Paper795654
The binding site of protein L1 on 23-S ribosomal RNA from Escherichia coli. 3. Nucleotide sequence.
Branlant C and 2 others. Eur J Biochem, 1976. Cited by 33 papers, by iCite.
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ConductScience Library. The binding site of protein L1 on 23-S ribosomal RNA from Escherichia coli. 3. Nucleotide sequence. Papers, record 795654. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/795654
Paper
PubMed's record of the paper, with iCite's citation figures. No abstract is shown.
- Title
- The binding site of protein L1 on 23-S ribosomal RNA from Escherichia coli. 3. Nucleotide sequence.
- PubMed
Topics13
NLM's MeSH indexing of the paper, its major topics first.
| MeSH term | Major |
|---|---|
| Escherichia coli | Major topic |
| RNA, Ribosomal | Major topic |
| Ribosomal Proteins | Major topic |
| Base Sequence | |
| Binding Sites | |
| Hydrogen Bonding | |
| Molecular Weight | |
| Nucleic Acid Conformation | |
| Oligoribonucleotides | |
| Pancreas | |
| Protein Binding | |
| Ribonucleases | |
| Ribosomes |
Source PubMed
Cited by8
The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 33 citations.
| PMID | Title | Journal | Year | In Papers | Source |
|---|---|---|---|---|---|
| 8,628,253 | Sequence and characterisation of a ribosomal RNA operon from Agrobacterium vitis. | Mol Gen Genet | 1996 | https://conductscience.org/library/papers/8628253 | PubMed |
| 7,010,313 | The secondary structure of the protein L1 binding region of ribosomal 23S RNA. Homologies with putative secondary structures of the L11 mRNA and of a region of mitochondrial 16S rRNA. | Nucleic Acids Res | 1981 | https://conductscience.org/library/papers/7010313 | PubMed |
| 6,265,904 | Specific binding of a prokaryotic ribosomal protein to a eukaryotic ribosomal RNA: implications for evolution and autoregulation. | Proc Natl Acad Sci U S A | 1981 | https://conductscience.org/library/papers/6265904 | PubMed |
| 6,162,152 | Characterization of the Escherichia coli 23S Ribosomal RNA region associated with ribosomal protein L1. Evidence for homologies with the 5'-end region of the L11 operon. | Nucleic Acids Res | 1980 | https://conductscience.org/library/papers/6162152 | PubMed |
| 2,107,529 | Structure, organization and evolution of the L1 equivalent ribosomal protein gene of the archaebacterium Methanococcus vannielii. | Nucleic Acids Res | 1990 | https://conductscience.org/library/papers/2107529 | PubMed |
| 1,702,198 | Localization of a series of RNA-protein cross-link sites in the 23S and 5S ribosomal RNA from Escherichia coli, induced by treatment of 50S subunits with three different bifunctional reagents. | Nucleic Acids Res | 1990 | https://conductscience.org/library/papers/1702198 | PubMed |
| 1,614,849 | How are tRNAs and mRNA arranged in the ribosome? An attempt to correlate the stereochemistry of the tRNA-mRNA interaction with constraints imposed by the ribosomal topography. | Nucleic Acids Res | 1992 | https://conductscience.org/library/papers/1614849 | PubMed |
| 364,413 | RNA-RNA interactions in the binding site of protein L24 on 23S ribosomal RNA of Escherichia coli: 1. Evidence for their occurrence between widely separated sequence regions. | Nucleic Acids Res | 1978 | https://conductscience.org/library/papers/364413 | PubMed |
Data1
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| Data bank | Accession |
|---|---|
| GENBANK | K01128 |
Source GENBANK
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- 2026-11-12
- Gene search
- 2026-11-11
- Pipelines
- 2026-09-18
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- 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
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- 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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