Paper · 376399
Functional interactions beween the DNA ligase of Escherichia coli and components of the DNA metabolic apparatus of T4 bacteriophage.
Karam JD and 2 others. Genetics, 1979. Cited by 6 papers, by iCite.
11 sourcespapers-2026-11-12-0.1.0
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ConductScience Library. Functional interactions beween the DNA ligase of Escherichia coli and components of the DNA metabolic apparatus of T4 bacteriophage. Papers, record 376399. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/376399
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Paper
PubMed's record of the paper, with iCite's citation figures. No abstract is shown.
- Title
- Functional interactions beween the DNA ligase of Escherichia coli and components of the DNA metabolic apparatus of T4 bacteriophage.
- PubMed
Topics9
NLM's MeSH indexing of the paper, its major topics first.
| MeSH term | Major |
|---|---|
| Coliphages | Major topic |
| DNA Ligases | Major topic |
| DNA, Viral | Major topic |
| Escherichia coli | Major topic |
| Mutation | Major topic |
| Polynucleotide Ligases | Major topic |
| DNA Repair | |
| DNA Replication | |
| Phenotype |
Source PubMed
Grants0
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None in this release.
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.
References18
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 | 885,343 | Multiple interactions of a DNA-binding protein in vivo. III. Phage T4 gene-32 mutations differentially affect insertion-type recombination and membrane properties. | Genetics | 1977 | https://conductscience.org/library/papers/885343 | PubMed |
| 2 | 791,948 | Translational, autogenous regulation of gene 32 expression during bacteriophage T4 infection. | J Biol Chem | 1976 | https://conductscience.org/library/papers/791948 | PubMed |
| 3 | 4,995,816 | Enzymatic characterization of a mutant of Escherichia coli with an altered DNA ligase. | Proc Natl Acad Sci U S A | 1971 | https://conductscience.org/library/papers/4995816 | PubMed |
| 4 | 4,377,758 | DNA ligase: structure, mechanism, and function. | Science | 1974 | https://conductscience.org/library/papers/4377758 | PubMed |
| 5 | 4,351,461 | Suppression of amber mutations of bacteriophage T4 gene 43 (DNA polymerase) by translational ambiguity. | J Virol | 1973 | https://conductscience.org/library/papers/4351461 | PubMed |
| 6 | 1,165,600 | Analysis of expression of the rII gene function of bacteriophage T4. | J Virol | 1975 | https://conductscience.org/library/papers/1165600 | PubMed |
| 7 | 4,588,574 | An electron microscopic analysis of pathways for bacteriophage T4 DNA recombination. | J Mol Biol | 1973 | https://conductscience.org/library/papers/4588574 | PubMed |
| 8 | 4,589,857 | Mutation to overproduction of bacteriophage T4 gene products. | J Virol | 1974 | https://conductscience.org/library/papers/4589857 | PubMed |
| 9 | 4,591,048 | Requirement of a functional gene 32 product of bacteriophage T4 in UV, repair. | J Virol | 1973 | https://conductscience.org/library/papers/4591048 | PubMed |
| 10 | 4,563,042 | A mutation of T4B phage, which enhances suppression of ligase mutants with rII mutations. | Virology | 1972 | https://conductscience.org/library/papers/4563042 | PubMed |
1 to 10 of 18
See all 18 referencesCited by1
The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 6 citations.
| PMID | Title | Journal | Year | In Papers |
|---|---|---|---|---|
| 15,507,125 | Divergence of the mRNA targets for the Ssb proteins of bacteriophages T4 and RB69. | Virol J | 2004 | https://conductscience.org/library/papers/15507125 |
Source PubMed
Genes0
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None in this release.
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None in this release.
Data0
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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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