Paper · 8970988
RNase H domain of Moloney murine leukemia virus reverse transcriptase retains activity but requires the polymerase domain for specificity.
Schultz SJ and 1 other. J Virol, 1996. Cited by 27 papers, by iCite.
11 sourcespapers-2026-11-12-0.1.0
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ConductScience Library. RNase H domain of Moloney murine leukemia virus reverse transcriptase retains activity but requires the polymerase domain for specificity. Papers, record 8970988. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/8970988
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Paper
PubMed's record of the paper, with iCite's citation figures. No abstract is shown.
- Title
- RNase H domain of Moloney murine leukemia virus reverse transcriptase retains activity but requires the polymerase domain for specificity.
- PubMed
Topics8
NLM's MeSH indexing of the paper, its major topics first.
| MeSH term | Major |
|---|---|
| DNA-Directed DNA Polymerase | Major topic |
| Moloney murine leukemia virus | Major topic |
| RNA-Directed DNA Polymerase | Major topic |
| Retroviridae Proteins | Major topic |
| Ribonuclease H | Major topic |
| Glutathione Transferase | |
| RNA | |
| RNA, Transfer |
Source PubMed
Grants1
Each grant PubMed's record writes, matched to the NIH project NIH's grant and paper links name for this paper, and each of those links the record does not write.
| Grant, as the record writes it | Agency | Country | NIH project | Stated by |
|---|---|---|---|---|
| R37 CA51605 | NCI NIH HHS | United States | R37CA051605 | PubMed and NIH |
Source NIH RePORTER
Trials0
The trials whose ClinicalTrials.gov record lists the paper, and the trial numbers the paper's PubMed record names.
None in this release.
Comments and corrections0
PubMed's comments and corrections, NLM's own indexing: retractions first, then expressions of concern, errata and updates, and comments last.
None in this release.
References47
The papers the reference list in PubMed's record names, those in our copy of PubMed, in the list's order.
| Order | PMID | Title | Journal | Year | In Papers | Source |
|---|---|---|---|---|---|---|
| 1 | 2,477,553 | Plus-strand priming by Moloney murine leukemia virus. The sequence features important for cleavage by RNase H. | J Mol Biol | 1989 | https://conductscience.org/library/papers/2477553 | PubMed |
| 2 | 2,466,838 | Human immunodeficiency virus 1 reverse transcriptase. Template binding, processivity, strand displacement synthesis, and template switching. | J Biol Chem | 1989 | https://conductscience.org/library/papers/2466838 | PubMed |
| 3 | 1,688,626 | Specificities involved in the initiation of retroviral plus-strand DNA. | J Virol | 1990 | https://conductscience.org/library/papers/1688626 | PubMed |
| 4 | 1,691,093 | HIV-1 RT-associated ribonuclease H displays both endonuclease and 3'----5' exonuclease activity. | EMBO J | 1990 | https://conductscience.org/library/papers/1691093 | PubMed |
| 5 | 1,691,564 | Mutational analysis of the ribonuclease H activity of human immunodeficiency virus 1 reverse transcriptase. | Virology | 1990 | https://conductscience.org/library/papers/1691564 | PubMed |
| 6 | 1,693,920 | Processing of the primer for plus strand DNA synthesis by human immunodeficiency virus 1 reverse transcriptase. | J Biol Chem | 1990 | https://conductscience.org/library/papers/1693920 | PubMed |
| 7 | 2,169,648 | Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein. | Science | 1990 | https://conductscience.org/library/papers/2169648 | PubMed |
| 8 | 2,173,791 | Plus-strand origin for human immunodeficiency virus type 1: implications for integration. | J Virol | 1990 | https://conductscience.org/library/papers/2173791 | PubMed |
| 9 | 1,713,059 | Human immunodeficiency virus reverse transcriptase ribonuclease H: specificity of tRNA(Lys3)-primer excision. | Biochemistry | 1991 | https://conductscience.org/library/papers/1713059 | PubMed |
| 10 | 1,718,968 | A recombinant ribonuclease H domain of HIV-1 reverse transcriptase that is enzymatically active. | J Biol Chem | 1991 | https://conductscience.org/library/papers/1718968 | PubMed |
1 to 10 of 47
See all 47 referencesCited by16
The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 27 citations.
| PMID | Title | Journal | Year | In Papers | Source |
|---|---|---|---|---|---|
| 31,269,675 | Structural and Functional Aspects of Foamy Virus Protease-Reverse Transcriptase. | Viruses | 2019 | https://conductscience.org/library/papers/31269675 | PubMed |
| 24,880,687 | 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 | 2014 | https://conductscience.org/library/papers/24880687 | PubMed |
| 23,382,176 | Structural analysis of monomeric retroviral reverse transcriptase in complex with an RNA/DNA hybrid. | Nucleic Acids Res | 2013 | https://conductscience.org/library/papers/23382176 | PubMed |
| 22,962,864 | The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding. | Retrovirology | 2012 | https://conductscience.org/library/papers/22962864 | PubMed |
| 22,366,278 | Crystal structures of the reverse transcriptase-associated ribonuclease H domain of xenotropic murine leukemia-virus related virus. | J Struct Biol | 2012 | https://conductscience.org/library/papers/22366278 | PubMed |
| 22,325,739 | Insights into the structure and activity of prototype foamy virus RNase H. | Retrovirology | 2012 | https://conductscience.org/library/papers/22325739 | PubMed |
| 20,358,252 | Retroviral reverse transcriptases. | Cell Mol Life Sci | 2010 | https://conductscience.org/library/papers/20358252 | PubMed |
| 20,122,939 | Multiple nucleotide preferences determine cleavage-site recognition by the HIV-1 and M-MuLV RNases H. | J Mol Biol | 2010 | https://conductscience.org/library/papers/20122939 | PubMed |
| 19,228,195 | Ribonuclease H: properties, substrate specificity and roles in retroviral reverse transcription. | FEBS J | 2009 | https://conductscience.org/library/papers/19228195 | PubMed |
| 18,261,820 | RNase H activity: structure, specificity, and function in reverse transcription. | Virus Res | 2008 | https://conductscience.org/library/papers/18261820 | PubMed |
1 to 10 of 16
See all 16 cited byGenes0
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None in this release.
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None in this release.
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Data dates
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- Trials
- 2026-11-12
- Gene search
- 2026-11-11
- Pipelines
- 2026-09-18
Sources 11
- ChEMBL, through Open TargetsCC BY-SA 3.0
- ClinicalTrials.govNo license stated
- HGNCCC0
- iCiteCC BY 4.0
- NCBI GenePublic domain (US government)
- NIH RePORTER's grant and paper linksPublic domain
- Open TargetsCC0 1.0
- PMC's ID filePublic domain (US government)
- PubMedNLM's terms
- PubTator 3Public domain
- UniProtCC BY 4.0
Each source's terms
- ChEMBL, through Open TargetsCC BY-SA 3.0, for the parts from ChEMBL. Read on 8 Nov 2026 at https://platform-docs.opentargets.org/licence
- ClinicalTrials.govnone stated
- HGNCCC0: https://www.genenames.org/about/license/
- iCiteCC BY 4.0
- NCBI GeneNone named for the file. NCBI says information created by or for the US government on its site is in the public domain, and asks that NLM be acknowledged: https://www.ncbi.nlm.nih.gov/home/about/policies/
- NIH RePORTER's grant and paper linksPublic domain (NIH RePORTER)
- Open TargetsCC0 1.0. Open Targets asks that users cite its latest paper: Buniello et al. 2025, Open Targets Platform: facilitating therapeutic hypotheses building in drug discovery, Nucleic Acids Research 53(D1):D1467, PMID 39657122. Read on 8 Nov 2026 at https://platform-docs.opentargets.org/licence
- PMC's ID fileNone named for the file. NCBI says information created by or for the US government on its site is in the public domain, and asks that NLM be acknowledged: https://www.ncbi.nlm.nih.gov/home/about/policies/
- PubMedNLM's terms
- PubTator 3Public domain
- UniProtCC BY 4.0. UniProt's licence file: "All databases and documents in the UniProt FTP directory may be copied and redistributed freely, without advance permission, provided that this copyright statement is reproduced with each copy." UniProt asks that users cite its latest paper: The UniProt Consortium, UniProt: the Universal Protein Knowledgebase in 2025, Nucleic Acids Research 53:D609-D617, https://doi.org/10.1093/nar/gkae1010. Read on 9 Nov 2026 at https://www.uniprot.org/help/license
ClinicalTrials.gov's data carry an international copyright outside the United States: https://clinicaltrials.gov/about-site/terms-conditions.
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