Outputs (8)

Sertoli Cell Development and Function in an Animal Model of Testicular Dysgenesis Syndrome1 (2007)
Journal Article
Hutchison, G. R., Scott, H. M., Walker, M., McKinnell, C., Ferrara, D., Mahood, I. K., & Sharpe, R. M. (2008). Sertoli Cell Development and Function in an Animal Model of Testicular Dysgenesis Syndrome1. Biology of Reproduction, 78(2), 352-360. https://doi.org/10.1095/biolreprod.107.064006

Pregnancy exposure to di(n-butyl) phthalate (DBP) in rats induces a testicular dysgenesislike syndrome (TDS) in male offspring. Earlier studies suggested altered Sertoli cell development/maturation may result, especially in testes that become cryptor... Read More about Sertoli Cell Development and Function in an Animal Model of Testicular Dysgenesis Syndrome1.

The origins and time of appearance of focal testicular dysgenesis in an animal model of testicular dysgenesis syndrome: evidence for delayed testis development? (2007)
Journal Article
Hutchison, G. R., Sharpe, R. M., Mahood, I. K., Jobling, M., Walker, M., McKinnell, C., Mason, J. I., & Scott, H. M. (2008). The origins and time of appearance of focal testicular dysgenesis in an animal model of testicular dysgenesis syndrome: evidence for delayed testis development?. International Journal of Andrology, 31(2), 103-111. https://doi.org/10.1111/j.1365-2605.2007.00816.x

A testicular dysgenesis-like syndrome is induced in rats by fetal exposure todi(n-butyl) phthalate (DBP). A key feature of this is the formation of focal dys-genetic areas comprising malformed seminiferous cords⁄tubules and intratubu-lar Leydig cells... Read More about The origins and time of appearance of focal testicular dysgenesis in an animal model of testicular dysgenesis syndrome: evidence for delayed testis development?.

Reduced alveolar macrophage migration induced by acute ambient particle (PM10) exposure (2007)
Journal Article
Barlow, P. G., Brown, D. M., Donaldson, K., MacCallum, J., & Stone, V. (2008). Reduced alveolar macrophage migration induced by acute ambient particle (PM10) exposure. Cell Biology and Toxicology, 24(3), 243-252. https://doi.org/10.1007/s10565-007-9033-y

Increased levels of particulate air pollution (PM10) have been implicated as a causal agent in pulmonary disease exacerbation and increased deaths from respiratory and cardiovascular disorders. The exact mechanism by which PM10 drives toxicity in the... Read More about Reduced alveolar macrophage migration induced by acute ambient particle (PM10) exposure.

Nanoparticle interactions with zinc and iron: Implications for toxicology and inflammation (2007)
Journal Article
Wilson, M. R., Foucaud, L., Barlow, P. G., Hutchison, G. R., Sales, J., Simpson, R. J., & Stone, V. (2007). Nanoparticle interactions with zinc and iron: Implications for toxicology and inflammation. Toxicology and Applied Pharmacology, 225(1), 80-89. https://doi.org/10.1016/j.taap.2007.07.012

Particulate air pollution (PM10) consists of a mixture of components, including nanoparticles and metals. Studies from our laboratory have demonstrated that transition metals can potentiate the ability of nanoparticles to induce lung inflammation and... Read More about Nanoparticle interactions with zinc and iron: Implications for toxicology and inflammation.

The MDM2 Ubiquitination Signal in the DNA-Binding Domain of p53 Forms a Docking Site for Calcium Calmodulin Kinase Superfamily Members (2007)
Journal Article
Craig, A. L., Chrystal, J. A., Fraser, J. A., Sphyris, N., Lin, Y., Harrison, B. J., Scott, M. T., Dornreiter, I., & Hupp, T. R. (2007). The MDM2 Ubiquitination Signal in the DNA-Binding Domain of p53 Forms a Docking Site for Calcium Calmodulin Kinase Superfamily Members. Molecular and Cellular Biology, 27(9), 3542-3555. https://doi.org/10.1128/mcb.01595-06

Genetic and biochemical studies have shown that Ser20 phosphorylation in the transactivation domain of p53 mediates p300-catalyzed DNA-dependent p53 acetylation and B-cell tumor suppression. However, the protein kinases that mediate this modification... Read More about The MDM2 Ubiquitination Signal in the DNA-Binding Domain of p53 Forms a Docking Site for Calcium Calmodulin Kinase Superfamily Members.

Identification of a dominant negative functional domain on DAPK-1 that degrades DAPK-1 protein and stimulates TNFR-1-mediated apoptosis. (2007)
Journal Article
Lin, Y., Stevens, C., & Hupp, T. (2007). Identification of a dominant negative functional domain on DAPK-1 that degrades DAPK-1 protein and stimulates TNFR-1-mediated apoptosis. Journal of Biological Chemistry, 282(23), 16792-16802. https://doi.org/10.1074/jbc.M611559200

DAPK-1 is a stress-activated tumor suppressor protein that plays a role in both proapoptotic or antiapoptotic signal transduction pathways. To define mechanisms of DAPK-1 protein regulation, we have determined that DAPK-1 protein has a long half-life... Read More about Identification of a dominant negative functional domain on DAPK-1 that degrades DAPK-1 protein and stimulates TNFR-1-mediated apoptosis..

Chemical Genetics Approach to Identify Peptide Ligands that Selectively Stimulate DAPK-1 Kinase Activity (2007)
Journal Article
Fraser, J. A., & Hupp, T. R. (2007). Chemical Genetics Approach to Identify Peptide Ligands that Selectively Stimulate DAPK-1 Kinase Activity. Biochemistry, 46(10), 2655-2673. https://doi.org/10.1021/bi061562j

Dissection of signal transduction pathways has been advanced by classic genetic approaches including targeted gene deletion and siRNA-based inhibition of gene product synthesis. Chemical genetics is a biochemical approach to develop small peptide-mim... Read More about Chemical Genetics Approach to Identify Peptide Ligands that Selectively Stimulate DAPK-1 Kinase Activity.

A Germ Line Mutation in the Death Domain of DAPK-1 Inactivates ERK-induced Apoptosis (2007)
Journal Article
Stevens, C., Lin, Y., Sanchez, M., Amin, E., Copson, E., White, H., Durston, V., Eccles, D. M., & Hupp, T. (2007). A Germ Line Mutation in the Death Domain of DAPK-1 Inactivates ERK-induced Apoptosis. Journal of Biological Chemistry, 282(18), 13791-13803. https://doi.org/10.1074/jbc.m605649200

p53 is activated genetically by a set of kinases that are components of the calcium calmodulin kinase superfamily, including CHK2, AMP kinase, and DAPK-1. In dissecting the mechanism of DAPK-1 control, a novel mutation (N1347S) was identified in the... Read More about A Germ Line Mutation in the Death Domain of DAPK-1 Inactivates ERK-induced Apoptosis.