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5'-end-labeled 267 nt-long RNA annealed to 20 nt-long synthetic DNA + H2O
?
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?
5'-rGrGrGrCrGrArArUrUrCrGrArGrCrUrCrGrGrUrArCrCrC-dGdGdGdGdAdTdCdCdTdCdTdAdG-3'/3'-dTdCdGdAdGdCdCdAdTdGdGdG-dCdCdCdCdTdAdGdGdAdGdTdC-5' + H2O
5'-rGrGrGrCrGrArArUrUrCrGrArGrCrUrCrGrGrUrArCrCrC/dGdGdGdGdAdTdCdCdTdCdTdAdG-3' + 3'-dTdCdGdAdGdCdCdAdTdGdGdG/dCdCdCdCdTdAdGdGdAdGdTdC-5'
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model substrate, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication, contains sequences from the HIV genome and sequences unrelated to the HIV viral genome
hydrolysis of the phosphodiester bond at the DNA-RNA junction
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?
5'-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA-dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3'/3'-dGdAdCdAdAdGdCdCdCdGdCdGdGdT-dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5' + H2O
5'-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA/dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3' + 3'-dGdAdCdAdAdGdCdCdCdGdCdGdGdT/dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5'
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model substrate containing sequences from the HIV genome, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication. The DNA-extended RNA was a template and was annealed to a DNA oligonucleotide that primed reverse transcription of the RNA in the template
hydrolysis of the phosphodiester bond at the DNA-RNA junction
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?
5-rGrGrGrCrGrArArUrUrCrGrArGrCrUrCrGrGrUrArCrCrC-dGdGdGdGdAdTdCdCdTdCdTdAdG-3 + 3-dTdCdGdAdGdCdCdAdTdGdGdG-dCdCdCdCdTdAdGdGdAdGdTdC-5' + H2O
?
5-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA-dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3 + 3-dGdAdCdAdAdGdCdCdCdGdCdGdGdT-dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5 + H2O
?
DNA-RNA/DNA hybrid + H2O
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poly(A)+ mRNA primed with oligo(dT) + H2O
double-stranded DNA copies between 1.3 and 9.9 kilobases in length + ?
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multifunctional enzyme containing RNase H and reverse transcriptase activity
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?
poly(dC)-poly(rG) + H2O
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poly(dT)-poly(rA) + H2O
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substrate poly(dC)-poly(rG) is markedly preferred over substrate poly(dT)-poly(rA)
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poly(rA)/oligo(dT) + H2O
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synthetic hybrid
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poly(rA)n-poly(dT)n + H2O
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poly(rG)/poly(dC) + H2O
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RNA-DNA duplex + H2O
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RNA-DNA hybrid containing the polypurine tract + H2O
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extension of the polypurine tract primer by at least 2 nucleotides is sufficient for recognition and correct cleavage by RNase H at the RNA-DNA junction to remove the primer. Primer removal occurs by cleavage one nucleotide away from the RNA-DNA junction. The same polypurine tract specificity determinants responsible for generation of the polypurine tract primer also direct polypurine tract primer removal. Once the primer has been extended and removed from the nascent plus-strand DNA, reinitiation at the resulting plus-strand primer terminus does not occur
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?
RNA:DNA hybrid + H2O
AMP + ?
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additional information
?
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5-rGrGrGrCrGrArArUrUrCrGrArGrCrUrCrGrGrUrArCrCrC-dGdGdGdGdAdTdCdCdTdCdTdAdG-3 + 3-dTdCdGdAdGdCdCdAdTdGdGdG-dCdCdCdCdTdAdGdGdAdGdTdC-5' + H2O

?
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model substrate, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication, contains sequences from the HIV genome and sequences unrelated to the HIV viral genome
hydrolysis of the substrate to leave a single ribonucleotide 5-phosphate at the 5-terminus of the model DNA genome
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?
5-rGrGrGrCrGrArArUrUrCrGrArGrCrUrCrGrGrUrArCrCrC-dGdGdGdGdAdTdCdCdTdCdTdAdG-3 + 3-dTdCdGdAdGdCdCdAdTdGdGdG-dCdCdCdCdTdAdGdGdAdGdTdC-5' + H2O
?
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model substrate, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication, contains sequences from the HIV genome and sequences unrelated to the HIV viral genome
hydrolysis of the substrate to leave a single ribonucleotide 5-phosphate at the 5-terminus of the model DNA genome
-
?
5-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA-dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3 + 3-dGdAdCdAdAdGdCdCdCdGdCdGdGdT-dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5 + H2O

?
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model substrate containing sequences from the HIV genome, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication. The DNA-extended RNA was a template and was annealed to a DNA oligonucleotide that primed reverse transcription of the RNA in the template
hydrolysis of the substrate to leave a single ribonucleotide 5'-phosphate at the 5'-terminus of the model DNA genome
-
?
5-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA-dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3 + 3-dGdAdCdAdAdGdCdCdCdGdCdGdGdT-dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5 + H2O
?
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model substrate containing sequences from the HIV genome, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication. The DNA-extended RNA is a template and is annealed to a DNA oligonucleotide that primed reverse transcription of the RNA in the template
hydrolysis of the substrate to leave a single ribonucleotide 5-phosphate at the 5-terminus of the model DNA genome
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?
poly(rG)/poly(dC) + H2O

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poly(rG)/poly(dC) + H2O
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RNA-DNA hybrid + H2O

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RNA-DNA hybrid + H2O
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RNA-DNA hybrid + H2O
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5'-GTTTTCTTTTCCCCCCTGAC-3'-fluorescein/5'-CAAAAGAAAAGGGGGGACUG-3'-dabcyl
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?
additional information

?
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evaluation of activity by enzyme's ability to select and extend the 3' polypurine tract primers into (+) strand DNA. Evaluation via concerted and two-step reactions for (+) strand priming, the latter of which allows discrimination between selection end extension events
3' polypurine tract primer selection appears to represent a specialized form of RNase H activity that is more sensitive to minor structural alterations within this domain
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additional information
?
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no substrate: single-stranded RNA or the DNA component of DNA-RNA hybrids. Products consist primarily of monomers, dimers, and trimers with 3'-OH groups
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additional information
?
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the HIV polymerase and RNase H active sites are separated by a distance equivalent to the length of a 15-nucleotide RNA-DNA heteroduplex
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additional information
?
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a nick separating an upstream RNA and a downstream RNA annealed to DNA is essentially ignored by RNase H, indicating that the RNA 5' end at a nick is not sufficient to position 5' end-directed cleavages. Cleavage sites that are located close to the 5' end of the downstream RNA are not recognized in the absence of the upstream RNA, and the 5' ends of the shorter upstream RNAs enhance cleavage at these sites. The recognition of an internal cleavage site depends on local sequence features found both upstream and downstream of the cleavage site, designated as the -1/+1 position. Preferred nucleotides have been identified in the flanking sequences spanning positions -14 to +1
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additional information
?
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interdependence of the polymerase and RNase H activities of HIV-1 reverse transcription during viral DNA synthesis
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additional information
?
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RNase H acts at or about 14 to 18 nucleotides from the 5' end of the template, the cleavage site for the RNase H is therefore held at around this distance behind the DNA polymerase activity. For the intact protein, the RNase H and reverse transcriptase activities may work in a coupled or coordinate manner. More than 80% of the residual 5' oligonucleotides remain base paired to the RNA-directed DNA product. Under certain conditions, these short RNAs can act as efficient primers for an associated DNA-directed DNA synthesis in the reverse direction
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additional information
?
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study on specificity of RNase H cleavage by use of synthetic DNA-RNA hybrids based on the same 81-base RNA template. First series of RNase H substrates is prepared with complementary DNA oligonucleotides of different lengths, ranging from 6 to 20 nucleotides, all of which share a common 5' end and are successively shorter at their 3' ends. The second series of oligonucleotides has a common 3' end but shorter 5' ends. The DNA oligonucleotides in the third series are all 20 bases long but have non-complementary stretches at either the 5' end, 3' end, or both ends. Enzyme cleaves fairly efficiently if the duplex region is at least eight bases long, but not if it is shorter. Although enzyme requires the substrate to have a region of RNA-DNA duplex, Moloney murine leukemia virus RT can cleave RNA outside the region that is part of the RNA-DNA duplex. The polymerase domain of HIV-1 RT uses certain mismatched segments of RNA-DNA to position the enzyme for RNase H cleavage. A mismatched region near the RNase H domain can interfere with RNase H cleavage, cleavage is usually but not always more efficient if the mismatched segment is deleted
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additional information
?
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substrate heteropolymeric 90-nt 5' end-labeled RNA template-annealed to a 36-nt DNA primer is cleaved by wild-type p66/p51 RT precisely at the RNA/DNA junction to liberate a 20-nt (+) strand DNA
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additional information
?
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substrates consist of SP6 runoff transcripts from a portion of the gag region of the HIV-1 genome hybridized to complementary single-stranded DNA from either an M 13 subclone or a phagemid transcription vector subclone. The corresponding hybrids are fully base-paired
products formed from the fully complementary hybrid consist of a nonuniform distribution of oligonucleotides ranging in size from 4 to 15 nt
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additional information
?
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substrates consist of SP6 runoff transcripts from a portion of the gag region of the HIV-1 genome hybridized to complementary single-stranded DNA from either an M 13 subclone or a phagemid transcription vector subclone. The corresponding hybrids carry a 5'-mismatch of seven nucleotides
products are a few prominent intermediates of 24-42 nt in size with relatively little accumulation of larger products
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additional information
?
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the recognition and precise cleavage of the polypurine tract of the human immunodeficiency virus type 1 is an essential step in HIV-1 reverse transcription. Mutations at positions 2 and 5 of the 3'-end of the polypurine tract do significantly alter the cleavage specificity at the polypurine tract/U3 junction. The structure of the polypurine tract primer, rather than the base-specific contacts between the polypurine tract and HIV-1 RT, are the primary determinants of RNase H cleavage specificity at the polypurine tract/U3 junction
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additional information
?
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the selection of 5' end-directed cleavage sites by retroviral RNases H results from a combination of nucleotide sequence, permissible distance, and accessibility to the RNA 5' end. Enzyme strongly prefers A or U at the +1 position and C or G at the -2 position, and A is disfavored at the -4 position. 5' End-directed cleavages occur when sites are positioned between the 13th and 20th nucleotides from the RNA 5' end. The extent of 5' end-directed cleavages observed in substrates containing a free recessed RNA 5' end is most comparable to substrates with a gap of 2 or 3 bases between the upstream and downstream RNAs
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additional information
?
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5'end-directed RNase H of reverse transcriptase
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additional information
?
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HIV-1 reverse transcriptase has two enzymatic functions, DNA polymerase and RNase H activities
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additional information
?
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RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview
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additional information
?
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cleavage of DNA-RNA and RNA-DNA primer templates
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additional information
?
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RNA-DNA duplex substrate from a 41-mer 5'-labeled 32P-heteropolymeric RNA template kim40R annealed to complementary 32-mer DNA oligomer kim32D
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additional information
?
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RNA-DNA substrate
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additional information
?
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RNA-DNA substrate in a tRNA removal assay, the cleavage patterns for the recombinant HIV-1 reverse transcriptase and mutant p51-G-TCR construct correspond to the release of the 11mer RNA, corresponding with the authentic cleavage identified in vivo. The relative activity of the isolated HIV-1 RNaseH(p51-G-TCR) is comparable to that of the full-length HIV reverse transcriptase
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additional information
?
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RNA/DNA hybrid duplex substrate
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additional information
?
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substrate is 18-nucleotide 3'-fluourescein-labeled RNA annealed to a complementary 18-nucleotide 5'-dabsyl-labeled DNA
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additional information
?
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the tC5U-p12 hybrid is used as reaction substrate the RNase H activity
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additional information
?
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conserved residues in the connection subdomain and C-terminal ribonuclease H, RNase H, domain of HIV-1 RT contact the nascent DNA primer and modulate the trajectory of the template relative to the RNase H catalytic center. Within the RNase H domain, these residues include Thr473, Glu475, Lys476, Tyr501, and Ile505, while His539 and Asn474 interact with the scissile phosphate of the RNA template,m substrate recognition and binding, overview
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additional information
?
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a 5'-32P-labeled AZT-MP chain-terminated RNA/DNA template/primer substrate
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additional information
?
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cleavage of DNA-RNA and RNA-DNA primer templates
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additional information
?
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RNA-DNA duplex substrate from a 41-mer 5'-labeled 32P-heteropolymeric RNA template kim40R annealed to complementary 32-mer DNA oligomer kim32D
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additional information
?
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RNA/DNA hybrid duplex substrate
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additional information
?
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RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview
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additional information
?
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a nick separating an upstream RNA and a downstream RNA annealed to DNA is essentially ignored by RNase H, indicating that the RNA 5' end at a nick is not sufficient to position 5' end-directed cleavages. Cleavage sites that are located close to the 5' end of the downstream RNA are not recognized in the absence of the upstream RNA, and the 5' ends of the shorter upstream RNAs enhance cleavage at these sites. The recognition of an internal cleavage site depends on local sequence features found both upstream and downstream of the cleavage site, designated as the -1/+1 position. Preferred nucleotides have been identified in the flanking sequences spanning positions -11 to +1
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additional information
?
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study on specificity of RNase H cleavage by use of synthetic DNA-RNA hybrids based on the same 81-base RNA template. First series of RNase H substrates is prepared with complementary DNA oligonucleotides of different lengths, ranging from 6 to 20 nucleotides, all of which share a common 5' end and are successively shorter at their 3' ends. The second series of oligonucleotides has a common 3' end but shorter 5' ends. The DNA oligonucleotides in the third series are all 20 bases long but have non-complementary stretches at either the 5' end, 3' end, or both ends. Enzyme cleaves fairly efficiently if the duplex region is at least eight bases long, but not if it is shorter. Although enzyme requires the substrate to have a region of RNA-DNA duplex, Moloney murine leukemia virus RT can cleave RNA outside the region that is part of the RNA-DNA duplex. The polymerase domain of Moloney murine leukemia virus RT does not use the same mismatched segments to define the position for RNase H cleavage
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additional information
?
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the selection of 5' end-directed cleavage sites by retroviral RNases H results from a combination of nucleotide sequence, permissible distance, and accessibility to the RNA 5' end. Enzyme strongly prefers A or U at the +1 position and C or G at the -2 position. 5' End-directed cleavages occurr when sites are positioned between the 13th and 20th nucleotides from the RNA 5' end. The extent of 5' end-directed cleavages observed in substrates containing a free recessed RNA 5' end is most comparable to substrates with a gap of 2 or 3 bases between the upstream and downstream RNAs
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additional information
?
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Moloney murine leukemia virus reverse transcriptase, M-MuLV RT, is a domain structured enzyme that has the N-terminally located DNA polymerization activity and C-terminally located RNase H activity, which interferes with the efficient synthesis of long cDNA molecules
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additional information
?
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Moloney murine leukemia virus reverse transcriptase, MMLV RT, shows DNA polymerization activity and RNase H activity. Stabilization of the reverse transcriptase activity by eliminating the RNase H activity, overview
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additional information
?
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retroviral reverse transcriptase also possesses a ribonuclease H activity, an enzyme which cleaves the RNA strand of RNA/DNA hetroduplex
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additional information
?
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DNA binding by M-MuLV RT assay using 5'-end labeled 48/36 bp RNA-DNA oligonucleotide duplex, method, overview. RNA-DNA hybrid binding and 5'-end labeled 48/36 bp RNA-DNA oligonucleotide duplex by M-MuLV RT derivatives, overview
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additional information
?
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substrate is a 3H-UTP-labeled RNA: RNA-DNA hybrid, synthesis, overview
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additional information
?
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the active site of the RNase H function contains four acidic residues, D443, E478, D498, and D549, that likely coordinate two divalent metal ions that are essential for catalysis
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(2S)-5,7-dihydroxy-2-(2-hydroxy-1-(phenylsulfonyl)propan-2-yl)-9-methyl-3,4-dihydro-1H-benzo[7]annulen-6(2H)-one
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(2Z)-4-[1-(4-fluorobenzyl)-4-oxo-7-(pyrrolidin-1-yl)-1,4-dihydroquinolin-3-yl]-2-hydroxy-4-oxobut-2-enoic acid
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(4-N,N-dimethylaminobenzoyl)-2-hydroxy-1-naphthyl hydrazone
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specific
(5E)-6-[1-(2,4-dimethylbenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
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(5E)-6-[1-(2-chlorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
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(5E)-6-[1-(3-methoxybenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
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(5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
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(5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoic acid
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(5E)-6-[1-(4-fluorobenzyl)-4-phenyl-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoic acid
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(6,6,12,12,18,18,18-heptaoxido-5,7,11,13,17-pentaoxa-6l5,12l5,18l5-triphosphaoctadec-1-yl)phosphonate
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1,2-bis(2-oxopropoxy)anthracene-9,10-dione
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9% inhibition
1,2-bis[(3-oxobutan-2-yl)oxy]anthracene-9,10-dione
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20% inhibition
1,2-dihydroxyanthracene-9,10-dione
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i.e. alizarine, 8% inhibition
1,3,4,5-tetrahydrogalloylapitol
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1,6,8-trihydroxy-3-methylanthraquinone
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i.e. frangula-emodin
1-(2-hydroxyethoxymethyl)-6-(phenylthio)thymine
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1-(3-[[(4-benzyl-5-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]methyl]-4-methoxyphenyl)ethanone
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1-hydroxy-4-((4-(morpholinomethyl)phenyl)amino)pyrido[2,3-d]pyrimidin-2(1H)-one
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1-hydroxy-4-((4-(pyridin-4-yl)phenyl)amino)pyrido[2,3-d]pyrimidin-2(1H)-one
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1-hydroxy-4-([[3-(4-morpholinyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
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1-hydroxy-4-([[3-(4-morpholinylmethyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
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1-hydroxy-4-([[4-(4-morpholinyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
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1-hydroxy-4-([[4-(4-pyridinyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
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1-hydroxy-4-[[4-(4-morpholinyl)phenyl]amino]pyrido[2,3-d]pyrimidin-2(1H)-one
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1-hydroxy-4-[[4-(quinolin-3-yl)phenyl]amino]pyrido[2,3-d]pyrimidin-2(1H)-one
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GSK5724, exceptional RNase H inhibitory potency
1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
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10,12,15,16-tetrahydroxy-8-methoxy-11-methyl-2-phenyl-6,7-dihydrotetraceno[1,2-g]phthalazine-1,9,14(2H)-trione
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2',3'-dideoxy-3'-triaz-2-en-2-ium-3-id-1-yl-3,4-dihydrothymidine
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2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-guanosine
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40% inhibition of RNase H at 0.05 microM
2'-deoxy-P-thioguanylyl-(3'->5')-guanosine
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65% inhibition of RNase H at 0.05 microM
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2,3,7-trihydroxy-6-(3-nitrobenzyl)cyclohepta-2,4,6-trien-1-one
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2,7-dihydroxy-4-(propan-2-yl)cyclohepta-2,4,6-trien-1-one
2,7-dihydroxy-4-isopropyl-cyclohepta-2,4,6-triene
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i.e. beta-thujaplicinol
2-(1,2-dihydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
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2-(1-benzylamino-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
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2-(2,3-dihydro-1H-inden-1-ylamino)-2-oxoethyl 5-nitrofuran-2-carboxylate
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2-(2,3-dihydro-1H-inden-2-ylamino)-2-oxoethyl 5-nitrofuran-2-carboxylate
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2-(2-benzylsulfanyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
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2-(2-diethylamino-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
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2-(2-ethanesulfonyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
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2-(2-ethylsulfanyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
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2-(3,4-dichlorobenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acid
2-(3-bromo-4-methoxybenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acid
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inhibition of enzymatic activity, but no antiviral effect
2-(tert-butylamino)-2-oxoethyl 5-nitrofuran-2-carboxylate
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2-amino-2-oxoethyl 5-nitrofuran-2-carboxylate
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2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
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2-hydroxy-(4H)-isoquinoline-1,3-dione
-
inhibits RNase H in vitro with submicromolar potency
2-hydroxy-4-(2-phenyl)ethylisoquinoline-1,3(2H,4H)-dione
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enol-form
2-hydroxy-4-(3-phenyl)propylisoquinoline-1,3(2H,4H)-dione
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mixture of th mixed ketoenol forms or keto-form
2-hydroxy-4-(4-methylbenzyl)isoquinoline-1,3(2H,4H)-dione
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mixture of th mixed ketoenol forms or keto-form
2-hydroxy-4-(4-trifluoromethylbenzyl)isoquinoline-1,3(2H-4H)-dione
-
keto-form
2-hydroxy-4-butylisoquinoline-1,3(2H,4H)-dione
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mixture of th mixed ketoenol forms or keto-form
2-hydroxy-4-ethylisoquinoline-1,3(2H,4H)-dione
-
-
2-hydroxy-4-isopropylisoquinoline-1,3(2H,4H)-dione
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2-hydroxy-4-methoxycarbonylisoquinoline-1,3(2H, 4H)-dione
-
inhibits RNase H in vitro with nanomolar potency
2-hydroxy-4-methoxycarbonylisoquinoline-1,3(2H,4H)-dione
-
shows antiviral activity
2-hydroxy-4-methylisoquinoline-1,3(2H,4H)-dione
2-hydroxy-4-pentylisoquinoline-1,3(2H,4H)-dione
-
-
2-hydroxy-4-propylisoquinoline-1,3(2H,4H)-dione
-
-
2-hydroxyisoquinoline-1,3(2H,4H)-dione
2-hydroxyisoquinoline-1,3(2H,4H)-dione magnesium complex
-
-
-
2-oxo-2-(1,2,3,4-tetrahydronaphthalen-1-ylamino)ethyl 5-nitrofuran-2-carboxylate
-
-
2-oxo-2-(phenylamino)ethyl dibenzylcarbamodithioate
-
-
2-oxo-2-(propan-2-yloxy)ethyl 5-nitrofuran-2-carboxylate
-
-
2-oxo-2-(tetrahydrofuran-2-ylamino)ethyl 5-nitrofuran-2-carboxylate
-
-
2-oxo-2-[(2,3,4-trichlorophenyl)amino]ethyl benzyl(phenyl)carbamodithioate
-
-
2-oxo-2-[(2,3,4-trichlorophenyl)amino]ethyl dibenzylcarbamodithioate
-
-
2-oxo-2-[(2-phenylpropan-2-yl)amino]ethyl 5-nitrofuran-2-carboxylate
-
-
2-[(2,3,4-trichlorophenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
-
inhibitor indentified by FRET-based high-throughput screening assay
2-[(2,4-dichlorophenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
-
-
2-[(2,4-dimethylphenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
-
; inhibitor indentified by FRET-based high-throughput screening assay
2-[(2-bromo-5-chloro-1-benzothiophen-3-yl)methyl]-5,6-dihydroxypyrimidine-4-carboxylic acid
-
-
2-[(2-methoxy-5-methylphenyl)amino]-2-oxoethyl benzyl(phenyl)carbamodithioate
-
-
2-[(2-methyl-1-phenylpropan-2-yl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[(2-methylbutan-2-yl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[(3-cyanophenyl)amino]-2-oxoethyl benzyl(phenyl)carbamodithioate
-
-
2-[(3-cyanophenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
-
-
2-[(4-hydroxybenzyl)(tetrahydrofuran-2-ylmethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[2-(2-fluoro-benzylamino)-1-hydroxy-1-methyl-ethyl]-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
2-[2-(4-bromophenyl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetate
-
-
2-[2-(biphenyl-4-yl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetate
-
-
2-[4-benzyl-5-(benzylsulfanyl)-4H-1,2,4-triazol-3-yl]pyridine
-
; inhibitor indentified by FRET-based high-throughput screening assay
2-[4-benzyl-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridine
-
-
2-[benzyl(tetrahydrofuran-2-ylmethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[bis(4-methoxyphenyl)(phenyl)methoxy]ethyl 2-cyanoethyl dipropan-2-ylphosphoramidoite
-
-
2-[tert-butyl(2-phenylethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(3-nitrobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(3-oxo-3-phenylpropyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(3-phenylpropyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(4-fluorobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(4-methoxybenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(4-nitrobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(pentafluorobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(phenyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl[2-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl[3-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl[4-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[[2-(acetyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[[4-(acetyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[[4-(benzyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
3'-[(E)-[2-(3,4,5-trihydroxybenzoyl)hydrazinylidene]methyl]biphenyl-4-carboxylic acid
-
-
3,3-dimethyl-2-oxobutyl 5-nitrofuran-2-carboxylate
-
-
3,4-dihydroxy-N'-[(E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide
-
-
3,9,11,14,15-pentahydroxy-7-methoxy-10-methyl-5,6-dihydrobenzo[9,10]tetrapheno[2,3-c]furan-1,8,13(3H)-trione
-
-
3-(furan-2-yl)-4-(4-methoxybenzyl)-5-[[4-(trifluoromethyl)benzyl]sulfanyl]-4H-1,2,4-triazole
-
-
3-(furan-2-yl)-4-phenyl-5-[[4-(trifluoromethyl)benzyl]sulfanyl]-4H-1,2,4-triazole
-
-
3-cyclopentyl-1,4-dihydroxy-1,8-naphthyridin-2(1H)-one
-
3-[2-(4-bromophenyl)-2-oxoethoxy]-1,8-dihydroxy-6-methylanthracene-9,10-dione
-
-
3-[4-(2-methyl-imidazo[4,5-c]pyridin-1-yl)-benzyl]-3H-benzothiazol-2-one
-
-
4-((cyclopropylmethyl)amino)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
-
-
4-(([1,1'-biphenyl]-4-ylmethyl)amino)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
-
-
4-(4,4-difluoropiperidin-1-yl)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
-
-
4-([1,1'-biphenyl]-4-ylamino)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
-
-
4-([[4-benzyl-5-(furan-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
-
-
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
4-benzyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
-
keto-form; mixture of th mixed ketoenol forms
4-benzyl-3-(benzylsulfanyl)-5-(furan-2-yl)-4H-1,2,4-triazole
-
; inhibitor indentified by FRET-based high-throughput screening assay
4-benzyl-3-(benzylsulfanyl)-5-(thiophen-2-yl)-4H-1,2,4-triazole
-
; inhibitor indentified by FRET-based high-throughput screening assay
4-benzyl-3-(benzylsulfanyl)-5-phenyl-4H-1,2,4-triazole
-
; inhibitor indentified by FRET-based high-throughput screening assay
4-benzyl-3-(furan-2-yl)-5-[(4-methoxybenzyl)sulfanyl]-4H-1,2,4-triazole
-
-
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-(furan-2-yl)-4H-1,2,4-triazole
-
-
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazole
-
; inhibitor indentified by FRET-based high-throughput screening assay
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-phenyl-4H-1,2,4-triazole
-
-
4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazole
-
-
4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-phenyl-4H-1,2,4-triazole
-
inhibitor indentified by FRET-based high-throughput screening assay
4-heptyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
-
enol form
4-hexyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
-
keto-form; mixture of th mixed ketoenol forms
4-tert-butyl-N'-[(E)-(2-hydroxynaphthalen-1-yl)methylidene]benzohydrazide
-
-
4-[1-4-[(4-fluorophenyl)methyl]-7-[N-(3-chloroprop-1-yl)-piperazin-1-yl]-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
35% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(dimethylamino)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
72% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(dimethylamino)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
26% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(morpholin-4-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
0.7% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(N-acetylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
22% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(N-acetylpiperazin-1-yl)-4-(1h)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
30% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(N-ethylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
34% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(N-ethylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
63% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(N-methylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
44% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(N-methylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
41% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(piperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
44% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(piperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
18% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(thiomorpholin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
74% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-[N-(3-chloroprop-1-yl)piperazin-1-yl]-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
78% inhibition at 0.01 mM
4-[5-(benzoylamino)thien-2-yl]-2,4-dioxobutanoic acid
-
-
4-[5-(benzoylamino)thiophen-2-yl]-2,4-dioxobutanoic acid
-
-
4-[[(4-fluorophenyl)methyl]amino]-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
-
-
4-[[4'-(aminomethyl)biphenyl-4-yl]methyl]-1-hydroxy-1,8-naphthyridin-2(1H)-one
-
-
4-[[4-([4-[(E)-2-cyanovinyl]-2,6-dimethylphenyl]amino)pyrimidin-2-yl]amino]benzonitrile
-
i.e. TMC278 or rilpivirine, enzyme-bound structure, overview
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-phenylaminoethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-phenylsulfanylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-piperidin-1-ylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
5,7-dihydroxy-2-(1-hydroxy-2-imadazol-1-yl-1-methyl ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
5,7-dihydroxy-2-(1-hydroxy-ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
5,7-dihydroxy-2-isopropenyl-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
i.e. manicol, the alpha-hydroxytroplone potently and specifically inhibits HIV RT ribonuclease H, enzyme-bound structure, overview
5-(1,1-dioxido-1,2-thiazinan-2-yl)-N-(4-fluorobenzyl)-8-hydroxy-1,6-naphthyridine-7-carboxamide
-
-
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
6-[1-(4-fluorophenyl)methyl-1H-pyrrol-2-yl]-2,4-dioxo-5-hexenoic acid ethyl ester
-
i.e. RDS-1643, shows relatively weak but selective inhibitory activity against RNase H
6-[4-(diethylamino)phenoxy]-3-[ethoxy(hydroxy)methyl]-1,4-dihydroxy-1,8-naphthyridin-2(1H)-one
-
8-hydroxy-1,6-naphthyridine-7-carboxylic acid
-
-
9,10-dioxo-2-(2-oxo-2-phenylethoxy)-9,10-dihydroanthracen-1-yl acetate
-
-
9,10-dioxo-2-(2-oxopropoxy)-9,10-dihydroanthracen-1-yl acetate
-
10% inhibition
9,10-dioxo-2-(prop-2-en-1-yloxy)-9,10-dihydroanthracen-1-yl acetate
-
-
9,10-dioxo-2-(prop-2-yn-1-yloxy)-9,10-dihydroanthracen-1-yl acetate
-
-
9,10-dioxo-2-[(2-oxopentan-3-yl)oxy]-9,10-dihydroanthracen-1-yl acetate
-
inhibits the RNase H function and is inactive on the DNA polymerase function
9,10-dioxo-2-[(3-oxobutan-2-yl)oxy]-9,10-dihydroanthracen-1-yl acetate
-
-
9,10-dioxo-9,10-dihydroanthracene-1,2-diyl diacetate
-
12% inhibition
9,10-dioxo-9,10-dihydroanthracene-1,2-diyl dibenzoate
-
-
actinomycin D
-
limits the enzyme to the first strand synthesis
bis[3-(phosphonatooxy)propyl] phosphate
-
-
delaviridine
-
a nonnucleoside reverse transcriptase inhibitor
Dextran sulfate
-
more potent inhibitor of RNase H than of reverse transcriptase. 50% infective dose corresponds to 0.1 nM
-
dihydroxybenzoyl naphthyl hydrazone
-
-
ethyl (2Z)-4-[1-(4-fluorobenzyl)-4-oxo-7-(pyrrolidin-1-yl)-1,4-dihydroquinolin-3-yl]-2-hydroxy-4-oxobut-2-enoate
-
-
ethyl (5E)-6-[1-(2,4-dimethylbenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
-
-
ethyl (5E)-6-[1-(2-chlorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
-
selectively inhibits RNase H activity in the low micromolar range
ethyl (5E)-6-[1-(3-methoxybenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
-
-
ethyl (5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
-
-
ethyl (5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoate
-
-
ethyl (5E)-6-[1-(4-fluorobenzyl)-4-phenyl-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoate
-
-
ethyl 1,4-dihydroxy-2-oxo-1,2-dihydro-1,8-naphthyridine-3-carboxylate
F3284-8495
-
specific inhibitor with low micromolar potency in vitro
GSK5750
-
active site inhibitor
guanylyl-(3'->5')-guanosine
-
89% inhibition of RNase H at 0.05 microM
heparin
-
more potent inhibitor of RNase H than of reverse transcriptase. 50% infective dose corresponds to 0.5-1.5 nM
methyl 2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinoline-4-carboxylate
-
-
Mn2+
-
activation at 0.01-1 mM, inhibitory above
N-(4-chlorobenzyl)-8-hydroxy-1,6-naphthyridine-7-carboxamide
-
-
NSC727447
-
mutation T473C increases sensitivity of the enzyme for NSC727447 by 50fold
P-thioguanylyl-(3'->5')-guanosine
-
50% inhibition of RNase H at 0.05 microM
-
pyrimidinol carboxylic acid
-
-
sodium 2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-naphthalen-1-ylguanosine
-
sodium 2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-[2-(4-nitrophenyl)ethyl]guanosine
-
69% inhibition of RNase H at 0.05 microM
-
tenofovir disoproxil
-
a nucleoside reverse transcriptase inhibitor
tetrahydroimidazo[4,5,1-jk][1,4]benzodiazepin-2(1H)-one
-
-
xylan polysulfate
-
more potent inhibitor of RNase H than of reverse transcriptase. 50% infective dose corresponds to 8 nM
-
zalcitabine
-
a nucleoside reverse transcriptase inhibitor
zidovudine
-
a nucleoside reverse transcriptase inhibitor
[2-(4-chlorophenyl)hydrazinylidene]propanedioic acid
2,7-dihydroxy-4-(propan-2-yl)cyclohepta-2,4,6-trien-1-one

-
inhibition of enzymatic activity, but no antiviral effect
2,7-dihydroxy-4-(propan-2-yl)cyclohepta-2,4,6-trien-1-one
-
-
2-(3,4-dichlorobenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acid

-
inhibition of enzymatic activity, but no antiviral effect
2-(3,4-dichlorobenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acid
-
-
2-hydroxy-4-methylisoquinoline-1,3(2H,4H)-dione

-
-
2-hydroxy-4-methylisoquinoline-1,3(2H,4H)-dione
-
-
2-hydroxyisoquinoline-1,3(2H,4H)-dione

-
-
2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
inhibition of enzymatic activity, but no antiviral effect
2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
-
2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
-
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine

-
; inhibitor indentified by FRET-based high-throughput screening assay
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
-
-
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester

-
inhibitor has little effect on bacterial RNase H activity in vitro
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
-
-
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester

-
additionally inhibits HIV-1 replication effectively. Inhibitor has little effect on bacterial RNase H activity in vitro
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
-
-
Abacavir

-
a nucleoside reverse transcriptase inhibitor
beta-thujaplicinol

-
slow-binding RNase H inhibitor with noncompetitive kinetics that forms a tropylium ion that interacts favorably with reverse transcriptase and the RNA:DNA substrate
beta-thujaplicinol
-
shows submicromolar inhibitory activity against RNase H
beta-thujaplicinol
-
; weak inhibition at 0.05 mM
didanosine

-
a nucleoside reverse transcriptase inhibitor
efavirenz

-
second generation non-nucleoside reverse transcriptase inhibitor, shows the effect of simultaneously reorienting domain motions and obstructing the p66 thumb fluctuations
efavirenz
-
stronger effect of mutation N348I on RNase H susceptibility to nevirapine as compared with efavirenz
efavirenz
-
a nonnucleoside reverse transcriptase inhibitor
Emtricitabine

-
a nucleoside reverse transcriptase inhibitor
ethyl 1,4-dihydroxy-2-oxo-1,2-dihydro-1,8-naphthyridine-3-carboxylate

interactions between MK1 and two Mn2+ ions, which are coordinated by the RNase H active site residues D443, E478, D498, and D549, binding structure, overview. In addition, G444, S499, A538, H539, V552, and S553 contribute to the binding site
ethyl 1,4-dihydroxy-2-oxo-1,2-dihydro-1,8-naphthyridine-3-carboxylate
-
-
Etravirine

-
a nonnucleoside reverse transcriptase inhibitor
lamivudine

-
a nucleoside reverse transcriptase inhibitor
nevirapine

-
non-nucleoside RT inhibitors such as nevirapine interfere directly with the global hinge-bending mechanism that controls the cooperative motions of the p66 fingers and thumb subdomains. The net effect of nevirapine binding is to change the direction of domain movements rather than suppress their mobilities
nevirapine
-
a non-nucleoside RT inhibitor, NNRTI, stronger effect of mutation N348I on RNase H susceptibility to nevirapine as compared with efavirenz
nevirapine
a nonnucleoside reverse transcriptase inhibitor, NNRTI
nevirapine
-
a nonnucleoside reverse transcriptase inhibitor
sodium 2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-naphthalen-1-ylguanosine

-
61% inhibition of RNase H at 0.05 microM
-
sodium 2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-naphthalen-1-ylguanosine
-
11% inhibition of RNase H at 0.05 microM
-
stavudine

-
a nucleoside reverse transcriptase inhibitor
[2-(4-chlorophenyl)hydrazinylidene]propanedioic acid

-
additionally inhibits DNA strand transfer and DNA polymerase activity of the retroviral reverse transcriptase
[2-(4-chlorophenyl)hydrazinylidene]propanedioic acid
-
inhibits RNase H activity, does not significantly affect DNA polymerase activity of reverse transcriptase. In the absence of DNA synthesis, [2-(4-chlorophenyl)hydrazinylidene]propanedioic acid interferes with the translocation, or repositioning, of the enzyme on the RNA-DNA template duplex. Inhibitor is highly specific for human immunodeficiency virus. The dicarboxylic acid moiety is essential for activity, and Mg2+ chelates directly with a Kd value of 2.4 mM
additional information

-
synthesis of 2-hydroxyisoquinoline-1,3(2H,4H)-dione derivatives as inhibitors of the RNase H activity of the reverse transcriptase of HIV-1, docking, study, overview. No inhibition by keto-5i and 5l
-
additional information
-
identification and evaluation of thiocarbamate and triazole inhibitors targeting RNase H activity of HIV reverse transcriptase, overview
-
additional information
-
design, synthesis, and screening of derivatives of 5-nitro-furan-2-carboxylic acid as inhibitors of the RNAse H activity of HIV-1 reverse transcriptase, overview. Modulation of the 5-nitro-furan-2-carboxylic moiety results in a drastic decrease in inhibitory potency. Binding mode of active derivatives, in which three oxygen atoms aligned in a straight form at the nitro-furan moiety are coordinated to two divalent metal ions located at RNase H reaction site. The nitro-furan-carboxylic moiety is one of the critical scaffolds for RNase H inhibition. Cytotoxicity of the synthesized compounds, overview
-
additional information
-
non-nucleoside RT inhibitors, NNRTIs, bind to an allosteric site that is 10 A from the polymerase active site and 60 A from the RNase H active site
-
additional information
-
no inhibition by 5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-piperidin-1-ylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one, 5,7-dihydroxy-2-(1-hydroxy-2-imadazol-1-yl-1-methyl ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one, 2-(2-diethylamino-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one, and 2-(1-benzylamino-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
additional information
structures of naphthyridinone-containing inhibitors bound to the RNase H active site, overview. This class of compounds binds to the active site via two metal ions that are coordinated by catalytic site residues, D443, E478, D498, and D549. The directionality of the naphthyridinone pharmacophore is restricted by the ordering of D549 and H539 in the RNase H domain
-
additional information
-
C-terminal domain mutations reduce RNase H activity either directly by affecting the RNase H cleavage activity of the enzyme, or indirectly by affecting the overall positioning of the template/primer strand, which in turn affects RNase H activity, template switching, polymerization and/or nucleotide excision. Effects of enzyme mutations on treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors, detailed overview. Nucleoside reverse transcriptase inhibitors are nucleoside analogues that lack the 3' OH on the sugar ring and competitively block reverse transcription by causing chain termination during DNA polymerization. Nucleoside reverse transcriptase inhibitors are prodrugs that require intracellular phosphorylation to the 5'-triphosphate formed by host cell kinases in order to become active. Nonnucleoside reverse transcriptase inhibitors in general are non-competitive inhibitors of RT that bind to a hydrophobic pocket near the polymerase active site, inducing conformational changes that inhibit RT enzymatic activity. Inhibition mechanisms of the two inhibitor classes, overview
-
additional information
-
mechanisms of catalysis and drug inhibition of polymerase and RNase H functions of RT by nucleos(t)ide reverse transcriptase inhibitor and non-nucleoside reverse transcriptase inhibitor drugs, and molecular mechanisms of drug resistance, detailed overview
-
additional information
-
discovery and development of bona fide RNase H inhibitors, overview
-
additional information
-
not inhibited by GSK5750
-
additional information
-
inhibitory potency and binding of dumbbell oligonucleotides to MoMuL virus RNase H, overview. The best dumbbell oligonucleotide, inhibitor contained phosphorothioate residues in both the loops
-
additional information
-
magnesium chelating 2-hydroxyisoquinoline-1,3(2H,4H)-diones, as inhibitors of HIV-1 integrase and/or the HIV-1 reverse transcriptase ribonuclease H domain, overview. 2-Hydroxyisoquinoline-1,3(2H,4H)-dione forms a 1:1 complex with Mg2+, but a 1:2 complex with Mn2+,
-
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0.00051
(2S)-5,7-dihydroxy-2-(2-hydroxy-1-(phenylsulfonyl)propan-2-yl)-9-methyl-3,4-dihydro-1H-benzo[7]annulen-6(2H)-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0193
(5E)-6-[1-(2,4-dimethylbenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0192
(5E)-6-[1-(2-chlorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.087
(5E)-6-[1-(3-methoxybenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0161
(5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.028
(5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoic acid
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0077
(5E)-6-[1-(4-fluorobenzyl)-4-phenyl-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoic acid
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.075
1,6,8-trihydroxy-3-methylanthraquinone
Human immunodeficiency virus 1
-
-
0.0008
1-(3-[[(4-benzyl-5-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]methyl]-4-methoxyphenyl)ethanone
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0002
1-hydroxy-4-((4-(morpholinomethyl)phenyl)amino)pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000079
1-hydroxy-4-((4-(pyridin-4-yl)phenyl)amino)pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.0002
1-hydroxy-4-([[3-(4-morpholinyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000398
1-hydroxy-4-([[3-(4-morpholinylmethyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.0001
1-hydroxy-4-([[4-(4-morpholinyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000016
1-hydroxy-4-([[4-(4-pyridinyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.00005
1-hydroxy-4-[[4-(4-morpholinyl)phenyl]amino]pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000003
1-hydroxy-4-[[4-(quinolin-3-yl)phenyl]amino]pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0006
2,7-dihydroxy-4-(propan-2-yl)cyclohepta-2,4,6-trien-1-one
Human immunodeficiency virus 1
-
-
0.0019
2-(1,2-dihydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00096
2-(1-benzylamino-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0061
2-(2,3-dihydro-1H-inden-1-ylamino)-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0055
2-(2,3-dihydro-1H-inden-2-ylamino)-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0013
2-(2-benzylsulfanyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0005
2-(2-diethylamino-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00024
2-(2-ethanesulfonyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00038
2-(2-ethylsulfanyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0012
2-(3,4-dichlorobenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acid
Human immunodeficiency virus 1
-
-
0.0009
2-(3-bromo-4-methoxybenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acid
Human immunodeficiency virus 1
-
-
0.018
2-(tert-butylamino)-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0071
2-amino-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.002
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0668
2-hydroxy-4-(3-phenyl)propylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.08
2-hydroxy-4-(4-methylbenzyl)isoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0427
2-hydroxy-4-(4-trifluoromethylbenzyl)isoquinoline-1,3(2H-4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0132
2-hydroxy-4-butylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0388
2-hydroxy-4-ethylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0185
2-hydroxy-4-isopropylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.000061
2-hydroxy-4-methoxycarbonylisoquinoline-1,3(2H, 4H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000061
2-hydroxy-4-methoxycarbonylisoquinoline-1,3(2H,4H)-dione
Moloney murine leukemia virus
-
pH 8.0, 37°C
0.0388 - 0.07
2-hydroxy-4-methylisoquinoline-1,3(2H,4H)-dione
0.0336
2-hydroxy-4-pentylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0468
2-hydroxy-4-propylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.00012 - 0.0591
2-hydroxyisoquinoline-1,3(2H,4H)-dione
0.0301
2-hydroxyisoquinoline-1,3(2H,4H)-dione magnesium complex
Moloney murine leukemia virus
-
pH 8.0, 37°C
-
0.0043
2-oxo-2-(1,2,3,4-tetrahydronaphthalen-1-ylamino)ethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0019
2-oxo-2-(phenylamino)ethyl dibenzylcarbamodithioate
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0132
2-oxo-2-(propan-2-yloxy)ethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0042
2-oxo-2-(tetrahydrofuran-2-ylamino)ethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0266
2-oxo-2-[(2,3,4-trichlorophenyl)amino]ethyl benzyl(phenyl)carbamodithioate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0033
2-oxo-2-[(2,3,4-trichlorophenyl)amino]ethyl dibenzylcarbamodithioate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0082
2-oxo-2-[(2-phenylpropan-2-yl)amino]ethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0033
2-[(2,3,4-trichlorophenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
Human immunodeficiency virus 1
-
pH 8.0, 25°C
0.0058
2-[(2,4-dichlorophenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0019
2-[(2,4-dimethylphenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
Human immunodeficiency virus 1
-
pH 8.0, 25°C; pH not specified in the publication, temperature not specified in the publication
0.00017
2-[(2-bromo-5-chloro-1-benzothiophen-3-yl)methyl]-5,6-dihydroxypyrimidine-4-carboxylic acid
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0083
2-[(2-methoxy-5-methylphenyl)amino]-2-oxoethyl benzyl(phenyl)carbamodithioate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0043
2-[(2-methyl-1-phenylpropan-2-yl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0058
2-[(2-methylbutan-2-yl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0114
2-[(3-cyanophenyl)amino]-2-oxoethyl benzyl(phenyl)carbamodithioate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0047
2-[(3-cyanophenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.005
2-[(4-hydroxybenzyl)(tetrahydrofuran-2-ylmethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0012
2-[2-(2-fluoro-benzylamino)-1-hydroxy-1-methyl-ethyl]-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.021
2-[2-(4-bromophenyl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.1
2-[2-(biphenyl-4-yl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0017
2-[4-benzyl-5-(benzylsulfanyl)-4H-1,2,4-triazol-3-yl]pyridine
Human immunodeficiency virus 1
-
pH 8.0, 25°C; pH not specified in the publication, temperature not specified in the publication
0.0026
2-[4-benzyl-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridine
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0077
2-[benzyl(tetrahydrofuran-2-ylmethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0142
2-[tert-butyl(2-phenylethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0098
2-[tert-butyl(3-nitrobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.05
2-[tert-butyl(3-oxo-3-phenylpropyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.05
2-[tert-butyl(3-phenylpropyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0085
2-[tert-butyl(4-fluorobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0075
2-[tert-butyl(4-methoxybenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0069
2-[tert-butyl(4-nitrobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0068
2-[tert-butyl(pentafluorobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0009
2-[tert-butyl(phenyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.009
2-[tert-butyl[2-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0085
2-[tert-butyl[3-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.008
2-[tert-butyl[4-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0128
2-[[2-(acetyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0087
2-[[4-(acetyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.05
2-[[4-(benzyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0001
3'-[(E)-[2-(3,4,5-trihydroxybenzoyl)hydrazinylidene]methyl]biphenyl-4-carboxylic acid
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0219
3,3-dimethyl-2-oxobutyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0065
3-(furan-2-yl)-4-(4-methoxybenzyl)-5-[[4-(trifluoromethyl)benzyl]sulfanyl]-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0047
3-(furan-2-yl)-4-phenyl-5-[[4-(trifluoromethyl)benzyl]sulfanyl]-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.029
3-[2-(4-bromophenyl)-2-oxoethoxy]-1,8-dihydroxy-6-methylanthracene-9,10-dione
Human immunodeficiency virus 1
-
-
0.000398
4-((cyclopropylmethyl)amino)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.00001
4-(([1,1'-biphenyl]-4-ylmethyl)amino)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000501
4-(4,4-difluoropiperidin-1-yl)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000032
4-([1,1'-biphenyl]-4-ylamino)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.004
4-([[4-benzyl-5-(furan-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0002 - 0.2
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
0.0149
4-benzyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0012
4-benzyl-3-(benzylsulfanyl)-5-(furan-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH 8.0, 25°C; pH not specified in the publication, temperature not specified in the publication
0.00021
4-benzyl-3-(benzylsulfanyl)-5-(thiophen-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH 8.0, 25°C; pH not specified in the publication, temperature not specified in the publication
0.001
4-benzyl-3-(benzylsulfanyl)-5-phenyl-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH 8.0, 25°C; pH not specified in the publication, temperature not specified in the publication
0.0038
4-benzyl-3-(furan-2-yl)-5-[(4-methoxybenzyl)sulfanyl]-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0028
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-(furan-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.001
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH 8.0, 25°C; pH not specified in the publication, temperature not specified in the publication
0.006
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-phenyl-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.001 - 0.0059
4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazole
0.001
4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-phenyl-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH 8.0, 25°C
0.045
4-heptyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0078 - 0.038
4-hexyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
0.0035
4-tert-butyl-N'-[(E)-(2-hydroxynaphthalen-1-yl)methylidene]benzohydrazide
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0066
4-[1-[(4-fluorophenyl)methyl]-7-(dimethylamino)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0068
4-[1-[(4-fluorophenyl)methyl]-7-(morpholin-4-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0033
4-[1-[(4-fluorophenyl)methyl]-7-(N-acetylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0262
4-[1-[(4-fluorophenyl)methyl]-7-(N-ethylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0185
4-[1-[(4-fluorophenyl)methyl]-7-(N-methylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0287
4-[1-[(4-fluorophenyl)methyl]-7-(piperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0057
4-[1-[(4-fluorophenyl)methyl]-7-[N-(3-chloroprop-1-yl)piperazin-1-yl]-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0032
4-[5-(benzoylamino)thiophen-2-yl]-2,4-dioxobutanoic acid
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000158
4-[[(4-fluorophenyl)methyl]amino]-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000045
4-[[4'-(aminomethyl)biphenyl-4-yl]methyl]-1-hydroxy-1,8-naphthyridin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0012
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-phenylaminoethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00093
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-phenylsulfanylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00082
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-piperidin-1-ylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00911
5,7-dihydroxy-2-(1-hydroxy-2-imadazol-1-yl-1-methyl ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00068
5,7-dihydroxy-2-(1-hydroxy-ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0038 - 0.0296
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
0.0026 - 0.0322
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
0.00013
6-[1-(4-fluorophenyl)methyl-1H-pyrrol-2-yl]-2,4-dioxo-5-hexenoic acid ethyl ester
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.039
9,10-dioxo-2-(2-oxo-2-phenylethoxy)-9,10-dihydroanthracen-1-yl acetate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.013
9,10-dioxo-9,10-dihydroanthracene-1,2-diyl dibenzoate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.000186 - 0.00047
ARK-2452
-
0.00007 - 0.0038
beta-thujaplicinol
0.0082
ethyl (5E)-6-[1-(2,4-dimethylbenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0073
ethyl (5E)-6-[1-(2-chlorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0063
ethyl (5E)-6-[1-(3-methoxybenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0086
ethyl (5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0112
ethyl (5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoate
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.008
ethyl (5E)-6-[1-(4-fluorobenzyl)-4-phenyl-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoate
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.00011
ethyl 1,4-dihydroxy-2-oxo-1,2-dihydro-1,8-naphthyridine-3-carboxylate
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0011 - 0.0048
F3284-8495
0.0019 - 0.0022
F3385-2581
0.0007 - 0.0021
F3385-2588
0.0004 - 0.0008
F3385-2590
0.00033
GSK5750
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.04
sodium 2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-naphthalen-1-ylguanosine, sodium 2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-[2-(4-nitrophenyl)ethyl]guanosine
Human immunodeficiency virus 1
-
-
-
0.0022 - 0.003
[2-(4-chlorophenyl)hydrazinylidene]propanedioic acid
0.0388
2-hydroxy-4-methylisoquinoline-1,3(2H,4H)-dione

Moloney murine leukemia virus
-
pH 8.0, 37°C
0.07
2-hydroxy-4-methylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.00012
2-hydroxyisoquinoline-1,3(2H,4H)-dione

Human immunodeficiency virus 1
-
-
0.0059
2-hydroxyisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0591
2-hydroxyisoquinoline-1,3(2H,4H)-dione
Moloney murine leukemia virus
-
pH 8.0, 37°C
0.0002
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine

Human immunodeficiency virus 1
-
pH 8.0, 25°C
0.0002
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.2
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.001
4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazole

Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0059
4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0078
4-hexyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione

Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.038
4-hexyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0038
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester

Human immunodeficiency virus 1
-
-
0.0084
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
Moloney murine leukemia virus
-
-
0.0265
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
Human immunodeficiency virus 1
-
-
0.0296
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
Human immunodeficiency virus 1
-
-
0.0026
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester

Human immunodeficiency virus 1
-
-
0.0086
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
Moloney murine leukemia virus
-
-
0.0267
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
Human immunodeficiency virus 1
-
-
0.0322
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
Human immunodeficiency virus 1
-
-
0.000186
ARK-2452

Human immunodeficiency virus 1
-
pH 8.0, 37°C, purified recombinant mutant p51-G-TCR construct
-
0.00047
ARK-2452
Human immunodeficiency virus 1
-
pH 8.0, 37°C, purified recombinant wild-type HIV-1 reverse transcriptase RNase H
-
0.00007
beta-thujaplicinol

Human immunodeficiency virus 1
-
mutant enzyme Y501A, at pH 7.8 and 37°C
0.00009
beta-thujaplicinol
Human immunodeficiency virus 1
-
mutant enzyme N474A, at pH 7.8 and 37°C
0.00015
beta-thujaplicinol
Human immunodeficiency virus 1
-
mutant enzyme R448A, at pH 7.8 and 37°C
0.000176
beta-thujaplicinol
Human immunodeficiency virus 1
-
pH 8.0, 37°C, purified recombinant mutant p51-G-TCR construct
0.00019
beta-thujaplicinol
Human immunodeficiency virus 1
-
mutant enzyme Q475A, at pH 7.8 and 37°C
0.00022
beta-thujaplicinol
Human immunodeficiency virus 1
-
mutant enzyme R557A, at pH 7.8 and 37°C
0.000257
beta-thujaplicinol
Human immunodeficiency virus 1
-
pH 8.0, 37°C, purified recombinant wild-type HIV-1 reverse transcriptase RNase H
0.0038
beta-thujaplicinol
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0011
F3284-8495

Human immunodeficiency virus 1
-
10 mM Mg2+, at pH 8.0 and 37°C
0.0048
F3284-8495
Human immunodeficiency virus 1
-
1 mM Mg2+, at pH 7.4 and 37°C
0.0019
F3385-2581

Human immunodeficiency virus 1
-
10 mM Mg2+, at pH 8.0 and 37°C
0.0022
F3385-2581
Human immunodeficiency virus 1
-
1 mM Mg2+, at pH 7.4 and 37°C
0.0007
F3385-2588

Human immunodeficiency virus 1
-
10 mM Mg2+, at pH 8.0 and 37°C
0.0021
F3385-2588
Human immunodeficiency virus 1
-
1 mM Mg2+, at pH 7.4 and 37°C
0.0004
F3385-2590

Human immunodeficiency virus 1
-
10 mM Mg2+, at pH 8.0 and 37°C
0.0008
F3385-2590
Human immunodeficiency virus 1
-
1 mM Mg2+, at pH 7.4 and 37°C
0.0022
[2-(4-chlorophenyl)hydrazinylidene]propanedioic acid

Human immunodeficiency virus 1
-
pH 7.6, 37°C
0.003
[2-(4-chlorophenyl)hydrazinylidene]propanedioic acid
Human immunodeficiency virus 1
-
pH 7.6, 37°C
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D549A
-
mutation in polypeptide p66, decrease in RNase H activity
D549N
-
mutation in polypeptide p66, decrease in RNase H activity
A360I
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
A360I/V
-
site-directed mutagenesis, a connection/RNase H domain mutant
A360K
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
A400T
-
mutation in the connection domain
A554K
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
A554L
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
A554T
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
C280E
-
RNase H activity similar to wild-type
C280H
-
RNase H activity similar to wild-type
C280L
-
RNase H activity similar to wild-type
C280M
-
RNase H activity similar to wild-type
C280P
-
significant reduction in RNase H activity. A heterodimer p66C280p/p51C280P shows about 8% of wild-type RNaseH activity, 6% of strand transfer activity, and 105% of DNA polymerase activity. A heterodimer p66C280P/p51 shows about 60% of wild-type RNaseH activity, 80% of strand transfer activity, and 100% of DNA polymerase activity. A heterodimer p66/p51C280W shows about 30% of wild-type RNaseH activity, 6% of strand transfer activity, and 99% of DNA polymerase activity
C280Q
-
RNase H activity similar to wild-type
C280R
-
RNase H activity similar to wild-type
C280S/K172A/K173A
-
p66/p51 HIV-1 reverse transcriptase 52A mutant variant, the mutation C208S resides in both subunits, the p66 subunit also contains the mutations K172A and K173A
C280W
-
significant reduction in RNase H activity. A heterodimer p66C280W/p51C280W shows about 11% of wild-type RNaseH activity, 6% of strand transfer activity, and 100% of DNA polymerase activity. A heterodimer p66C280W/p51 shows about 44% of wild-type RNaseH activity, 80% of strand transfer activity, and 98% of DNA polymerase activity. A heterodimer p66/p51C280W shows about 29% of wild-type RNaseH activity, 7% of strand transfer activity, and 100% of DNA polymerase activity
C280Y
-
RNase H activity similar to wild-type
D498N
-
active site mutant
D549N
-
mutation increases the 3'-azido-3'-deoxythymidine concentration needed to inhibit viral replication by 50% 12fold by increasing the time available for excision of incorporated nucleoside reverse transcriptase inhibitors from terminated primers and results in 5- to 10fold reduction in viral titers in a single-replication cycle assay
D67N/K70R/T215F
-
site-directed mutagenesis
D67N/K70R/T215F/Q509L
-
site-directed mutagenesis
E396A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
E399D
-
mutation in the connection domain
E44A
-
mutation involved in lamivudine resistance
E44D
-
mutation involved in lamivudine resistance
E475A
-
site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera
E478Q/N348I
-
mutation of RNase H active site and connection domain
E706Q
-
site-directed mutagenesis of HIV-1 reverse transcriptase, inactive mutant; site-directed mutagenesis of the recombinant mutant construct G, E706 in construct G corresponds to E478 in HIV-1 reverse transcriptase, inactive mutant
E89K
-
mutation involved in foscarnet resistance
F160S
-
site-directed mutagenesis
F227L
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
G190S
-
site-directed mutagenesis, the mutant virus shows moderately reduced fitness compared to that of the wild-type virus
G333D
-
mutation in the connection domain
G335C
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
G359A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
G509L
-
Glu to Leu substitution at residue 509 in the ribonuclease H domain of HIV-1 reverse transcriptase confers zidovudine resistance, mechanism, overview. Q509L increases zidovudine monophosphate excision activity of RT on RNA/DNA template/primers, but not DNA/DNA template/primers, due to Q509L decreasing a secondary RNase H cleavage event that reduces the RNA/DNA duplex length to 10 nucleotides and significantly impairs the enzyme's ability to excise the chain-terminating nucleotide. Mutation Q509L does not affect initial rates of the polymerase-directed RNase H activity but only polymerase-independent cleavages that occur after a template/primer dissociation event. Q509L decreases the affinity of the enzyme to bind template/primers with duplex lengths less than 18 nucleotides in the polymerase-independent RNase H cleavage mode, while not affecting the enzyme's affinity to bind the same template/primers in an zidovudine monophosphate excision competent mode
G544Stop
-
C-terminal truncation of p66 polypeptide. Loss of RNase H activity, while dimerization with polypepitde p51 and DNA polymerase activity are not significantly affected
H539F
-
mutation in isolated RNase H domain, mutant fails to bind RNA/DNA hybrids. Structure of mutant is similar to wild-type
H539N
-
increases the 3'-azido-3'-deoxythymidine concentration needed to inhibit viral replication by 50% 180fold relative to wild-type by increasing the time available for excision of incorporated nucleoside reverse transcriptase inhibitors from terminated primers
H539S
-
active site mutant
I505G
-
site-directed mutagenesis, the mutant exhibits a dimerization defect. The efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera
K219E
-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway
K219N
-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway
K390A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
K395A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
K451R
-
mutation present in viral isolates of 11% of antiviral treatment-experienced patients but remaining 100% conserved among treatment-naive patients
K558E
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, associated with an increase in thymidine analogue mutations, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
K558G
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, associated with an increase in thymidine analogue mutations, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
K558R
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, associated with an increase in thymidine analogue mutations, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
K65R/Q151M/A62V/V75I/F77L/F116Y
-
mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance
L100I
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
L469H
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
L469I
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
L469M
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
L469T
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
L74V
-
mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance
M184V
-
naturally occuring mutation in HIV infection patients, arises with abacavir, emtricitabine, or lamivudine treatment
M230L
-
the naturally occuring mutation leads to reduced RNase H activity of the HIV reverse transcriptase
N474A/Q475A
-
mutation reduces the viral titer 5- to 10fold, , reduction in the efficiency of DNA synthesis. Mutant is less efficient than the wild-type enzyme in its ability to remove a polypurine tract primer from a model substrate and has an altered RNase H cleavage specificity
N494D
-
mutant closely resembles the wild-type RNase H, exhibits an endonuclease activity and a processive RNase H activity, gives rise to small RNA hydrolysis products, and acts in concert with the reverse transcriptase
P236L
-
site-directed mutagenesis, the mutant virus shows substantially reduced fitness compared to that of the wild-type virus
P537Stop
-
C-terminal truncation of p66 polypeptide. Loss of RNase H activity, while dimerization with polypepitde p51 and DNA polymerase activity are not significantly affected
Q151M
-
mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance
Q151M/A62V/V75I/F77L/F116Y
-
mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance
Q475E
-
mutant exhibits a retarded endonuclease activity and an impaired 3'-5' processive RNA cleavage activity, gives rise to predominantly larger RNA hydrolysis products, is less processive in the presence of competitor substrate, and is defective in its ability to hydrolyze the polypurine tract and homopolymeric hybrids
Q500A
-
mutation reduces the viral titer less than 2-fold
R557A
-
the mutant shows about 5fold reduced kcat value compared to the wild type enzyme
R557S
-
active site mutant
T369I
-
mutation in the connection domain
T470E
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
T470K
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
T470P
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
T470S
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
T473C
-
the mutation increases the sensitivity of the enzyme for inhibitor NSC727447 by 50fold
T473M
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
V552Stop
-
C-terminal truncation of p66 polypeptide. Mutant retains endonuclease activity but lacks the directional processing feature of wild-type and barely supports transfer of nascent (-)-stranded DNA between RNA templates
W229F
-
mutation in primer grip residue, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type
W229F/Y232W
-
mutation in primer grip residues, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type
W229Y
-
mutation in primer grip residue, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type
W88G
-
mutation involved in foscarnet resistance
Y188C
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
Y188L
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
Y229F/Y232F
-
mutation in primer grip residues, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type
Y232W
-
mutation in primer grip residue, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type
Y318F
-
mutation in the connection domain
E478Q
-
RNase H active site mutant
-
E478Q/N348I
-
mutation of RNase H active site and connection domain
-
K103N
-
a classic NNRTI resistance mutation
-
N348I
-
connection domain mutant, altered RNase H cleavage pattern compared to the wild-type HIV-1 RT
-
Y181C
-
a classic NNRTI resistance mutation
-
E396A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
-
K390A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
-
K395A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
-
K65R
-
naturally occuring mutation in HIV infection patients, arises with abacavir, didanosine, emtricitabine, lamivudine, or tenofovir disoproxil fumarate treatment
-
M230L
-
the naturally occuring mutation leads to reduced RNase H activity of the HIV reverse transcriptase
-
Y501A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
-
Q294P
-
site-directed mutagenesis of a residue in the catalytically inactive p54 subunit resulting in an increase in RNase H activity comparable with that of HIV-1 reverse transcriptase
A128T
-
the mutant strain is resistant to 2-hydroxyisoquinoline-1,3(2H,4H)-dione inhibitors in contrast to the wild-type
C635V
-
site-directed mutagenesis, the mutant shows slightly reduced reverse transcriptase and RNAse H activities compared the wild-type enzyme
D524A
-
mutant lacks RNase H activity, but retains reverse transcriptase activity. Elimination of RNase H activity enhances the intrinsic thermal stability of the protein rather than its affinity to template-primer; site-directed mutagenesis, RNase H-inactive mutant, that shows increased intrinsic thermal stability compared to the wild-type enzyme. The mutant loses RNase H activity through abolishing of Mg2+ binding to the RNase H domain
D583A
-
site-directed mutagenesis, RNase H-inactive mutant, that shows increased intrinsic thermal stability compared to the wild-type enzyme. The mutant loses RNase H activity through abolishing of Mg2+ binding to the RNase H domain
D583N
-
less than 0.5% of wild-type activity, no binding of Mn2+
D653N
-
4% of wild-type activity
E562Q
-
less than 0.5% of wild-type activity, no binding of Mn2+
G140S/Q148H
-
the mutant strain is resistant to 2-hydroxyisoquinoline-1,3(2H,4H)-dione inhibitors in contrast to the wild-type
H638G
-
15% of wild-type activity
D358N
-
mutation eliminates Mg2+- and Mn2+-dependent RNase H function
D426N
-
mutation eliminates Mg2+- and Mn2+-dependent RNase H function
D469N
-
reduced RNase H activity in presence of Mg2+, decrease of turnover rate in presence of Mn2+. Mutant fails to support DNA strand transfer and release of the (+)-strand polypurine tract primer from (+)-RNA
E401Q
-
mutation eliminates Mg2+- and Mn2+-dependent RNase H function
H427A
-
reduced RNase H activity in presence of Mg2+, decrease of turnover rate in presence of Mn2+. Mutant fails to support DNA strand transfer and release of the (+)-strand polypurine tract primer from (+)-RNA
Y459A
-
reduced RNase H activity in presence of Mg2+, decrease of turnover rate in presence of Mn2+. Mutant fails to support DNA strand transfer and release of the (+)-strand polypurine tract primer from (+)-RNA
E478Q

-
the efficiency with which mutant RT catalyzes transfer of nascent DNA between RNA templates is severely reduced
E478Q
-
mutation in polypeptide p66, loss of RNase H activity
A360V

-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
A360V
-
naturally occuring mutant from clinical isolates, a connection/RNase H domain mutant that shows reduced RNase H activity
A371V

-
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B, whereas the G335D and A371V substitutions are commonly observed in 69% and 75% of non-B HIV-1 isolates, respectively
A371V
-
mutation in the connection domain
A371V
-
site-directed mutagenesis, a connection/RNase H domain mutant
A376S

-
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B. Mutations N348I, A376S and Q509L do confer varying amounts of nevirapine resistance by themselves, even in the absence of excision-enhancing mutations
A376S
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
C280S

-
RNase H activity similar to wild-type
C280S
-
site-directed mutagenesis
D67N

-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway
D67N
-
mutation involved in zidovudine resistance
E312Q

-
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B
E312Q
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
E478Q

-
mutation in isolated RNase H domain, mutant fails to bind RNA/DNA hybrids. Structure of mutant is similar to wild-type
E478Q
-
RNase H active site mutant
G190A

-
site-directed mutagenesis, the mutant virus shows moderately reduced fitness compared to that of the wild-type virus
G190A
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
G333E

-
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B
G333E
-
mutation in the connection domain
G335D

-
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B, whereas the G335D and A371V substitutions are commonly observed in 69% and 75% of non-B HIV-1 isolates, respectively
G335D
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
I505A

-
no discernible effect on viral titer
I505A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
K103N

-
site-directed mutagenesis, the mutation does not affect RNase H function
K103N
-
a classic NNRTI resistance mutation
K103N
-
site-directed mutagenesis, the mutant virus shows fitness similar to that of the wild-type virus
K103N
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
K219Q

-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway
K219Q
-
mutation involved in zidovudine resistance
K476A

-
site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera
K476A
-
mutation reduces the viral titer less than 2fold
K476A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
K65R

-
naturally occuring mutation in HIV infection patients, arises with abacavir, didanosine, emtricitabine, lamivudine, or tenofovir disoproxil fumarate treatment
K65R
-
mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance
K70R

-
naturally occuring mutation in HIV infection patients, is common to stavudine, tenofovir disoproxil fumarate, and zidovudine therapy; thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway
K70R
-
mutation involved in zidovudine resistance
L210W

-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-1 pathway
L210W
-
mutation involved in zidovudine resistance
M41L

-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-1 pathway
M41L
-
mutation involved in zidovudine resistance
N348I

-
mutations N348I, A376S and Q509L do confer varying amounts of nevirapine resistance by themselves, even in the absence of excision-enhancing mutations
N348I
-
connection domain mutant, altered RNase H cleavage pattern compared to the wild-type HIV-1 RT
N348I
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
N348I
-
naturally occuring mutant from clinical isolates, a connection/RNase H domain mutant that shows reduced RNase H activity
N474A

-
mutation reduces the viral titer less than 2fold
N474A
-
the mutant shows about 40fold reduced kcat value compared to the wild type enzyme
Q475A

-
mutation reduces the viral titer 5- to 10fold
Q475A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
Q475A
-
the mutant shows about 10fold reduced kcat value compared to the wild type enzyme
Q509L

-
mutations N348I, A376S and Q509L do confer varying amounts of nevirapine resistance by themselves, even in the absence of excision-enhancing mutations
Q509L
-
mutation in the RNase H domain, the mutation significantly contributes to zidovudine resistance
Q509L
-
site-directed mutagenesis, a connection/RNase H domain mutant
R448A

-
no discernible effect on viral titer
R448A
-
the mutant shows about 3fold reduced kcat value compared to the wild type enzyme
T215F

-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway
T215F
-
mutation involved in zidovudine resistance
T215Y

-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-1 pathway
T215Y
-
mutation involved in zidovudine resistance
T473A

-
site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera
T473A
-
mutation abolishes viral replication
V106A

-
site-directed mutagenesis, the mutant virus shows moderately reduced fitness compared to that of the wild-type virus
V106A
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
V365I

-
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B
V365I
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
Y181C

-
site-directed mutagenesis, the mutation does not affect RNase H function
Y181C
-
a classic NNRTI resistance mutation
Y181C
-
site-directed mutagenesis, the mutant virus shows fitness similar to that of the wild-type virus
Y181C
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
Y181C
-
site-directed mutagenesis, the mutant shows resistance to non-nucleoside reverse transcriptase inhibitors
Y501A

-
site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera
Y501A
-
mutation reduces the viral titer 5- to 10fold, reduction in the efficiency of DNA synthesis. Mutant is less efficient than the wild-type enzyme in its ability to remove a polypurine tract primer from a model substrate and has an altered RNase H cleavage specificity
Y501A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
Y501A
-
the mutant shows about 400fold reduced kcat valuecompared to the wild type enzyme
D524N

-
loss of catalytic activity. Construction of vectors encapsidated in virions engineered to contain phenotypic mixtures of wild-type and RNase H catalytic site point mutant D524N reverse transcriptase. There is a steady decline in direct repeat deletion frequency that correlates with decreases in functional RNase H, with greater than fourfold decreases in repeat deletion frequency observed when 95% of virion reverse transcriptase is RNase H defective
D524N
-
less than 0.5% of wild-type activity, no binding of Mn2+
additional information

-
RNase H primer grip mutations suppress polymerization-independent RNase H cleavage. Alteration of RNase H primer grip residues Thr473, Asn474, and Gln475 has little influence on cleavage specificity. Altering the RNase H domain of HIV-1 RT can impact significantly on the ability of mutant enzymes to catalyze DNA synthesis, but all RNase H primer grip mutants show little difference in their DNA-dependent DNA polymerase activity
additional information
-
construction of chimeric HIV-1/HIV-2 reverse transcriptases, in which protein segments and/or subunits are exchanged. The RNase H specific activity of the chimeric enzymes is either high like HIV-1 reverse transcriptase or low like HIV-2 reverse transcriptase. The origin of the thumb subdomain in the small subunit of the chimeric reverse transcriptases, residues 244-322 determines the level of the RNase H activity
additional information
-
chemical modifications by thiol-specific reagents of cysteine 280, located in a helix I in the thumb subdomain of the polymerase domain, affect substantially only the RNase H activity
additional information
-
construction of two chimeric enzymes by swapping the RNase H domains between HIV-1 RT and Moloney murine leukemia virus MuLV RT. Chimeric HIV-1 RT, having the RNase H domain of MuLV RT, inherits the divalent cation preference characteristic of MuLV RT on the DNA template with no significant change on the RNA template. Chimeric MuLV RT, likewise partially inherits the metal ion preference of HIV-1 RT. Unlike the wild-type MuLV RT, chimeric MuLV RT is able to use both Mn-dNTP and Mg-dNTP on the RNA template with similar efficiency, while a 30-fold higher preference for Mn.dNTP was seen on the DNA template. The metal preferences for the RNase H activity of chimeric HIV-1 RT and chimeric MuLV RT are, respectively, Mn2+ and Mg2+, a property acquired through their swapped RNase H domains. Chimeric HIV-1 RT displays higher fidelity and discrimination against rNTPs than against dNTPs substrates, a property inherited from MuLV RT. The overall fidelity of the chimeric MuLV RT is decreased in comparison to the parental MuLV RT, suggesting that the RNase H domain profoundly influences the function of the polymerase domain
additional information
-
construction of an N-terminally His-tagged mutant p51-G-TCR construct designed to encode the p51 subunit joined by a linker to the thumb (T), connection (C), and RNase H (R) domains of p66, the p51-G-TCR RNase H construct displays Mg2+-dependent activity using a fluorescent nonspecific assay and shows the same cleavage pattern as HIV-1 reverse transcriptase on substrates that mimic the tRNA removal required for second-strand transfer reactions. The RNase H of the p51-G-TCR RNase H construct and wild-type HIV-1 reverse transcriptase have similar Kms for an RNA-DNA hybrid substrate and show similar inhibition kinetics to two known inhibitors of the HIV-1 reverse transcriptase RNase H, molecular modeling
additional information
-
construction of chimeric HIV-1/HIV-2 reverse transcriptases, in which protein segments and/or subunits are exchanged. The RNase H specific activity of the chimeric enzymes is either high like HIV-1 reverse transcriptase or low like HIV-2 reverse transcriptase. The origin of the thumb subdomain in the small subunit of the chimeric reverse transcriptases, residues 244-322 determines the level of the RNase H activity
additional information
-
construction of chimeric HIV-1/HIV-2 reverse transcriptases, in which protein segments and/or subunits are exchanged. The RNase H specific activity of the chimeric enzymes is either high like HIV-1 reverse transcriptase or low like HIV-2 reverse transcriptase. The origin of the thumb subdomain in the small subunit of the chimeric reverse transcriptases, residues 244-322 determines the level of the RNase H activity
-
additional information
-
construction of chimeric HIV-1/HIV-2 reverse transcriptases, in which protein segments and/or subunits are exchanged. The RNase H specific activity of the chimeric enzymes is either high like HIV-1 reverse transcriptase or low like HIV-2 reverse transcriptase. The origin of the thumb subdomain in the small subunit of the chimeric reverse transcriptases, residues 244-322 determines the level of the RNase H activity
-
additional information
-
deletion of 204 nucleotides at the 3'-terminus results in 4fold increase in activity level upon recombinant expression and allows for high-level production of the protein
additional information
-
construction of two chimeric enzymes by swapping the RNase H domains between HIV-1 RT and Moloney murine leukemia virus MuLV RT. Chimeric HIV-1 RT, having the RNase H domain of MuLV RT, inherits the divalent cation preference characteristic of MuLV RT on the DNA template with no significant change on the RNA template. Chimeric MuLV RT, likewise partially inherits the metal ion preference of HIV-1 RT. Unlike the wild-type MuLV RT, chimeric MuLV RT is able to use both Mn-dNTP and Mg-dNTP on the RNA template with similar efficiency, while a 30-fold higher preference for Mn.dNTP was seen on the DNA template. The metal preferences for the RNase H activity of chimeric HIV-1 RT and chimeric MuLV RT are, respectively, Mn2+ and Mg2+, a property acquired through their swapped RNase H domains. Chimeric HIV-1 RT displays higher fidelity and discrimination against rNTPs than against dNTPs substrates, a property inherited from MuLV RT. The overall fidelity of the chimeric MuLV RT is decreased in comparison to the parental MuLV RT, suggesting that the RNase H domain profoundly influences the function of the polymerase domain
additional information
-
site-directed chemical modification of the RNase H domain by selectively PEGylating Cys635, one of the eight cysteine residues present in the reverse transcriptase, specifically inactivates its ribonucleolytic activity, PEGylation as a tool for engineering the M-MuLV RT derivative deficient in RNase H activity, overview
additional information
-
construction of a chimeric enzyme containing the first 425 amino acid residues from the N-terminal domain of HIV-1 reverse transcriptase, i.e. the polymerase domain, and 200 amino acid residues from the C-terminal domain of murine leukemia virus reverse transcriptase, i.e. RNase H-domain. The chimeric enzyme exists as a monomer with intact DNA polymerase and RNase-H functions. It is able to catalyze both endonucleolytic and processive RNase-H functions in a manner similar to the wild type HIV-1 reverse transcriptase and murineleukemia virus reverse transcriptase
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Nucleic Acids Res.
38
1048-1056
2010
Human immunodeficiency virus 1
brenda
Himmel, D.M.; Maegley, K.A.; Pauly, T.A.; Bauman, J.D.; Das, K.; Dharia, C.; Clark, A.D.; Ryan, K.; Hickey, M.J.; Love, R.A.; Hughes, S.H.; Bergqvist, S.; Arnold, E.
Structure of HIV-1 reverse transcriptase with the inhibitor beta-thujaplicinol bound at the RNase H active site
Structure
17
1625-1635
2009
Human immunodeficiency virus 1 (P03366)
brenda
Talele, T.; Upadhyay, A.; Pandey, V.
Influence of the RNase H domain of retroviral reverse transcriptases on the metal specificity and substrate selection of their polymerase domains
Virol. J.
6
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2009
Human immunodeficiency virus 1, Moloney murine leukemia virus
brenda
Xu, H.; Quan, Y.; Schader, S.; Oliveira, M.; Bar-Magen, T.; Wainberg, M.
The M230L nonnucleoside reverse transcriptase inhibitor resistance mutation in HIV-1 reverse transcriptase impairs enzymatic function and viral replicative capacity
Antimicrob. Agents Chemother.
54
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2010
Human immunodeficiency virus 1, Human immunodeficiency virus 1 HXB2
brenda
Farias, R.V.; Vargas, D.A.; Castillo, A.E.; Valenzuela, B.; Cote, M.L.; Roth, M.J.; Leon, O.
Expression of an Mg2+-dependent HIV-1 RNase H construct for drug screening
Antimicrob. Agents Chemother.
55
4735-4741
2011
Human immunodeficiency virus 1
brenda
Yanagita, H.; Urano, E.; Matsumoto, K.; Ichikawa, R.; Takaesu, Y.; Ogata, M.; Murakami, T.; Wu, H.; Chiba, J.; Komano, J.; Hoshino, T.
Structural and biochemical study on the inhibitory activity of derivatives of 5-nitro-furan-2-carboxylic acid for RNase H function of HIV-1 reverse transcriptase
Bioorg. Med. Chem.
19
816-825
2011
Human immunodeficiency virus 1
brenda
Kumar, A.
Binding of dumbbell oligonucleotides to MoMuLV reverse transcriptase: inhibitory properties of RNase H activity
E-J. Chem.
7
701-708
2010
Moloney murine leukemia virus
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brenda
Billamboz, M.; Bailly, F.; Lion, C.; Calmels, C.; Andreola, M.L.; Witvrouw, M.; Christ, F.; Debyser, Z.; De Luca, L.; Chimirri, A.; Cotelle, P.
2-hydroxyisoquinoline-1,3(2H,4H)-diones as inhibitors of HIV-1 integrase and reverse transcriptase RNase H domain: influence of the alkylation of position 4
Eur. J. Med. Chem.
46
535-546
2011
Human Immunodeficiency Virus
brenda
Esposito, F.; Kharlamova, T.; Distinto, S.; Zinzula, L.; Cheng, Y.C.; Dutschman, G.; Floris, G.; Markt, P.; Corona, A.; Tramontano, E.
Alizarine derivatives as new dual inhibitors of the HIV-1 reverse transcriptase-associated DNA polymerase and RNase H activities effective also on the RNase H activity of non-nucleoside resistant reverse transcriptases
FEBS J.
278
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2011
Human immunodeficiency virus 1
brenda
Biondi, M.J.; Beilhartz, G.L.; McCormick, S.; Goette, M.
N348I in HIV-1 reverse transcriptase can counteract the nevirapine-mediated bias toward RNase H cleavage during plus-strand initiation
J. Biol. Chem.
285
26966-26975
2010
Human immunodeficiency virus 1, Human immunodeficiency virus 1 HXB-2
brenda
Billamboz, M.; Bailly, F.; Lion, C.; Touati, N.; Vezin, H.; Calmels, C.; Andreola, M.; Christ, F.; Debyser, Z.; Cotelle, P.
Magnesium chelating 2-hydroxyisoquinoline-1,3(2H, 4H)-diones, as inhibitors of HIV-1 integrase and/or the HIV-1 reverse transcriptase ribonuclease H domain: Discovery of a novel selective inhibitor of the ribonuclease H function
J. Med. Chem.
54
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2011
Moloney murine leukemia virus
brenda
Chung, S.; Himmel, D.; Jiang, J.; Wojtak, K.; Bauman, J.; Rausch, J.; Wilson, J.; Beutler, J.; Thomas, C.; Arnold, E.; Le Grice, S.
Synthesis, activity, and structural analysis of novel alpha-hydroxytropolone inhibitors of human immunodeficiency virus reverse transcriptase-associated ribonuclease H
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2011
Human immunodeficiency virus 1
brenda
Su, H.P.; Yan, Y.; Prasad, G.S.; Smith, R.F.; Daniels, C.L.; Abeywickrema, P.D.; Reid, J.C.; Loughran, H.M.; Kornienko, M.; Sharma, S.; Grobler, J.A.; Xu, B.; Sardana, V.; Allison, T.J.; Williams, P.D.; Darke, P.L.; Hazuda, D.J.; Munshi, S.
Structural basis for the inhibition of RNase H activity of HIV-1 reverse transcriptase by RNase H active site-directed inhibitors
J. Virol.
84
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2010
Human immunodeficiency virus 1 (P0C6F2), Human immunodeficiency virus 1 HXB2 (P0C6F2)
brenda
Wang, J.; Bambara, R.A.; Demeter, L.M.; Dykes, C.
Reduced fitness in cell culture of HIV-1 with nonnucleoside reverse transcriptase inhibitor-resistant mutations correlates with relative levels of reverse transcriptase content and RNase H activity in virions
J. Virol.
84
9377-9389
2010
Human immunodeficiency virus 1
brenda
Radzvilavicius, T.; Lagunavicius, A.
Selective inactivation of M-MuLV RT RNase H activity by site-directed PEGylation: an improved ability to synthesize long cDNA molecules
New Biotechnol.
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2012
Moloney murine leukemia virus
brenda
Lu, M.; Ngo, W.; Mei, Y.; Munshi, V.; Burlein, C.; Loughran, M.; Williams, P.; Hazuda, D.; Miller, M.; Grobler, J.; Diamond, T.; Lai, M.
Purification of untagged HIV-1 reverse transcriptase by affinity chromatography
Protein Expr. Purif.
71
231-239
2010
Human immunodeficiency virus 1
brenda
Delviks-Frankenberry, K.A.; Nikolenko, G.N.; Pathak, V.K.
The connection between HIV drug resistance and RNase H
Viruses
2
1476-1503
2010
Human immunodeficiency virus 1, Human immunodeficiency virus 1 HXB2
brenda
Singh, K.; Marchand, B.; Kirby, K.; Michailidis, E.; Sarafianos, S.
Structural aspects of drug resistance and inhibition of HIV-1 reverse transcriptase
Viruses
2
606-638
2010
Human immunodeficiency virus 1
brenda
Beilhartz, G.; Goette, M.
HIV-1 ribonuclease H: structure, catalytic mechanism and inhibitors
Viruses
2
900-926
2010
Human immunodeficiency virus 1, Human immunodeficiency virus 2
brenda
Sarafianos, S.G.; Das, K.; Tantillo, C.; Clark, A.D., Jr.; Ding, J.; Whitcomb, J.M.; Boyer, P.L.; Hughes, S.H.; Arnold, E.
Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA
EMBO J.
20
1449-1461
2001
Human immunodeficiency virus 1 (P03366)
brenda
Broecker, F.; Andrae, K.; Moelling, K.
Premature activation of the HIV RNase H drives the virus into suicide: a novel microbicide?
AIDS Res. Hum. Retroviruses
28
1397-1403
2012
Human Immunodeficiency Virus
brenda
Corona, A.; Di Leva, F.S.; Thierry, S.; Pescatori, L.; Cuzzucoli Crucitti, G.; Subra, F.; Delelis, O.; Esposito, F.; Rigogliuso, G.; Costi, R.; Cosconati, S.; Novellino, E.; Di Santo, R.; Tramontano, E.
Identification of highly conserved residues involved in inhibition of HIV-1 RNase H function by diketo acid derivatives
Antimicrob. Agents Chemother.
58
6101-6110
2014
Human immunodeficiency virus 1
brenda
Muchiri, J.M.; Li, D.; Dykes, C.; Bambara, R.A.
Efavirenz stimulates HIV-1 reverse transcriptase RNase H activity by a mechanism involving increased substrate binding and secondary cleavage activity
Biochemistry
52
4981-4990
2013
Human immunodeficiency virus 1
brenda
Ilina, T.; Labarge, K.; Sarafianos, S.G.; Ishima, R.; Parniak, M.A.
Inhibitors of HIV-1 reverse transcriptase-associated ribonuclease H activity
Biology
1
521-541
2012
Human immunodeficiency virus 1
brenda
Velthuisen, E.J.; Johns, B.A.; Gerondelis, P.; Chen, Y.; Li, M.; Mou, K.; Zhang, W.; Seal, J.W.; Hightower, K.E.; Miranda, S.R.; Brown, K.; Leesnitzer, L.
Pyridopyrimidinone inhibitors of HIV-1 RNase H
Eur. J. Med. Chem.
83
609-616
2014
Human immunodeficiency virus 1
brenda
Corona, A.; Masaoka, T.; Tocco, G.; Tramontano, E.; Le Grice, S.F.
Active site and allosteric inhibitors of the ribonuclease H activity of HIV reverse transcriptase
Future Med. Chem.
5
2127-2139
2013
Human immunodeficiency virus 1
brenda
Beilhartz, G.L.; Ngure, M.; Johns, B.A.; DeAnda, F.; Gerondelis, P.; Goette, M.
Inhibition of the ribonuclease H activity of HIV-1 reverse transcriptase by GSK5750 correlates with slow enzyme-inhibitor dissociation
J. Biol. Chem.
289
16270-16277
2014
Human immunodeficiency virus 1
brenda
Costi, R.; Metifiot, M.; Chung, S.; Cuzzucoli Crucitti, G.; Maddali, K.; Pescatori, L.; Messore, A.; Madia, V.N.; Pupo, G.; Scipione, L.; Tortorella, S.; Di Leva, F.S.; Cosconati, S.; Marinelli, L.; Novellino, E.; Le Grice, S.F.; Corona, A.; Pommier, Y.; Marchand, C.; Di Santo, R.
Basic quinolinonyl diketo acid derivatives as inhibitors of HIV integrase and their activity against RNase H function of reverse transcriptase
J. Med. Chem.
57
3223-3234
2014
Human immunodeficiency virus 1
brenda
Himmel, D.M.; Myshakina, N.S.; Ilina, T.; Van Ry, A.; Ho, W.C.; Parniak, M.A.; Arnold, E.
Structure of a dihydroxycoumarin active-site inhibitor in complex with the RNase H domain of HIV-1 reverse transcriptase and structure-activity analysis of inhibitor analogs
J. Mol. Biol.
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2617-2631
2014
Human immunodeficiency virus 1
brenda
Zheng, X.; Mueller, G.A.; DeRose, E.F.; London, R.E.
Metal and ligand binding to the HIV-RNase H active site are remotely monitored by Ile556
Nucleic Acids Res.
40
10543-10553
2012
Human immunodeficiency virus 1
brenda
Alvarez, M.; Barrioluengo, V.; Afonso-Lehmann, R.N.; Menendez-Arias, L.
Altered error specificity of RNase H-deficient HIV-1 reverse transcriptases during DNA-dependent DNA synthesis
Nucleic Acids Res.
41
4601-4612
2013
Human immunodeficiency virus 1
brenda
Zheng, X.; Pedersen, L.C.; Gabel, S.A.; Mueller, G.A.; Cuneo, M.J.; DeRose, E.F.; Krahn, J.M.; London, R.E.
Selective unfolding of one ribonuclease H domain of HIV reverse transcriptase is linked to homodimer formation
Nucleic Acids Res.
42
5361-5377
2014
Human immunodeficiency virus 1
brenda
Das, K.; Martinez, S.E.; Bandwar, R.P.; Arnold, E.
Structures of HIV-1 RT-RNA/DNA ternary complexes with dATP and nevirapine reveal conformational flexibility of RNA/DNA: insights into requirements for RNase H cleavage
Nucleic Acids Res.
42
8125-8137
2014
Human immunodeficiency virus 1 (P03366)
brenda