Dallam, R. A., Lubawy, W. C., & Hurley, L. H. (1979). Pyrrolo(1,4)benzodiazepine antitumor antibiotics. Combined protective therapy with co-enzyme Q10 or vitamin E and the antitumor antibiotic anthramycin. Journal of Natural Products, 42(6), 693-.
Grand, C. L., Powell, T. J., Nagle, R. B., Bearss, D. J., Tye, D., Gleason-Guzman, M., & Hurley, L. H. (2005). Erratum (Retracted Article): Mutations in the G-quadruplex silencer element and their relationship to c-MYC overexpression, NM23 repression, and therapeutic rescue (Proceedings of the National Academy of Sciences of the United States of America (April 20, 2004) 101:16 (6140-6145)). Proceedings of the National Academy of Sciences of the United States of America, 102(2), 516-.
Gonzalez, V., & Hurley, L. H. (2010). The c-MYC NHE III1: Function and regulation. Annual Review of Pharmacology and Toxicology, 50, 111-129.
PMID: 19922264;Abstract:
c-MYC is an important regulator of a wide array of cellular processes necessary for normal cell growth and differentiation, and its dysregulation is one of the hallmarks of many cancers. Consequently, understanding c-MYC transcriptional activation is critical for understanding developmental and cancer biology, as well as for the development of new anticancer drugs. The nuclease hypersensitive element (NHE) III1 region of the c-MYC promoter has been shown to be particularly important in regulating c-MYC expression. Specifically, the formation of a G-quadruplex structure appears to promote repression of c-MYC transcription. This review focuses on what is known about the formation of a G-quadruplex in the NHE III1 region of the c-MYC promoter, as well as on those factors that are known to modulate its formation. Last, we discuss the development of small molecules that stabilize or induce the formation of G-quadruplex structures and could potentially be used as anticancer agents. Copyright © 2010 by Annual Reviews. All rights reserved.
Warpehoski, M. A., & Hurley, L. H. (1988). Sequence selectivity of DNA covalent modification. Chemical Research in Toxicology, 1(6), 315-333.
Sun, D., Lopez-Guajardo, C. C., Quada, J., Hurley, L. H., & D., D. (1999). Regulation of catalytic activity and processivity of human telomerase. Biochemistry, 38(13), 4037-4044.
PMID: 10194316;Abstract:
The ends of eukaryotic chromosomes are specialized sequences, called telomeres comprising tandem repeats of simple DNA sequences. Those sequences are essential for preventing aberrant recombination and protecting genomic DNA against exonucleolytic DNA degradation. Telomeres are maintained at a stable length by telomerase, an RNA-dependent DNA polymerase. Recently, human telomerase has been recognized as a unique diagnostic marker for human tumors and is potentially a highly selective target for antitumor drugs. In this study, we have examined the major factors affecting the catalytic activity and processivity of human telomerase. Specifically, both the catalytic activity and processivity of human telomerase were modulated by temperature, substrate (dNTP and primer) concentration, and the concentration of K+. The catalytic activity of telomerase increased as temperature (up to 37°C), concentrations of dGTP, primer, and K+ were increased. However, the processivity of human telomerase decreased as temperature, primer concentration, and K+ were increased. Our results support the current model for human telomerase reaction and strengthen the hypothesis that a G- quadruplex structure of telomere DNA plays an important role in the regulation of the telomerase reaction.
