Results 21 to 30 of about 11,506,565 (250)

Ribonuclease H/DNA Polymerase HIV-1 Reverse Transcriptase Dual Inhibitor: Mechanistic Studies on the Allosteric Mode of Action of Isatin-Based Compound RMNC6. [PDF]

open access: yesPLoS ONE, 2016
The DNA polymerase and ribonuclease H (RNase H) activities of human immunodeficiency virus type 1 (HIV-1) are needed for the replication of the viral genome and are validated drug targets.
Angela Corona   +10 more
doaj   +1 more source

Flavonoids and Acid-Hydrolysis derivatives of Neo-Clerodane diterpenes from Teucrium flavum subsp. glaucum as inhibitors of the HIV-1 reverse transcriptase–associated RNase H function

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2021
Bioassay-guided fractionation of the ethyl acetate extract from Teucrium flavum subsp. glaucum, endowed with inhibitory activity towards the HIV-1 reverse transcriptase–associated RNase H function, led to the isolation of salvigenin (1), cirsimaritin (2)
Benedetta Fois   +8 more
doaj   +1 more source

Human immunodeficiency virus reverse transcriptase-associated RNase H activity [PDF]

open access: yes, 1989
Biochemical characteristics of the RNase H activity associated with immunoaffinity purified human immunodeficiency virus (HIV) reverse transcriptase (RT) were examined.
STARNES, M., CHENG, Y
core   +1 more source

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

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

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

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

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

The deduced amino acid sequence alignment for the S-RNase (PcS34-RNase),

open access: yes, 2011
S-RNase (PdoS5-RNase), . S-RNase (PaS1-RNase), . S-RNase (PdS11-RNase), and . S-RNase (PtS8-RNase). The asterisks indicate the five amino acid residues that are different between . S-RNase and . S-RNase. Conserved nucleotides are shown on a darkened
Daniel Potter (52965)   +5 more
core   +1 more source

A Novel Fully Human Antitumor ImmunoRNase Targeting ErbB2-Positive Tumors [PDF]

open access: yes, 2010
A second generation anti-ErbB2 ImmunoRNase, called Erb-hcAb-RNase, was obtained by the fusion of Erb-hcAb, a human compact anti-ErbB2 antibody, with human pancreatic ribonuclease (HP-RNase or RNase 1).
Borriello, Marianna
core   +1 more source

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