Short communicationStructure and function of the HOX A1 human homeobox gene cDNA
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Cited by (26)
Polyhistidine tract expansions in HOXA1 result in intranuclear aggregation and increased cell death
2005, Biochemical and Biophysical Research CommunicationsCitation Excerpt :It is generally believed that an altered, aggregation prone, conformation of the mutant protein confers the loss of a normal function, the gain of a toxic new function, or both [10–12]. In HOXA1 protein, polyhistidine is thought to be the site to interact with other proteins [4] and the variation in histidine repeat lengths may influence the function of the proteins that bind to HOXA1. Alteration of protein partner binding interaction is already described to confer neuronal damage in polyglutamine diseases, such as HIP-1, HAP, and GAPDH (as well as many others) for huntingtin [21–23], LANP and GAPDH for ataxin-1 [24], and A2BP for ataxin-2 [24,25].
Human growth hormone-regulated HOXA1 is a human mammary epithelial oncogene
2003, Journal of Biological ChemistryCitation Excerpt :The level of β-actin mRNA did not differ between the two cell lines under the different treatment conditions and was used as a control for RNA quality (Fig. 1 A). HOXA1 cDNA transfected into MCF-7 cells results in the appearance of two distinct protein species of 33 and 35 kDa (for example see Fig.2 B) as expected (37). To determine if the autocrine hGH-stimulated increase in HOXA1mRNA also resulted in increased HOXA1 protein, we examined the level of HOXA1 protein in nuclear extracts collected from MCF7-MUT and MCF7-hGH cells by Western blot analysis.
Biological significance of insulin-like growth factor binding proteins
2002, NeuroImmune BiologyDisrtruption of a novel imprinted zinc-finger gene, ZNF215, in Beckwith- Wiedemann syndrome
2000, American Journal of Human GeneticsCitation Excerpt :The finding that both ZNF214 and ZNF215V1 proteins are transported to the nucleus, as determined by transfection studies using GFP fusion proteins, is compatible with such a role. Alternative-spliced transcripts encoding truncated proteins are also found in some other transcription factors—for example, some members of the HOX gene family, whose alternative transcripts encode proteins lacking the homeobox domain (La Rosa et al. 1988; Shen et al. 1991; Hong et al. 1995; Fujimoto et al. 1998). The ZNF215V2 and ZNF215V3 alternative-spliced transcripts are partially antisense of ZNF214, and it is possible that transcription of ZNF215V2 and ZNF215V3 may modulate levels of ZNF214 transcription or translation.
Novel aspects of the insulin-like growth factor binding proteins
1999, Molecular Genetics and MetabolismEndothelial cells express a novel, tumor necrosis factor-α-regulated variant of HOXA9
1999, Journal of Biological Chemistry
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Present address: Division of Medical Oncology, Department of Internal Medicine, Kangnam St. Mary's Hospital, Catholic University, Medical College, Seoul, South Korea.