J. Paillart

发表

APOBEC3G Impairs the Multimerization of the HIV-1 Vif Protein in Living Cells

Y. Mély, L. Richert, H. de Rocquigny, 2013, Journal of Virology.

the HIV-1 Vif Protein in Living Cells APOBEC3G Impairs the Multimerization of

Y. Mély, L. Richert, Santiago Guerrero, 2013 .

A supramolecular assembly formed by influenza A virus genomic RNA segments

C. Isel, A. Cavalier, Daniel Thomas, 2011, Nucleic acids research.

Mechanisms of Inhibition of in Vitro Dimerization of HIV Type I RNA by Sense and Antisense Oligonucleotides*

C. Ehresmann, M. Blumenfeld, B. Ehresmann, 1996, The Journal of Biological Chemistry.

The evolution of RNA structural probing methods: From gels to next‐generation sequencing

R. Smyth, V. Vivet-Boudou, R. Marquet, 2018, Wiley interdisciplinary reviews. RNA.

Extensive uORF translation from HIV-1 transcripts conditions DDX3 dependency for expression of main ORFs and elicits specific T cell immune responses in infected individuals

O. Namy, A. Samri, B. Autran, 2022, bioRxiv.

CTIP2 is a negative regulator of P-TEFb

F. Dequiedt, C. Van Lint, X. Graña, 2013, Proceedings of the National Academy of Sciences.

Structural Variability of the Initiation Complex of HIV-1 Reverse Transcription*

C. Ehresmann, B. Ehresmann, Valérie Goldschmidt, 2004, Journal of Biological Chemistry.

The role of Vif oligomerization and RNA chaperone activity in HIV-1 replication.

C. Gabus, J. Darlix, S. Bernacchi, 2012, Virus research.

Dynamic nanopore long-read sequencing analysis of HIV-1 splicing events during the early steps of infection

S. Emiliani, Sophie Lemoine, C. Blugeon, 2020, Retrovirology.

Importance of Viral Late Domains in Budding and Release of Enveloped RNA Viruses

S. Bernacchi, J. Paillart, Lisa Welker, 2021, Viruses.

Degradation-Independent Inhibition of APOBEC3G by the HIV-1 Vif Protein

R. Marquet, J. Paillart, Benjamin Stupfler, 2021, Viruses.

Advances in the structural understanding of Vif proteins.

C. Tisné, R. Marquet, J. Paillart, 2008, Current HIV research.

[APOBEC3s: history of an antiviral and mutagenic protein family].

R. Marquet, J. Paillart, Benjamin Stupfler, 2020, Virologie.

Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling

E. Réal, J. Darlix, Y. Mély, 2016, Retrovirology.

In Search of New Inhibitors of HIV-1 Replication: Synthesis and Study of 1-(2′-Deoxy-β-D-Ribofuranosyl)-1,2,4-Triazole-3-Carboxamide as a Selective Viral Mutagenic Agent

V. Vivet-Boudou, R. Marquet, J. Paillart, 2007, Nucleosides, nucleotides & nucleic acids.

In Search of New Inhibitors of HIV‐1 Replication: Synthesis and Study of 1‐(2′‐Deoxy‐β‐D‐ribofuranosyl)‐1,2,4‐triazole‐3‐carboxamide as a Selective Viral Mutagenic Agent

V. Vivet-Boudou, R. Marquet, J. Paillart, 2008 .

Chemical and Enzymatic Probing of Viral RNAs: From Infancy to Maturity and Beyond

V. Vivet-Boudou, R. Marquet, J. Paillart, 2021, Viruses.

Identification of the primary site of the human immunodeficiency virus type 1 RNA dimerization in vitro.

C. Ehresmann, B. Ehresmann, R. Marquet, 1994, Proceedings of the National Academy of Sciences of the United States of America.

A Conserved uORF Regulates APOBEC3G Translation and Is Targeted by HIV-1 Vif Protein to Repress the Antiviral Factor

A. Cimarelli, J. Batisse, Santiago Guerrero, 2021, bioRxiv.

A conserved uORF impacts APOBEC3G translation and is essential for translational inhibition by the HIV-1 Vif protein

A. Cimarelli, J. Batisse, Santiago Guerrero, 2021 .

Argonaute proteins regulate HIV-1 multiply spliced RNA and viral production in a Dicer independent manner

J. Concordet, H. Seitz, J. Zagury, 2016, Nucleic acids research.

A dual role of the putative RNA dimerization initiation site of human immunodeficiency virus type 1 in genomic RNA packaging and proviral DNA synthesis

C. Ehresmann, J. Darlix, L. Berthoux, 1996, Journal of virology.

DNA synthesis . type 1 in genomic RNA packaging and proviral virusinitiation site of human immunodeficiency A dual role of the putative RNA dimerization

C. Ehresmann, J. Darlix, L. Berthoux, 1996 .

Dimerization of retroviral genomic RNAs: structural and functional implications.

C. Ehresmann, B. Ehresmann, R. Marquet, 1996, Biochimie.

The C-terminal p6 domain of the HIV-1 Pr55Gag precursor is required for specific binding to the genomic RNA

W. McKinstry, J. Mak, S. Bernacchi, 2018, RNA biology.

In vitro dimerization of human immunodeficiency virus type 1 (HIV-1) spliced RNAs.

J. Howard, D. Purcell, R. Marquet, 2007, RNA.

First Snapshots of the HIV-1 RNA Structure in Infected Cells and in Virions*

C. Ehresmann, B. Ehresmann, R. Marquet, 2004, Journal of Biological Chemistry.

Dimerization of retroviral RNA genomes: an inseparable pair

Roland Marquet, Johnson Mak, J. Mak, 2004, Nature Reviews Microbiology.

Opposing Effects of Human Immunodeficiency Virus Type 1 Matrix Mutations Support a Myristyl Switch Model of Gag Membrane Targeting

J. Paillart, H. Göttlinger, 1999, Journal of Virology.

Retroviral RNA Dimerization: From Structure to Functions

S. Bernacchi, R. Marquet, J. Paillart, 2018, Front. Microbiol..

The Life-Cycle of the HIV-1 Gag–RNA Complex

R. Smyth, S. Bernacchi, V. Vivet-Boudou, 2016, Viruses.

HIV-1 specifically encapsidates other nucleic acids than its genomic RNA

R. Marquet, J. Paillart, M. Mougel, 2009, Retrovirology.

HIV controls the selective packaging of genomic, spliced viral and cellular RNAs into virions through different mechanisms

R. Marquet, J. Paillart, M. Mougel, 2007, Nucleic acids research.

Retrovirology Open Access Hiv-1 Specifically Encapsidates Other Nucleic Acids than Its Genomic Rna Background

R. Marquet, J. Paillart, M. Mougel, 2022 .

Tumultuous Relationship between the Human Immunodeficiency Virus Type 1 Viral Infectivity Factor (Vif) and the Human APOBEC-3G and APOBEC-3F Restriction Factors

S. Bernacchi, R. Marquet, J. Paillart, 2009, Microbiology and Molecular Biology Reviews.

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

Pierre B. Cattenoz, F. Jossinet, R. Smyth, 2018, Nucleic acids research.

Mutational interference mapping experiment (MIME) for studying RNA structure and function

F. Jossinet, J. Mak, R. Smyth, 2015, Nature Methods.

Mutational analysis of the bipartite dimer linkage structure of human immunodeficiency virus type 1 genomic RNA.

C. Ehresmann, B. Ehresmann, R. Marquet, 1994, The Journal of biological chemistry.

Dimerization of human immunodeficiency virus type 1 RNA involves sequences located upstream of the splice donor site.

C. Ehresmann, B. Ehresmann, R. Marquet, 1994, Nucleic acids research.

The HDAC6/APOBEC3G complex regulates HIV-1 infectiveness by inducing Vif autophagic degradation

M. Biard-Piechaczyk, J. Batisse, J. Paillart, 2015, Retrovirology.

In Vitro Evidence for a Long Range Pseudoknot in the 5′-Untranslated and Matrix Coding Regions of HIV-1 Genomic RNA*

Chantal Ehresmann, Bernard Ehresmann, Roland Marquet, 2002, The Journal of Biological Chemistry.

Structural and Functional Motifs in Influenza Virus RNAs

Roland Marquet, Redmond P. Smyth, R. Smyth, 2018, Front. Microbiol..

Zinc Fingers in HIV-1 Gag Precursor Are Not Equivalent for gRNA Recruitment at the Plasma Membrane.

E. Réal, Y. Mély, P. Didier, 2020, Biophysical journal.

The two zinc fingers in the nucleocapsid domain of the HIV-1 Gag precursor are equivalent for the interaction with the genomic RNA in the cytoplasm, but not for the recruitment of the complexes at the plasma membrane

E. Réal, Y. Mély, P. Didier, 2020, bioRxiv.

HIV-1 viral infectivity factor interacts with microtubule-associated protein light chain 3 and inhibits autophagy

V. Robert-Hebmann, M. Biard-Piechaczyk, L. Espert, 2015, AIDS.

Translational regulation of APOBEC3G mRNA by Vif requires its 5′UTR and contributes to restoring HIV-1 infectivity

J. Batisse, Santiago Guerrero, R. Marquet, 2016, Scientific Reports.

Molecular architecture and dynamics of ASH1 mRNA recognition by its mRNA-transport complex

R. Janowski, M. Sattler, R. Jansen, 2017, Nature Structural &Molecular Biology.

Interaction network linking the human H3N2 influenza A virus genomic RNA segments.

C. Isel, A. Cavalier, Daniel Thomas, 2012, Vaccine.

Dynamic nanopore long-read sequencing analysis of HIV-1 splicing events during the early steps of infection

S. Emiliani, C. Blugeon, J. Paillart, 2020, Retrovirology.

Post-Translational Modifications of Retroviral HIV-1 Gag Precursors: An Overview of Their Biological Role

S. Bernacchi, R. Marquet, J. Paillart, 2021, International journal of molecular sciences.

Cooperative and specific binding of Vif to the 5' region of HIV-1 genomic RNA.

C. Ehresmann, E. Decroly, S. Bernacchi, 2005, Journal of molecular biology.

Evaluation of Anti-HIV-1 Mutagenic Nucleoside Analogues*

C. Isel, R. Smyth, V. Vivet-Boudou, 2014, The Journal of Biological Chemistry.

HIV-1 Pr55Gag binds genomic and spliced RNAs with different affinity and stoichiometry

J. Mak, R. Smyth, S. Bernacchi, 2017, RNA biology.

HIV-1 Pr 55 Gag binding to viral RNAs HIV-1 Pr 55 Gag binds genomic and spliced RNAs with different affinity and stoichiometry

R. Smyth, S. Bernacchi, R. Marquet, 2016 .

HIV-1 Replication and the Cellular Eukaryotic Translation Apparatus

S. Bernacchi, J. Batisse, Santiago Guerrero, 2015, Viruses.

Specific recognition of the HIV-1 genomic RNA by the Gag precursor

F. Jossinet, J. Mak, R. Smyth, 2014, Nature Communications.

HIV-1 Vif binds to APOBEC3G mRNA and inhibits its translation

S. Bernacchi, R. Marquet, J. Paillart, 2009, Nucleic acids research.

Hijacking of the Ubiquitin/Proteasome Pathway by the HIV Auxiliary Proteins

R. Marquet, J. Paillart, Tanja Seissler, 2017, Viruses.

Initiation of HIV-1 reverse transcription and functional role of nucleocapsid-mediated tRNA/viral genome interactions.

C. Tisné, R. Marquet, J. Paillart, 2012, Virus research.

Structural maturation of the HIV-1 RNA 5’ untranslated region by Pr55Gag and its maturation products

J. Mak, R. Smyth, Assia Mouhand, 2022, RNA biology.

The use of chemical modification interference and inverse PCR mutagenesis to identify the dimerization initiation site of HIV-1 genomic RNA.

C. Ehresmann, B. Ehresmann, R. Marquet, 1996, Pharmaceutica acta Helvetiae.

Requirements for nucleocapsid-mediated regulation of reverse transcription during the late steps of HIV-1 assembly

H. de Rocquigny, S. Bernacchi, J. Paillart, 2016, Scientific Reports.

Characterization of RNA binding and chaperoning activities of HIV-1 Vif protein

V. Larue, S. Bernacchi, C. Tisné, 2014, RNA biology.

Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 Vif

S. Bernacchi, R. Marquet, J. Paillart, 2010, Nucleic acids research.

RNA and DNA Binding Properties of HIV-1 Vif Protein

P. Dumas, S. Bernacchi, R. Marquet, 2007, Journal of Biological Chemistry.

Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription

R. Gorelick, R. Marquet, J. Paillart, 2007, Nucleic acids research.

A structure-based approach for targeting the HIV-1 genomic RNA dimerization initiation site.

P. Dumas, J. Décout, S. Bernacchi, 2007, Biochimie.

Targeting the dimerization initiation site of HIV-1 RNA with aminoglycosides: from crystal to cell

Philippe Dumas, Roland Marquet, Patrick Pale, 2006, Nucleic acids research.

A loop-loop "kissing" complex is the essential part of the dimer linkage of genomic HIV-1 RNA.

C. Ehresmann, B. Ehresmann, R. Marquet, 1996, Proceedings of the National Academy of Sciences of the United States of America.

HIV-1 RNA Dimerization Initiation Site Is Structurally Similar to the Ribosomal A Site and Binds Aminoglycoside Antibiotics* 210

Philippe Dumas, Chantal Ehresmann, Bernard Ehresmann, 2003, The Journal of Biological Chemistry.

Dimerization of HIV-1 genomic RNA of subtypes A and B: RNA loop structure and magnesium binding.

E. Westhof, T. Hermann, C. Ehresmann, 1999, RNA.

Non-canonical interactions in a kissing loop complex: the dimerization initiation site of HIV-1 genomic RNA.

E. Westhof, C. Ehresmann, B. Ehresmann, 1997, Journal of molecular biology.

Oligonucleotide-mediated inhibition of genomic RNA dimerization of HIV-1 strains MAL and LAI: a comparative analysis.

C. Ehresmann, B. Ehresmann, R. Marquet, 1998, Antisense & nucleic acid drug development.

The HIV-1 Nucleocapsid Regulates Its Own Condensation by Phase-Separated Activity-Enhancing Sequestration of the Viral Protease during Maturation

J. Gatell, A. Meyerhans, R. Gorelick, 2021, Viruses.

The HIV-1 ribonucleoprotein dynamically regulates its condensate behavior and drives acceleration of protease activity through membraneless granular phase separation

J. Gatell, A. Meyerhans, R. Gorelick, 2019, bioRxiv.

The DEAD box RNA helicase DDX42 is an intrinsic inhibitor of positive‐strand RNA viruses

C. Goujon, N. Jouvenet, V. Vivet-Boudou, 2022, EMBO reports.

Characterization of the interaction between the HIV-1 Gag structural polyprotein and the cellular ribosomal protein L7 and its implication in viral nucleic acid remodeling

E. Réal, J. Darlix, Y. Mély, 2016, Retrovirology.

Synthesis of a neamine dimer targeting the dimerization initiation site of HIV-1 RNA.

P. Dumas, R. Marquet, J. Paillart, 2007, Organic letters.

The role of Vif oligomerization and RNA chaperone activity in HIV-1 replication.

C. Gabus, J. Darlix, S. Bernacchi, 2012, Virus research.

Characterization of RNA binding and chaperoning activities of HIV-1 Vif protein

V. Larue, S. Bernacchi, C. Tisné, 2014, RNA biology.

Intrinsically disordered RNA-binding motifs cooperate to catalyze RNA folding and drive phase separation

R. Janowski, J. Hennig, D. Niessing, 2024, bioRxiv.

Evaluation of Anti-HIV-1 Mutagenic Nucleoside Analogues*

C. Isel, R. Smyth, V. Vivet-Boudou, 2014, The Journal of Biological Chemistry.

Molecular Mechanisms of Bacterial Resistance to Antimicrobial Peptides in the Modern Era: An Updated Review

J. Paillart, Z. Fajloun, Jean-Marc Sabatier, 2024, Microorganisms.