Paper2784
The determination of stability constants from small-angle x-ray scattering data and the analysis of pH-dependent macromolecular equilibria.
Osterberg R. J Mol Biol, 1975. Cited by 8 papers, by iCite.
11 sourcespapers-2026-11-12-0.1.0
Cite this record
ConductScience Library. The determination of stability constants from small-angle x-ray scattering data and the analysis of pH-dependent macromolecular equilibria. Papers, record 2784. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/2784
Paper
PubMed's record of the paper, with iCite's citation figures. No abstract is shown.
- Title
- The determination of stability constants from small-angle x-ray scattering data and the analysis of pH-dependent macromolecular equilibria.
- PubMed
Topics13
NLM's MeSH indexing of the paper, its major topics first.
| MeSH term | Major |
|---|---|
| Amino Acyl-tRNA Synthetases | Major topic |
| Lysine-tRNA Ligase | Major topic |
| Binding Sites | |
| Hydrogen-Ion Concentration | |
| Kinetics | |
| Macromolecular Substances | |
| Mathematics | |
| Nucleic Acid Conformation | |
| Protein Binding | |
| Protein Conformation | |
| RNA, Transfer | |
| Saccharomyces cerevisiae | |
| X-Ray Diffraction |
Source PubMed
Cited by2
The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 8 citations.
| PMID | Title | Journal | Year | In Papers | Source |
|---|---|---|---|---|---|
| 364,415 | 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. | Nucleic Acids Res | 1978 | https://conductscience.org/library/papers/364415 | PubMed |
| 333,390 | A neutron investigation of yeast valyl-tRNA synthetase interaction with tRNAs. | Nucleic Acids Res | 1977 | https://conductscience.org/library/papers/333390 | PubMed |
Data dates
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- 2026-11-12
- Gene search
- 2026-11-11
- Pipelines
- 2026-09-18
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- Drugs
- Data
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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