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Information on EC 3.1.13.2 - exoribonuclease H and Organism(s) Moloney murine leukemia virus and UniProt Accession P03355
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3.1.13.2 exoribonuclease HSpecify your search results
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- 3.1.13.2
- strand
- duplex
- nucleic
- rna-dna
-
single-stranded
-
integrase
-
r-loops
- oligodeoxynucleotides
-
retrotransposons
- heteroduplexes
- transcriptases
- phosphorothioate
- retroviruses
-
polypurine
-
moloney
-
phosphodiester
-
exonuclease
-
rna-dependent
- pre-mrnas
- nucleases
- oligodeoxyribonucleotides
-
plus-strand
-
nnrti
-
template-primer
-
nucleocapsids
-
minus-strand
- dntp
-
spliceosome
-
myeloblastosis
-
thumb
-
endonucleolytic
-
oligonucleotide-directed
-
2'-o-methylated
- nevirapine
-
snrnp
- oligoribonucleotide
-
primer-template
-
okazaki
-
nonnucleoside
-
rna-directed
-
a-form
- efavirenz
-
retroelements
- 3'-exonuclease
-
heteropolymeric
-
phosphoramidite
-
pregenomic
-
hepadnavirus
- hiv-rt
- pharmacology
- medicine
- drug development
-
internucleotide
The taxonomic range for the selected organisms is: Moloney murine leukemia virus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
rnase h, rnase h1, rnase hi, rnaseh, rt rnase h, hiv rnase h, t4 rnase h, rt/rnase h, lc11-rnase h1, retroviral rnase h, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
RNase H
retroviral reverse transcriptase RNaseH
-
-
-
-
RNase H
additional information
-
the enzyme is part of the viral reverse transcriptase
RNase H
-
retroviral reverse transcriptases possess both a DNA polymerase and an RNase H activity
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
the selection of 5'-end-directed cleavage sites by the retroviral RNase H results from a combination of nucleotide sequence, permissible distance, and accessibility to the RNA 5'-end
-
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
RNase H domain structure and mechanism of catalysis
-
3'-end directed exonucleolytic cleavage of viral RNA-DNA hybrid
RNase H utilizes a two-metal ion mechanism of catalysis, the first metal ion A activates the nucleophilic water molecule and the second metal ion B, possibly in conjunction with metal ion A, stabilizes the transition state intermediate, substrate interactions, reaction mechanism and cleavage mode, overview
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9050-76-4
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
DNA/DNA + H2O
?
RNase H catalysis by the retroviral enzyme appears to involve a two-metal ion mechanism. Unlike cellular RNases H, the retroviral RNase H displays three different modes of cleavage: internal, 3'-end-DNA-directed, and 5'-end-RNA-directed, all three modes of cleavage appear to have essential roles in reverse transcription, overview, RNase H activities of murine retroviral reverse transcriptases preferentially cleave between two ribonucleotide residues in an RNA chain, and between the penultimate and last ribonucleotide of an extended RNA primer rather than precisely at the RNA-DNA junction
-
-
?
DNA-RNA hybrid + H2O
?
-
cleavage site recognition and specificity, mechanism, in vitro synthesis of substrates, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
in vitro synthesis of substrates, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
sequence preference for internal cleavage. 3 distinct cleavage modes are described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages
-
-
?
DNA-RNA hybrid + H2O
?
-
a Cy3-Tr35/Pd22 RNA-DNA hybrid is cut at approximately 19 base pair upstream from the 3' primer end
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
4-30 nucleotides in length
?
RNA/DNA hybrid + H2O
?
RNase H catalysis by the retroviral enzyme appears to involve a two-metal ion mechanism. Unlike cellular RNases H, the retroviral RNase H displays three different modes of cleavage: internal,3'-end-DNA-directed, and 5'-end-RNA-directed, all three modes of cleavage appear to have essential roles in reverse transcription, overview
-
-
?
RNA/DNA hybrid + H2O
?
-
secondary structure and substrate binding, overview
-
-
?
additional information
?
-
-
retroviral RNases H display three different modes of cleavage: internal, DNA 3' end-directed, and RNA 5' end-directed
-
-
?
additional information
?
-
retroviral RNases H display three different modes of cleavage: internal, DNA 3' end-directed, and RNA 5' end-directed
-
-
?
additional information
?
-
RNase H activity is determined by measuring the [3H]oligo(rA) released from [3H]poly(rA)*p(dT)45
-
-
?
additional information
?
-
-
RNase H activity is determined by measuring the [3H]oligo(rA) released from [3H]poly(rA)*p(dT)45
-
-
?
additional information
?
-
-
the enzyme is essential for retroviral replication
-
-
?
additional information
?
-
-
the enzyme is essential to complete retroviral replication
-
-
?
additional information
?
-
-
the enzyme recognizes 3' ends of DNA and 5' ends of RNA for cleavage, the enzyme cleaves downstream of a nick, recognition of internal cleavage sites, influence of 5' end position of upstream RNA on cleavage of downstream RNA, overview
-
-
?
additional information
?
-
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, i.e. NRTIs
-
-
?
additional information
?
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, i.e. NRTIs
-
-
?
additional information
?
-
-
the polymerization-dependent RNase H activity is insufficient to completely degrade the genomic template during minus-strand synthesis, pausing by reverse transcriptase during transcription promotes RNase H cleavages and facilitates strand transfers, overview, cleavage site selection modelling, overview, the isolated MoMLV RNase H domain retains enzymatic activity, but is unable to carry out specific cleavages such as removal of the tRNA or PPT primers in vitro, cleavage specificity of RNase H, overview
-
-
?
additional information
?
-
the polymerization-dependent RNase H activity is insufficient to completely degrade the genomic template during minus-strand synthesis, pausing by reverse transcriptase during transcription promotes RNase H cleavages and facilitates strand transfers, overview, cleavage site selection modelling, overview, the isolated MoMLV RNase H domain retains enzymatic activity, but is unable to carry out specific cleavages such as removal of the tRNA or PPT primers in vitro, cleavage specificity of RNase H, overview
-
-
?
additional information
?
-
-
3 distinct cleavage modes are described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
additional information
?
-
-
retroviral RNases H display three different modes of cleavage: internal, DNA 3' end-directed, and RNA 5' end-directed
-
-
?
additional information
?
-
retroviral RNases H display three different modes of cleavage: internal, DNA 3' end-directed, and RNA 5' end-directed
-
-
?
additional information
?
-
RNase H activity is determined by measuring the [3H]oligo(rA) released from [3H]poly(rA)*p(dT)45
-
-
?
additional information
?
-
-
RNase H activity is determined by measuring the [3H]oligo(rA) released from [3H]poly(rA)*p(dT)45
-
-
?
additional information
?
-
-
the enzyme is essential for retroviral replication
-
-
?
additional information
?
-
-
the enzyme is essential to complete retroviral replication
-
-
?
additional information
?
-
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, i.e. NRTIs
-
-
?
additional information
?
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, i.e. NRTIs
-
-
?
additional information
?
-
-
3 distinct cleavage modes are described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Mg2+
-
optimum: 2 mM for degradation of poly(A)-poly(dT), optimum: 1-2 mM for degradation of X174-DNA-RNA hybrid
Mg2+
-
coordination of the magnesium ion within the catalytic core comprised of the highly conserved acidic residues D524, E562, and D583
Mg2+
-
four highly conserved acidic amino acids (Asp524, Glu562, Asp583 and Asp653) coordinate the binding of two Mg2+ ions
Mn2+
-
optimum: 2 mM for degradation of poly(A)-poly(dT), optimum: 0.1-1.0 mM for degradation of X174DNA-RNA hybrid
Mn2+
-
optimal RNase H activitiy in the presence of Mn2+ and not Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
non-nucleotide or non-nucleoside reverse transcriptase inhibitor
targets the DNA polymerasec activity of reverse transcriptase. Non-competitive inhibitor that binds a hydrophobic pocket near the polymerase active site of the p66 subunit in HIV-1 reverse transcriptase
-
nucleotide or nucleoside reverse transcriptase inhibitor
targets the DNA polymerasec activity of reverse transcriptase. NRTIs inhibit replication by competing with cellular dNTPs for incorporation into the nascent DNAchain; upon incorporation, the absence of a 3' hydroxyl group on the NRTI prevents additional synthesis and causes premature chain termination
-
3'-azido-3'-deoxythymidine
a nucleoside analog RT inhibitor
4-[(4'-aminomethyl-1,1'-biphenyl)methyl]-1-hydroxy-1,8-naphthyridin-2-one
-
potent inhibitor
non-nucleoside reverse transcriptase inhibitors
i.e. NNRTIs
-
nucleoside analog RT inhibitors
i.e. NRTIs, nucleoside analog RT inhibitors are non-competitive inhibitors
-
additional information
-
one potential class of RNase H inhibitors involves drugs that alter the interactions between the RNase H domain and substrate or that alter the alignment of substrate in the RNase H active site
-
additional information
one potential class of RNase H inhibitors involves drugs that alter the interactions between the RNase H domain and substrate or that alter the alignment of substrate in the RNase H active site
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Km value of Moloney murine leukemia virus reverse transcriptase (RNase H reaction) above 25 microM. Km values for different Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases with poly(rA)*p(dT)45 as a substrate: 0.013 mM for MRT-AF, 0.0070 mM for MRT-AP, 0.0089 mM for MRT-AT, and 0.0043 mM for MRT-AR
-
additional information
additional information
-
Km value of Moloney murine leukemia virus reverse transcriptase (RNase H reaction) above 25 microM. Km values for different Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases with poly(rA)*p(dT)45 as a substrate: 0.013 mM for MRT-AF, 0.0070 mM for MRT-AP, 0.0089 mM for MRT-AT, and 0.0043 mM for MRT-AR
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kcat value of Moloney murine leukemia virus reverse transcriptase (RNase H reaction) above 3 ms-1. The kcat values for different Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases with poly(rA)*p(dT)45 as a substrate: 6.3 1/s for MRT-AF, 3.8 1/s for MRT-AP, 4.6 1/s for MRT-AT, and 2.4 1/s for MRT-AR
-
additional information
additional information
-
kcat value of Moloney murine leukemia virus reverse transcriptase (RNase H reaction) above 3 ms-1. The kcat values for different Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases with poly(rA)*p(dT)45 as a substrate: 6.3 1/s for MRT-AF, 3.8 1/s for MRT-AP, 4.6 1/s for MRT-AT, and 2.4 1/s for MRT-AR
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
specific activity of Moloney murine leukemia virus reverse transcriptase at 37°C is 53000 U/mg RNase H, specific activity of the MRT-D224A mutant = 42000 U/mg RNase H, specific activity of the Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases: MRT-AF = 10000 U/mg RNase H, MRT-AP U/mg = 10000 U/mg RNase H, MRT-AT U/mg = 13000 U/mg RNase H, and MRT-AR U/mg = 11000 U/mg RNase H. One unit (U) is defined as the amount which produces 1 pmol oligo(rA) (the amount is expressed as that of the total nucleotide) of 10%(w/v) TCA-soluble RNA in 20 min
additional information
-
specific activity of Moloney murine leukemia virus reverse transcriptase at 37°C is 53000 U/mg RNase H, specific activity of the MRT-D224A mutant = 42000 U/mg RNase H, specific activity of the Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases: MRT-AF = 10000 U/mg RNase H, MRT-AP U/mg = 10000 U/mg RNase H, MRT-AT U/mg = 13000 U/mg RNase H, and MRT-AR U/mg = 11000 U/mg RNase H. One unit (U) is defined as the amount which produces 1 pmol oligo(rA) (the amount is expressed as that of the total nucleotide) of 10%(w/v) TCA-soluble RNA in 20 min
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
44 - 50
Moloney murine leukemia virus reverse transcriptase shows a curve with the optimal temperature range of around 44-50°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
RNase H activities of Moloney murine leukemia virus reverse transcriptase and the chimeric reverse transcriptases at various temperatures ranging 30-60°C
additional information
-
RNase H activities of Moloney murine leukemia virus reverse transcriptase and the chimeric reverse transcriptases at various temperatures ranging 30-60°C
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
additional information
additional information
single band with a molecular mass of 75 kDa for Moloney murine leukemia virus reverse transcriptase and the mutants MRT-D224A and MRT-D524A, SDS-PAGE. Major single bands with molecular masses in the range of 65-73 kDa, each corresponding to their calculated molecular masses (70203, 71342, 71973 and 66387 Da), respectively, for the Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases (MRT-AF, MRT-AP, MRT-AT, and MRT-AR)
additional information
-
single band with a molecular mass of 75 kDa for Moloney murine leukemia virus reverse transcriptase and the mutants MRT-D224A and MRT-D524A, SDS-PAGE. Major single bands with molecular masses in the range of 65-73 kDa, each corresponding to their calculated molecular masses (70203, 71342, 71973 and 66387 Da), respectively, for the Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases (MRT-AF, MRT-AP, MRT-AT, and MRT-AR)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
-
RNase H domain occupies the C-terminal of the protein
additional information
additional information
-
surface charge mapping of the Mo-MLV structure reveals a high density of basic charges on one side of the enzyme, secondary structure and substrate binding, overview, structure comparisons, overview
additional information
-
viral RNase H domain structure, overview
additional information
viral RNase H domain structure, overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant mutant Mo-MLV RNase H lacking the putative helix C complexed with the DNA/RNA hybrid substrate, DELTAC monomers and dimers, equilibration against a reservoir solution of 30% PEG 4000 and 0.2 M ammonium sulfate, protein solution, containing 7-10 mg/ml, 10 mM HEPES, pH 7.0, 150 mM NaCl, 5 mM DTT, and 0.1 mM EDTA, is mixed with reservoir solution at pH 5.2-6.0, DELTAC monomer crystallization fails to yield single, large crystals, DELTAC monomer crystals are soaked in 15% PEG 4000, 20% PEG 400, 0.1 M ammonium sulfate, 150 mM NaCl, 1% 2-propanol, 1.25% PEG MME 550, 5 mM MES, pH 6.5, and 0.5 mM zinc sulfate for 5 min, X-ray diffractions tructure determination and analysis at 1.6 A resolution, modelling
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D224A
two Moloney murine leukemia virus reverse transcriptase variants (named MRT-D224A and MRT-D524A) as a negative control, in which the catalytically important residue for the reverse transcription activity, Asp224 and that for the RNase H activity, Asp524, are substituted with Ala, respectively
D524A
two Moloney murine leukemia virus reverse transcriptase variants (named MRT-D224A and MRT-D524A) as a negative control, in which the catalytically important residue for the reverse transcription activity, Asp224 and that for the RNase H activity, Asp524, are substituted with Ala, respectively
additional information
additional information
design of four Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases (named MRT-AF, MRT-AP, MRT-AT and MRT-AR)
additional information
-
design of four Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases (named MRT-AF, MRT-AP, MRT-AT and MRT-AR)
additional information
-
construction of a mutant Mo-MLV RNase H lacking the putative helix C, surface mapping and substrate binding determinants, overview
additional information
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, NRTIs, e.g. 3'-azido-3'-deoxythymidine, mutations in the RNase H domain that decrease RNase H activity can increase the resistance of reverse transcriptase to NRTIs, overview
additional information
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, NRTIs, e.g. 3'-azido-3'-deoxythymidine, mutations in the RNase H domain that decrease RNase H activity can increase the resistance of reverse transcriptase to NRTIs, overview
additional information
-
isolated RNase H domain of Moloney murine leukemia virus reverse transcriptase is enzymatically active, but the activity is low and exhibits a greatly relaxed substrate specificity. Primer grip residue Tyr586 in Moloney murine leukemia virus reverse transcriptase appears to be a particularly important substrate contact residue because changes at this site profoundly affect both the RNase H activity and proper substrate recognition
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
all chimeric reverse transcriptases are more thermally stable than Moloney murine leukemia virus reverse transcriptase in the RNase H reaction
additional information
-
all chimeric reverse transcriptases are more thermally stable than Moloney murine leukemia virus reverse transcriptase in the RNase H reaction
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant wild-type and mutant enzymes, containing a Factor Xa cleavage site and a GST-tag, from Escherichia coli strain BL21(DE3) by glutathione affinity chromatograpy and by cleavage through Factor Xa, followed by anion and cation exchang chromatography, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of wild-type and mutant enzymes, containing a Factor Xa cleavage site and a GST-tag, in Escherichia coli strain BL21(DE3)
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
drug development
reverse transcriptase is a primary target for antiretroviral therapy of HIV-1 infected patients. While the vast majority of anti-virals are specific for the polymerase domain, the RNaseH activity of reverse transcriptase represents an excellent target for antiretroviral drugs as well
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Verma, I.M.
Studies on reverse transcriptase of RNA tumor viruses III. Properties of purified Moloney murine leukemia virus DNA polymerase and associated RNase H
J. Virol.
15
843-854
1975
Moloney murine leukemia virus, Moloney murine leukemia virus M-MuLV, More
Grandgenett, D.P.; Gerard, G.F.; Green, M.
Ribonuclease H: a ubiquitous activity in virions of ribonucleic acid tumor viruses
J. Virol.
10
1136-1142
1972
Avian myeloblastosis virus, feline leukemia virus, Harvey murine sarcoma virus, Mason-Pfizer monkey virus, Moloney murine leukemia virus, More, Rauscher leukemia virus, RD-feline leukemia virus, Rous sarcoma virus, Harvey murine sarcoma virus MSV-MLV(H)
Schultz, S.J.; Zhang, M.; Champoux, J.J.
Sequence, distance, and accessibility are determinants of 5'-end-directed cleavages by retroviral RNases H
J. Biol. Chem.
281
1943-1955
2006
Human immunodeficiency virus 1, Moloney murine leukemia virus
Schultz, S.J.; Zhang, M.; Champoux, J.J.
Recognition of internal cleavage sites by retroviral RNases H
J. Mol. Biol.
344
635-652
2004
Human immunodeficiency virus 1, Moloney murine leukemia virus
Lim, D.; Gregorio, G.G.; Bingman, C.; Martinez-Hackert, E.; Hendrickson, W.A.; Goff, S.P.
Crystal structure of the moloney murine leukemia virus RNase H domain
J. Virol.
80
8379-8389
2006
Moloney murine leukemia virus
Schultz, S.J.; Champoux, J.J.
RNase H activity: structure, specificity, and function in reverse transcription
Virus Res.
134
86-103
2008
Moloney murine leukemia virus, Moloney murine leukemia virus (P03355), Human immunodeficiency virus 1 (P03366), Human immunodeficiency virus 1
Champoux, J.J.; Schultz, S.J.
Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription
FEBS J.
276
1506-1516
2009
Moloney murine leukemia virus, Avian sarcoma leukosis virus, Human immunodeficiency virus 1 (P03366)
Yasukawa, K.; Mizuno, M.; Inouye, K.
Characterization of Moloney murine leukaemia virus/avian myeloblastosis virus chimeric reverse transcriptases
J. Biochem.
145
315-324
2009
Avian myeloblastosis virus, Moloney murine leukemia virus (P03355), Moloney murine leukemia virus
Kirby, K.A.; Marchand, B.; Ong, Y.T.; Ndongwe, T.P.; Hachiya, A.; Michailidis, E.; Leslie, M.D.; Sietsema, D.V.; Fetterly, T.L.; Dorst, C.A.; Singh, K.; Wang, Z.; Parniak, M.A.; Sarafianos, S.G.
Structural and inhibition studies of the RNase H function of xenotropic murine leukemia virus-related virus reverse transcriptase
Antimicrob. Agents Chemother.
56
2048-2061
2012
Human immunodeficiency virus 1, Moloney murine leukemia virus, Xenotropic MuLV-related virus (A1Z651), Xenotropic MuLV-related virus
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