Results 11 to 20 of about 11,347,920 (284)

HIV-1 Ribonuclease H: Structure, Catalytic Mechanism and Inhibitors

open access: yesViruses, 2010
Since the human immunodeficiency virus (HIV) was discovered as the etiological agent of acquired immunodeficiency syndrome (AIDS), it has encouraged much research into antiviral compounds.
Greg L. Beilhartz, Matthias Götte
doaj   +3 more sources

Discovery of Benzisothiazolone Derivatives as Bifunctional Inhibitors of HIV-1 Reverse Transcriptase DNA Polymerase and Ribonuclease H Activities [PDF]

open access: yesBiomolecules
The ribonuclease H (RNase H) active site of HIV-1 reverse transcriptase (RT) is the only viral enzyme not targeted by approved antiretroviral drugs. Using a fluorescence-based in vitro assay, we screened 65,239 compounds at a final concentration of 10 µM
Alondra Vázquez Rivera   +7 more
doaj   +2 more sources

Inhibitors of HIV-1 Reverse Transcriptase—Associated Ribonuclease H Activity

open access: yesBiology, 2012
HIV-1 enzyme reverse transcriptase (RT) is a major target for antiviral drug development, with over half of current FDA-approved therapeutics against HIV infection targeting the DNA polymerase activity of this enzyme. HIV-1 RT is a multifunctional enzyme
Michael A. Parniak   +4 more
doaj   +2 more sources

Scaffold hopping and optimisation of 3’,4’-dihydroxyphenyl- containing thienopyrimidinones: synthesis of quinazolinone derivatives as novel allosteric inhibitors of HIV-1 reverse transcriptase-associated ribonuclease H [PDF]

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2020
Bioisosteric replacement and scaffold hopping are powerful strategies in drug design useful for rationally modifying a hit compound towards novel lead therapeutic agents.
Graziella Tocco   +8 more
doaj   +2 more sources

The hepatitis B virus ribonuclease H as a drug target. [PDF]

open access: yesAntiviral Res, 2015
Chronic hepatitis B virus (HBV) infection is a leading cause of hepatitis, liver failure, and hepatocellular carcinoma. An outstanding vaccine is available; however, the number of infections remains high. Current anti-HBV treatments with interferon α and nucleos(t)ide analogs clear the infection in only a small minority of patients, and either induce ...
Tavis JE, Lomonosova E.
europepmc   +4 more sources

Mechanical Wounding Induces Rapid RNA-Degrading Activity Mediated by the S-like Ribonuclease PvRNS2 in Common Bean [PDF]

open access: yesPlants
Common bean (Phaseolus vulgaris) is an important crop for human nutrition due to its high protein content and capacity to fix atmospheric nitrogen. However, crop productivity is frequently compromised by biotic and abiotic stresses, among which wounding ...
Lucia O. Pareja   +3 more
doaj   +2 more sources

Convergent evolution of ribonuclease h in LTR retrotransposons and retroviruses. [PDF]

open access: yesMol Biol Evol, 2015
Ty3/Gypsy long terminals repeat (LTR) retrotransposons are structurally and phylogenetically close to retroviruses. Two notable structural differences between these groups of genetic elements are 1) the presence in retroviruses of an additional envelope gene, env, which mediates infection, and 2) a specific dual ribonuclease H (RNH) domain encoded by ...
Ustyantsev K   +3 more
europepmc   +4 more sources

Human Cancer Antigen Globo H Is a Cell-Surface Ligand for Human Ribonuclease 1

open access: yesACS Central Science, 2015
Pancreatic-type ribonucleases are secretory enzymes that catalyze the cleavage of RNA. Recent efforts have endowed the homologues from cow (RNase A) and human (RNase 1) with toxicity for cancer cells, leading to a clinical trial.
Chelcie H. Eller   +7 more
doaj   +2 more sources

Ribonuclease H: the enzymes in eukaryotes [PDF]

open access: yesThe FEBS Journal, 2009
Ribonucleases H are enzymes that cleave the RNA of RNA/DNA hybrids that form during replication and repair and which could lead to DNA instability if they were not processed. There are two main types of RNase H, and at least one of them is present in most organisms.
Susana M, Cerritelli, Robert J, Crouch
openaire   +2 more sources

Acetylation regulates the oligomerization state and activity of RNase J, the Helicobacter pylori major ribonuclease

open access: yesNature Communications, 2023
In the gastric pathogen Helicobacter pylori, post-transcriptional regulation relies strongly on the activity of the essential ribonuclease RNase J. Here, we elucidated the crystal and cryo-EM structures of RNase J and determined that it assembles into ...
Alejandro Tejada-Arranz   +10 more
doaj   +1 more source

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