Results 31 to 40 of about 290,253 (274)

Crystal structure of archaeal RNase HII: a homologue of human major RNase H [PDF]

open access: yesStructure, 2000
RNases H are present in all organisms and cleave RNAs in RNA/DNA hybrids. There are two major types of RNases H that have little similarity in sequence, size and specificity. The structure of RNase HI, the smaller enzyme and most abundant in bacteria, has been extensively studied.
Lai, Luhua   +4 more
openaire   +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

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   +1 more source

RNase HI Is Essential for Survival of Mycobacterium smegmatis. [PDF]

open access: yesPLoS ONE, 2015
RNases H are involved in the removal of RNA from RNA/DNA hybrids. Type I RNases H are thought to recognize and cleave the RNA/DNA duplex when at least four ribonucleotides are present.
Alina E Minias   +7 more
doaj   +1 more source

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   +1 more source

Silencing Antibiotic Resistance with Antisense Oligonucleotides

open access: yesBiomedicines, 2021
Antisense technologies consist of the utilization of oligonucleotides or oligonucleotide analogs to interfere with undesirable biological processes, commonly through inhibition of expression of selected genes.
Saumya Jani   +2 more
doaj   +1 more source

From cycloheptathiophene-3-carboxamide to oxazinone-based derivatives as allosteric HIV-1 ribonuclease H inhibitors

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2019
The paper focussed on a step-by-step structural modification of a cycloheptathiophene-3-carboxamide derivative recently identified by us as reverse transcriptase (RT)-associated ribonuclease H (RNase H) inhibitor.
Serena Massari   +12 more
doaj   +1 more source

Nonradioactive Detection of Retroviral- Associated RNase H Activity in a Microplate-Based, High-Throughput Format

open access: yesBioTechniques, 2002
None of the available antiretroviral drugs that are currently used in the clinic to treat infection with HIV-1 is directed against the RNase H active site of the reverse transcriptase.
N. McLellan   +4 more
doaj   +1 more source

The RNase J-Based RNA Degradosome Is Compartmentalized in the Gastric Pathogen Helicobacter pylori

open access: yesmBio, 2020
Posttranscriptional regulation is a major level of gene expression control in any cell. In bacteria, multiprotein machines called RNA degradosomes are central for RNA processing and degradation, and some were reported to be compartmentalized inside these
Alejandro Tejada-Arranz   +5 more
doaj   +1 more source

Mapping the evolution of mitochondrial complex I through structural variation

open access: yesFEBS Letters, EarlyView.
Respiratory complex I (CI) is crucial for bioenergetic metabolism in many prokaryotes and eukaryotes. It is composed of a conserved set of core subunits and additional accessory subunits that vary depending on the organism. Here, we categorize CI subunits from available structures to map the evolution of CI across eukaryotes. Respiratory complex I (CI)
Dong‐Woo Shin   +2 more
wiley   +1 more source

Redesignation of the RNase D activity associated with retroviral reverse transcriptase as RNase H [PDF]

open access: yesJournal of Virology, 1994
In the presence of Mn2+, reverse transcriptase of both human immunodeficiency virus and murine leukemia virus hydrolyzes duplex RNA. However, designating this novel activity RNase D conflicts with Escherichia coli RNase D, which participates in tRNA processing.
Z, Hostomsky   +3 more
openaire   +2 more sources

Home - About - Disclaimer - Privacy