Martin Bisaillon

Characterization of the metal ion binding properties of the hepatitis C virus RNA polymerase.

Investigating the role of metal ions in the catalytic mechanism of the yeast RNA triphosphatase.

Initial binding of the broad spectrum antiviral nucleoside ribavirin to the hepatitis C virus RNA polymerase.

The broad spectrum antiviral nucleoside ribavirin as a substrate for a viral RNA capping enzyme.

Thermodynamics of ligand binding by the yeast mRNA-capping enzyme reveals different modes of binding.

Effect of metal ion binding on the structural stability of the hepatitis C virus RNA polymerase.

Iron inactivates the RNA polymerase NS5B and suppresses subgenomic replication of hepatitis C Virus.

Ribavirin is not a functional mimic of the 7-methyl guanosine mRNA cap.

Energetics of RNA binding by the West Nile virus RNA triphosphatase.

Inhibition of a metal-dependent viral RNA triphosphatase by decavanadate.

[Synergy between transcription and mRNA processing events].

Examination of the folding pathway of the antigenomic hepatitis delta virus ribozyme reveals key interactions of the L3 loop.

Expression of the subgenomic hepatitis C virus replicon alters iron homeostasis in Huh7 cells.

Characterization of the RNA binding energetics of the Candida albicans poly(A) polymerase.

Characterization of the DNA- and dNTP-binding activities of the human cytomegalovirus DNA polymerase catalytic subunit UL54.

Magnesium-binding studies reveal fundamental differences between closely related RNA triphosphatases.

Kinetic and thermodynamic characterization of the RNA guanylyltransferase reaction.

Metal ion-binding studies highlight important differences between flaviviral RNA polymerases.

Monitoring of an RNA multistep folding pathway by isothermal titration calorimetry.

Characterization of the vaccinia virus D10 decapping enzyme provides evidence for a two-metal-ion mechanism.

Nucleotide analogs and molecular modeling studies reveal key interactions involved in substrate recognition by the yeast RNA triphosphatase.

Identification of proteins from prunus persica that interact with peach latent mosaic viroid.

The flavivirus NS5 protein is a true RNA guanylyltransferase that catalyzes a two-step reaction to form the RNA cap structure.

The RNA strands of the plus and minus polarities of peach latent mosaic viroid fold into different structures.

Deciphering the molecular basis for nucleotide selection by the West Nile virus RNA helicase.

Insights into the molecular determinants involved in cap recognition by the vaccinia virus D10 decapping enzyme.

Developing three-dimensional models of putative-folding intermediates of the HDV ribozyme.

Mapping studies of the Peach latent mosaic viroid reveal novel structural features.

Virtual high-throughput screening identifies mycophenolic acid as a novel RNA capping inhibitor.

The RNA capping machinery as an anti-infective target.

A novel ribozyme-based prophylaxis inhibits influenza A virus replication and protects from severe disease.

Elements in the canine distemper virus M 3' UTR contribute to control of replication efficiency and virulence.

Further characterization and determination of the single amino acid change in the tsI138 reovirus thermosensitive mutant.

Programming a highly structured ribozyme into complex allostery using RNA oligonucleotides.

The immunosuppressive agent mizoribine monophosphate is an inhibitor of the human RNA capping enzyme.

Enzymatic synthesis of RNAs capped with nucleotide analogues reveals the molecular basis for substrate selectivity of RNA capping enzyme: impacts on RNA metabolism.

Analysis of decapping scavenger cap complex using modified cap analogs reveals molecular determinants for efficient cap binding.

The intracellular inhibition of HCV replication represents a novel mechanism of action by the innate immune Lactoferrin protein.

Small antisense oligonucleotides against G-quadruplexes: specific mRNA translational switches.

Shu1 is a cell-surface protein involved in iron acquisition from heme in Schizosaccharomyces pombe.