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The Journal of Biological Chemistry|August 26, 1998
A direct interaction between the aryl hydrocarbon receptor and retinoblastoma protein. Linking dioxin signaling to the cell cycleN L Ge, C J ElferinkReceptor|January 1, 1994
Dioxin-dependent, DNA sequence-specific binding of a multiprotein complex containing the Ah receptorC J Elferink, J P WhitlockThe Journal of Biological Chemistry|April 5, 1990
2,3,7,8-Tetrachlorodibenzo-p-dioxin-inducible, Ah receptor-mediated bending of enhancer DNAC J Elferink, J P WhitlockBiotechniques|March 1, 1996
Quantitative RT-PCR on CYP1A1 heterogeneous nuclear RNA: a surrogate for the in vitro transcription run-on assayC J Elferink, J J ReinersThe Journal of Biological Chemistry|September 15, 1988
Regulation of 5-aminolevulinate synthase in mouse erythroleukemic cells is different from that in liverC J Elferink, S Sassa, B K MayMolecular Pharmacology|March 22, 2001
Maximal aryl hydrocarbon receptor activity depends on an interaction with the retinoblastoma proteinC J Elferink, N L Ge, A LevineBiochemistry|March 19, 1991
Characterization of multiple forms of the Ah receptor: recognition of a dioxin-responsive enhancer involves heteromer formationT A Gasiewicz, C J Elferink, E C HenryThe Journal of Biological Chemistry|November 25, 1990
Protein-DNA interactions at a dioxin-responsive enhancer. Evidence that the transformed Ah receptor is heteromericC J Elferink, T A Gasiewicz, J P WhitlockToxicology Research|January 20, 2016
Ah Receptor Pathway Intricacies; Signaling Through Diverse Protein Partners and DNA-MotifsD P Jackson, A D Joshi, C J ElferinkThe Journal of Biological Chemistry|March 25, 1987
A unique gene for 5-aminolevulinate synthase in chickens. Evidence for expression of an identical messenger RNA in hepatic and erythroid tissuesC J Elferink, G Srivastava, D J Maguire, et al.Pageof 2