Paper · 16900
Repressible alkaline phosphatase from Thermus aquaticus: associated phosphodiesterase activity.
Smile DH and 4 others. J Biol Chem, 1977. Cited by 10 papers, by iCite.
11 sourcespapers-2026-11-12-0.1.0
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ConductScience Library. Repressible alkaline phosphatase from Thermus aquaticus: associated phosphodiesterase activity. Papers, record 16900. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/16900
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Paper
PubMed's record of the paper, with iCite's citation figures. No abstract is shown.
- Title
- Repressible alkaline phosphatase from Thermus aquaticus: associated phosphodiesterase activity.
- PubMed
Topics12
NLM's MeSH indexing of the paper, its major topics first.
| MeSH term | Major |
|---|---|
| Alkaline Phosphatase | Major topic |
| Gram-Negative Aerobic Bacteria | Major topic |
| Phosphoric Diester Hydrolases | Major topic |
| Adenine Nucleotides | |
| Electrophoresis, Disc | |
| Enzyme Repression | |
| Glucosephosphates | |
| Hydrogen-Ion Concentration | |
| Isoelectric Point | |
| Phosphates | |
| Phosphodiesterase Inhibitors | |
| Temperature |
Source PubMed
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References0
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Cited by6
The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 10 citations.
| PMID | Title | Journal | Year | In Papers | Source |
|---|---|---|---|---|---|
| 23,100,645 | Differential expression of thermophilic phosphatases in the wild type and auxotrophic mutant strains of Thermoactinomyces vulgaris. | Indian J Microbiol | 2007 | https://conductscience.org/library/papers/23100645 | PubMed |
| 19,156,357 | Thermus thermophilus as biological model. | Extremophiles | 2009 | https://conductscience.org/library/papers/19156357 | PubMed |
| 17,657,541 | Mg2+ decreases arrhenius energies of activation for high temperature catalysis of phosphatases in Thermoactinomyces vulgaris. | Curr Microbiol | 2007 | https://conductscience.org/library/papers/17657541 | PubMed |
| 6,258,569 | Phosphate utilization and constitutive synthesis of phosphatases in Thermoactinomyces vulgaris Tsilinsky. | Biochem J | 1980 | https://conductscience.org/library/papers/6258569 | PubMed |
| 3,020,000 | Purification and characterization of an inorganic pyrophosphatase from the extreme thermophile Thermus aquaticus. | J Bacteriol | 1986 | https://conductscience.org/library/papers/3020000 | PubMed |
| 500,561 | Protein turnover in the extreme thermophile Thermus aquaticus. | J Bacteriol | 1979 | https://conductscience.org/library/papers/500561 | PubMed |
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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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