell MIME) identifies the 5′ polyadenylation signal as a dual regulator of HIV-1 genomic RNA production and packaging
- The HIV-1 ribonucleoprotein dynamically regulates its condensate behavior and drives acceleration of protease activity through membrane-less granular phase-separation
- The C-terminal p6 domain of the HIV-1 Pr55Gag precursor is required for specific binding to the genomic RNA
- The C-terminal p6 domain of the HIV-1 Pr55<sup>Gag</sup> precursor is required for specific binding to the genomic RNA.
- The evolution of RNA structural probing methods: From gels to next-generation sequencing
- Initiation of Reverse Transcripion of HIV-1: Secondary Structure of the HIV-1 RNA/tRNA|rlmbopopnbop|Lys|clobop|3 (Template/Primer) Complex
- 8-Modified-2'-Deoxyadenosine Analogues Induce Delayed Polymerization Arrest during HIV-1 Reverse Transcription.
- Direct and Indirect Contributions of RNA Secondary Structure Elements to the Initiation of HIV-1 Reverse Transcription
- Initiation of HIV Reverse Transcription
- Dynamics of the HIV-1 Reverse Transcription Complex during Initiation of DNA Synthesis
- Structural basis for the specificity of the initiation of HIV‐1 reverse transcription
- Contacts between Reverse Transcriptase and the Primer Strand Govern the Transition from Initiation to Elongation of HIV-1 Reverse Transcription
- HIV-1 replication and the cellular eukaryotic translation apparatus
- Post-Translational Modifications of Retroviral HIV-1 Gag Precursors: An Overview of Their Biological Role
- Mutational analysis of the tRNA3Lys/HIV-1 RNA (primer/template) complex
- Determining the conformation of RNAs in solution. Application to a retroviral system: structure of the HIV-1 primer binding site region and effect of tRNA3Lys binding
- NMR and biochemical characterization of recombinant human tRNA3Lys expressed in Escherichia coli: Identification of posttranscriptional nucleotide modifications required for efficient initiation of HIV-1 reverse transcription
- Effects of tRNA3Lys aminoacylation on the initiation of HIV-1 reverse transcription
- Hijacking of the Ubiquitin/Proteasome Pathway by the HIV Auxiliary Proteins
- Primer Unblocking and Rescue of DNA Synthesis by Azidothymidine (AZT)-resistant HIV-1 Reverse Transcriptase COMPARISON BETWEEN INITIATION AND ELONGATION OF REVERSE TRANSCRIPTION AND BETWEEN (−) AND (+) STRAND DNA SYNTHESIS
- Structural Variability of the Initiation Complex of HIV-1 Reverse Transcription
- APOBEC3G impairs the multimerization of the HIV-1 Vif protein in living cells
- The role of Vif oligomerization and RNA chaperone activity in HIV-1 replication.
- Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 Vif
- APOBEC3F/G and Vif: action and counteractions.:
- Degradation-Independent Inhibition of APOBEC3G by the HIV-1 Vif Protein
- Un facteur de transcription se fait complice du VIH-1 pour détruire les défenses cellulaires. [A transcription factor acts as a HIV-1 accomplice to destroy the cellular defences].
- Initiation of HIV-1 reverse transcription and functional role of nucleocapsid-mediated tRNA/viral genome interactions.
- Functional Sites in the 5′ Region of Human Immunodeficiency Virus Type 1 RNA Form Defined Structural Domains
- Structural and functional motifs in influenza virus RNAs
- A supramolecular assembly formed by influenza A virus genomic RNA segments.
- A functional sequence-specific interaction between influenza A virus genomic RNA segments
- Expression, purification, and characterization of biologically active full-length Mason-Pfizer monkey virus (MPMV) Pr78Gag
- The bifurcated stem loop 4 (SL4) is crucial for efficient packaging of mouse mammary tumor virus (MMTV) genomic RNA
- Structure–function relationships of the initiation complex of HIV‐1 reverse transcription: the case of mutant viruses using tRNAHis as primer
- Psoralen Crosslinking between Human Immunodeficiency Virus Type 1 RNA and Primer tRNA 3Lys
- Structural basis of genomic RNA (gRNA) dimerization and packaging determinants of mouse mammary tumor virus (MMTV).
- Critical role of segment-specific packaging signals in genetic reassortment of influenza A viruses.
- Interaction network linking the human H3N2 influenza A virus genomic RNA segments.
- Purification and Functional Characterization of a Biologically Active Full-Length Feline Immunodeficiency Virus (FIV) Pr50<sup>Gag</sup>.
- Packaging of Mason-Pfizer Monkey Virus (MPMV) Genomic RNA Depends upon Conserved Long Range Interactions (LRIs) Between U5 and gag Sequences.
- Biochemical and Functional Characterization of Mouse Mammary Tumor Virus Full-Length Pr77Gag Expressed in Prokaryotic and Eukaryotic Cells
- SHAPE analysis of the 5' end of the Mason-Pfizer monkey virus (MPMV) genomic RNA reveals structural elements required for genome dimerization.
- Role of Purine-Rich Regions in Mason-Pfizer Monkey Virus (MPMV) Genomic RNA Packaging and Propagation
- Identification of Pr78Gag binding sites on the Mason-Pfizer monkey virus genomic RNA packaging determinants
- Binding of the HIV-1 Nucleocapsid Protein to the Primer tRNA, inVitro, Is Essentially Not Specific
- In vitro evidence for the interaction of tRNA3Lys with U3 during the first strand transfer of HIV-1 reverse transcription
- Probing the higher order structure of RNA with peroxonitrous acid
- An in vitro network of intermolecular interactions between viral RNA segments of an avian H5N2 influenza A virus: comparison with a human H3N2 virus
- Labeling of multiple HIV-1 proteins with the biarsenical-tetracysteine system
- A pyrophosphatase activity associated with purified HIV-1 particles.
- Does the HIV‐1 primer activation signal interact with tRNA3Lys during the initiation of reverse transcription?
- Identification of the in Vitro HIV-2/SIV RNA Dimerization Site Reveals Striking Differences with HIV-1
- Inhibition of the Initiation of HIV-1 Reverse Transcription by 3′-Azido-3′-deoxythymidine COMPARISON WITH ELONGATION
- Stabilizing Role of Structural Elements within the 5´ Untranslated Region (UTR) and Gag Sequences in Mason-Pfizer monkey virus (MPMV) Genomic RNA Packaging
- Zinc Fingers in HIV-1 Gag Precursor Are Not Equivalent for gRNA Recruitment at the Plasma Membrane
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