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Paper364415

Small-angle X-ray titration of the complex formed between the ribosomal protein S4 and its 16S binding site, S4-RNA: a central core in the 30S subunit.

Osterberg R and 3 others. Nucleic Acids Res, 1978. Cited by 7 papers, by iCite.

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ConductScience Library. Small-angle X-ray titration of the complex formed between the ribosomal protein S4 and its 16S binding site, S4-RNA: a central core in the 30S subunit. Papers, record 364415. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/364415

Paper

PubMed's record of the paper, with iCite's citation figures. No abstract is shown.

Title
Small-angle X-ray titration of the complex formed between the ribosomal protein S4 and its 16S binding site, S4-RNA: a central core in the 30S subunit.
PubMed
Journal
Nucleic Acids Res
PubMed
Year
1978
PubMed
Publication types
Journal Article
PubMed
Citations, by iCite
7
iCite
Relative citation ratio, by iCite
0.21
iCite
Revised in PubMed
2019-05-01
PubMed

Authors4

The authors in the order PubMed's record lists them, with the ORCID iDs it states.

OrderAuthorForenameKindORCID iD
1Osterberg RR
2Sjöberg BB
3Garrett RAR A
4Littlechild JJ

Source PubMed

Topics10

NLM's MeSH indexing of the paper, its major topics first.

MeSH termMajor
RNA, RibosomalMajor topic
Ribosomal ProteinsMajor topic
RibosomesMajor topic
Binding Sites
Escherichia coli
Nucleic Acid Conformation
Protein Binding
Protein Conformation
Scattering, Radiation
X-Rays

Source PubMed

References24

The papers the reference list in PubMed's record names, those in our copy of PubMed, in the list's order.

OrderPMIDTitleJournalYearIn PapersSource
1338,355Proton magnetic resonance studies to compare Escherichia coli ribosomal proteins prepared by two different methods.FEBS Lett1977https://conductscience.org/library/papers/338355PubMed
221,073Physical studies on the conformation of ribosomal protein S4 from Escherichia coli.Eur J Biochem1977https://conductscience.org/library/papers/21073PubMed
3334,548Small-angle X-ray titration study on the complex formation between 5-S RNA and the L18 protein of the Escherichia coli 50-S ribosome particle.Eur J Biochem1977https://conductscience.org/library/papers/334548PubMed
4330,240Small-angle x-ray scattering study of S4-RNA, the 16 S RNA binding site for the protein S4 from Escherichia coli ribosomes.FEBS Lett1977https://conductscience.org/library/papers/330240PubMed
5332,520A topographical study of the 5'-region of 16 S rna of Escherichia coli in the presence and absence of protein S4.FEBS Lett1977https://conductscience.org/library/papers/332520PubMed
6328,283A trypsin-resistant fragment from complexes of ribosomal protein S4 with 16-S RNA of Escherichia coli and from the uncomplexed protein.Eur J Biochem1977https://conductscience.org/library/papers/328283PubMed
7320,037Small-angle x-ray scattering study of the 16S RNA binding protein S4 from Escherichia coli ribosomes.FEBS Lett1977https://conductscience.org/library/papers/320037PubMed
8796,464The function of the N-terminal region of ribosomal protein S4.J Mol Biol1976https://conductscience.org/library/papers/796464PubMed
94,587,210The primary structure of ribosomal protein S4 from Escherichia coli.FEBS Lett1973https://conductscience.org/library/papers/4587210PubMed
102,784The determination of stability constants from small-angle x-ray scattering data and the analysis of pH-dependent macromolecular equilibria.J Mol Biol1975https://conductscience.org/library/papers/2784PubMed
114,607,041RNA-protein interactions in the ribosome. II. Binding of ribosomal proteins to isolated fragments of the 16 S RNA.J Mol Biol1974https://conductscience.org/library/papers/4607041PubMed
124,607,040RNA-protein interactions in the ribosome. I. Characterization and ribonuclease digestion of 16 S RNA-ribosomal protein complexes.J Mol Biol1974https://conductscience.org/library/papers/4607040PubMed
134,552,713Molecular interactions of ribosomal components. 3. Isolation of the RNA binding site for a ribosomal protein.Mol Gen Genet1972https://conductscience.org/library/papers/4552713PubMed
144,944,319The structure and coding specificity of a lysine transfer ribonucleic acid from the haploid yeast Saccharomyces cerevisiae alpha S288C.J Biol Chem1971https://conductscience.org/library/papers/4944319PubMed
154,912,319Assembly mapping of 30S ribosomal proteins from E. coli.Nature1970https://conductscience.org/library/papers/4912319PubMed
164,904,865Small angle x-ray scattering of a homogeneous gamm G-1 immunoglobulin.Biochemistry1970https://conductscience.org/library/papers/4904865PubMed
171,092,684Characterization of fragments of 16 S ribonucleic acid protected against pancreatic ribonuclease digestion by ribosomal protein S4.J Biol Chem1975https://conductscience.org/library/papers/1092684PubMed
181,091,919Location and characteristics of ribosomal protein binding sites in the 16S RNA of Escherichia coli.Nucleic Acids Res1975https://conductscience.org/library/papers/1091919PubMed
191,091,486An investigation of the 16-S RNA binding sites of ribosomal proteins S4, S8, S15, and S20 FROM Escherichia coli.Eur J Biochem1975https://conductscience.org/library/papers/1091486PubMed
201,107,026Small-angle x-ray studies on the structure of 16-S ribosomal RNA and of a complex of ribosomal protein S4 and 16-S ribosomal RNA from Escherichia coli.Eur J Biochem1975https://conductscience.org/library/papers/1107026PubMed

See all 24 references

Cited by1

The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 7 citations.

PMIDTitleJournalYearIn Papers
6,162,161The conformation of a large RNA fragment from the E.coli ribosomal 16S-RNA. An X-ray and neutron small-angle scattering study.Nucleic Acids Res1980https://conductscience.org/library/papers/6162161

Source PubMed

Data dates

The date of each source this release read.

PubMed
2026-11-06
PubMed
iCite
2026-11-05
iCite
PMC's ID file
2026-11-05
PMC's ID file
NIH RePORTER's grant and paper links
2026-11-01
NIH RePORTER's grant and paper links
Trials
2026-11-12
Gene search
2026-11-11
Pipelines
2026-09-18

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  • NCBI GenePublic domain (US government)
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  • 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

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