Versatile anti-infective properties of pyrido- and dihydropyrido[2,3-d]pyrimidine-based compounds [PDF]
A series of 1H-indeno[2',1':5,6]dihydropyrido[2,3-d]pyrimidine and 1H-indeno[2',1':5,6]pyrido[2,3-d]pyrimidine derivatives was prepared and screened for antiparasitic and viral RNase H inhibitory activity.
Al Nasr, Ibrahim S+10 more
core +1 more source
Yeast RNase H(35) is the counterpart of the mammalian RNase HI, and is evolutionarily related to prokaryotic RNase HII1We dedicate this work to the memory of our colleague Robert Karwan (1959–1997).1 [PDF]
We cloned the Saccharomyces cerevisiae homologue of mammalian RNase HI, which itself is related to the prokaryotic RNase HII, an enzyme of unknown function and previously described as having minor activity in Escherichia coli.
Frank, Peter+2 more
core +1 more source
Structure and function of an RNase H domain at the heart of the spliceosome [PDF]
Precursor-messenger RNA (pre-mRNA) splicing encompasses two sequential transesterification reactions in distinct active sites of the spliceosome that are transiently established by the interplay of small nuclear (sn) RNAs and spliceosomal proteins.
Vladimir Peña+4 more
openalex +7 more sources
Biochemical characterization of a multi-drug resistant HIV-1 subtype AG reverse transcriptase: antagonism of AZT discrimination and excision pathways and sensitivity to RNase H inhibitors [PDF]
We analyzed a multi-drug resistant (MR) HIV-1 re- verse transcriptase (RT), subcloned from a patient- derived subtype CRF02 AG, harboring 45 amino acid exchanges, amongst them four thymidine analog mutations (TAMs) relevant for high-level AZT (azi-
Bodem, Jochen+9 more
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The Unfolding Behavior of RNase H Under Force [PDF]
We have used optical tweezers to revisit the energy landscape of E. coli RNase H under mechanical force. This protein's equilibrium energetics and folding pathway have been studied in bulk and in single-molecule mechanical denaturation experiments, which showed the presence of a collapsed folding intermediate that is on-pathway to the native state (1 ...
Susan Marqusee+2 more
openaire +2 more sources
Inhibitory effect of 2,3,5,6-tetrafluoro-4-[4-(Aryl)-1H-1,2,3-triazol-1-yl]benzenesulfonamide derivatives on HIV reverse transcriptase associated rnase H activities [PDF]
The HIV-1 ribonuclease H (RNase H) function of the reverse transcriptase (RT) enzyme catalyzes the selective hydrolysis of the RNA strand of the RNA:DNA heteroduplex replication intermediate, and represents a suitable target for drug development.
Carcelli, Mauro+10 more
core +2 more sources
Polypurine Tract Formation by Ty1 RNase H [PDF]
To better understand the mechanism by which Ty1 RNase H creates the polypurine tract (PPT) primer, we have demonstrated the polymerase-dependent hydrolytic activity of Ty1 reverse transcriptase (RT) during minus-strand synthesis. Using RNase H and polymerase mutants of the recombinant Ty1 RT protein, we show that the two domains of Ty1 RT can act ...
Ozcan Uzun+4 more
openaire +3 more sources
Structure of HIV-1 reverse transcriptase cleaving RNA in an RNA/DNA hybrid [PDF]
HIV-1 reverse transcriptase (RT) contains both DNA polymerase and RNase H activities to convert the viral genomic RNA to dsDNA in infected host cells. Here we report the 2.65-angstrom resolution structure of HIV-1 RT engaging in cleaving RNA in an RNA ...
KIM, MIN SUNG+4 more
core +1 more source
Escherichia coli RNase H has a basic extension that is involved in binding nucleic acid substrates. This basic extension is present in the RNase H of Moloney murine leukemia virus reverse transcriptase (MLV RT), but has been deleted from the RNase H of HIV-1 RT. Previous work showed that removing the basic loop from MLV RT (the mutant is called DeltaC)
Stephen H. Hughes+4 more
openaire +3 more sources
Crystal structure of xenotropic murine leukaemia virus-related virus (XMRV) ribonuclease H [PDF]
RNase H (retroviral ribonuclease H) cleaves the phosphate backbone of the RNA template within an RNA/DNA hybrid to complete the synthesis of double-stranded viral DNA.
Chung, Bong Hyun+8 more
core +1 more source