Protein‐protein interaction via PAS domains: role of the PAS domain in positive and negative regulation of the bHLH/PAS dioxin receptor‐Arnt transcription factor complex.
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Summary
The PAS domains of the dioxin receptor and Arnt are therefore novel dimerizing regions critical in formation of a functional doxin receptor‐Arnt complex, while the PerPAS domain is a potential negative regulator of bHLH/PAS factor function.
- Type
- article
- Published
- 1995-07-01
- Cited by
- 208
- References
- 1
- Access
- Open access
- OpenAlex
- https://openalex.org/W1876406296
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:31629121
Keywords
Aryl hydrocarbon receptor nuclear translocator, Biology, PAS domain, Transcription factor, Genetics
References
Cited by
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- A point mutation responsible for defective function of the aryl-hydrocarbon-receptor nuclear translocator in mutant Hepa-1c1c7 cells.
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- Differential Usage of Nuclear Export Sequences Regulates Intracellular Localization of the Dioxin (Aryl Hydrocarbon) Receptor*
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- CHARACTERIZATION OF A PUTATIVE TRANSCRIPTION FACTOR
- Role of the PAS2 domain of the NifL regulatory protein in redox signal transduction
- Expression, transkriptionelle Regulation und biologische Funktion des humanen Arylhydrokarbon Rezeptor Repressors
- Mechanisitic studies of the toxicities of the aryl hydrocarbon receptor agonist PCB126
- Induction of cytochrome P4501A1: a model for analyzing mammalian gene transcription
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- Steroid/nuclear receptor coactivators.
- Dynamic Regulation of Aryl Hydrocarbon Receptor Function and Activity by Different Stimuli
- Structure-function analysis of phototropin receptor kinases
- Assessment of HIF-1alpha function and identification of a novel degradation mechanism
- The Role of the Retinoblastoma Protein on Hypoxia-Inducible Factor Dependent Tumor Cell Transformation: Microarray Validation
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