Paper · 4577136
Isolation of the self-regulated repressor protein of the Hut operons of Salmonella typhimurium.
Hagen DC and 1 other. Proc Natl Acad Sci U S A, 1973. Cited by 25 papers, by iCite.
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ConductScience Library. Isolation of the self-regulated repressor protein of the Hut operons of Salmonella typhimurium. Papers, record 4577136. Release papers-2026-11-12-0.1.0, 12 Nov 2026. https://conductscience.org/library/papers/4577136
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Paper
PubMed's record of the paper, with iCite's citation figures. No abstract is shown.
- Title
- Isolation of the self-regulated repressor protein of the Hut operons of Salmonella typhimurium.
- PubMed
Topics17
NLM's MeSH indexing of the paper, its major topics first.
| MeSH term | Major |
|---|---|
| Bacterial Proteins | Major topic |
| Genes, Regulator | Major topic |
| Operon | Major topic |
| Salmonella typhimurium | Major topic |
| Acrylates | |
| Amidohydrolases | |
| Ammonia-Lyases | |
| DNA, Viral | |
| Enzyme Induction | |
| Genes | |
| Genotype | |
| Histidine | |
| Imidazoles | |
| Mutation | |
| Phosphorus Isotopes | |
| Protein Binding | |
| Transduction, Genetic |
Source PubMed
Grants0
Each grant PubMed's record writes, matched to the NIH project NIH's grant and paper links name for this paper, and each of those links the record does not write.
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.
References10
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 | 4,875,714 | DNA repair. | Annu Rev Biochem | 1968 | https://conductscience.org/library/papers/4875714 | PubMed |
| 2 | 4,899,017 | Genetic control of histidine degradation in Salmonella typhimurium, strain LT-2. | J Biol Chem | 1969 | https://conductscience.org/library/papers/4899017 | PubMed |
| 3 | 4,899,018 | Genetic and metabolic control of histidase and urocanase in Salmonella typhimurium, strain 15-59. | J Biol Chem | 1969 | https://conductscience.org/library/papers/4899018 | PubMed |
| 4 | 5,422,623 | Active form of two coliphage repressors. | Nature | 1970 | https://conductscience.org/library/papers/5422623 | PubMed |
| 5 | 4,915,295 | Lac repressor-operator interaction. I. Equilibrium studies. | J Mol Biol | 1970 | https://conductscience.org/library/papers/4915295 | PubMed |
| 7 | 4,930,060 | The two operons of the histidine utilization system in Salmonella typhimurium. | J Biol Chem | 1971 | https://conductscience.org/library/papers/4930060 | PubMed |
| 8 | 4,934,521 | Nature and self-regulated synthesis of the repressor of the hut operons in Salmonella typhimurium. | Proc Natl Acad Sci U S A | 1971 | https://conductscience.org/library/papers/4934521 | PubMed |
| 9 | 4,938,552 | DNA binding of the lac repressor. | J Mol Biol | 1968 | https://conductscience.org/library/papers/4938552 | PubMed |
| 10 | 4,939,450 | Specialized transduction of the Salmonella hut operons by coliphage lambda: deletion analysis of the hut operons employing lambda-phut. | Virology | 1971 | https://conductscience.org/library/papers/4939450 | PubMed |
| 11 | 4,930,059 | Genetic and metabolic control of enzymes responsible for histidine degradation in Salmonella typhimurium. 4-imidazolone-5-propionate amidohydrolase and N-formimino-L-glutamate formiminohydrolase. | J Biol Chem | 1971 | https://conductscience.org/library/papers/4930059 | PubMed |
Cited by10
The papers in our copy of PubMed whose reference list names this one, newest first. iCite, which reads more sources, counts 25 citations.
| PMID | Title | Journal | Year | In Papers | Source |
|---|---|---|---|---|---|
| 32,291,279 | Global Regulatory Roles of the Histidine-Responsive Transcriptional Repressor HutC in Pseudomonas fluorescens SBW25. | J Bacteriol | 2020 | https://conductscience.org/library/papers/32291279 | PubMed |
| 28,352,553 | Effect of amino acids on the repression of alkaline protease synthesis in haloalkaliphilic Nocardiopsis dassonvillei. | Biotechnol Rep (Amst) | 2016 | https://conductscience.org/library/papers/28352553 | PubMed |
| 2,858,467 | Cloning and expression in Escherichia coli of histidine utilization genes from Pseudomonas putida. | J Bacteriol | 1985 | https://conductscience.org/library/papers/2858467 | PubMed |
| 790,386 | lac repressor: 3-fluorotyrosine substitution for nuclear magnetic resonance studies. | Proc Natl Acad Sci U S A | 1976 | https://conductscience.org/library/papers/790386 | PubMed |
| 353,483 | Linkage map of Salmonella typhimurium, edition V. | Microbiol Rev | 1978 | https://conductscience.org/library/papers/353483 | PubMed |
| 238,937 | Gene order of the histidine utilization (hut) operons in Klebsiella aerogenes. | J Bacteriol | 1975 | https://conductscience.org/library/papers/238937 | PubMed |
| 234,417 | Isolation of super-repressor mutants in the histidine utilization system of Salmonella typhimurium. | J Bacteriol | 1975 | https://conductscience.org/library/papers/234417 | PubMed |
| 16,868 | Regulation of enzyme synthesis by the glutamine synthetase of Salmonella typhimurium: a factor in addition to glutamine synthetase is required for activation of enzyme formation. | J Bacteriol | 1977 | https://conductscience.org/library/papers/16868 | PubMed |
| 8,423 | Deoxyribonucleic acid-binding studies on the hut repressor and mutant forms of the hut repressor of Salmonella typhimurium. | J Bacteriol | 1976 | https://conductscience.org/library/papers/8423 | PubMed |
| 362 | Expression of the hut operons of Salmonella typhimurium in Klebsiella aerogenes and in Escherichia coli. | J Bacteriol | 1975 | https://conductscience.org/library/papers/362 | PubMed |
Genes0
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None in this release.
Drugs0
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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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