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| Creator | Title | Description | Subject | Date | ||
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Baehr, Wolfgang; Prestwich, Glenn D. | Photoreceptor cGMP phosphodiesterase delta subunit (PDEdelta) functions as a prenyl-binding protein | Bovine PDEdelta was originally copurified with rod cGMP phosphodiesterase (PDE) and shown to interact with prenylated, carboxymethylated C-terminal Cys residues. Other studies showed that PDEdelta can interact with several small GTPases including Rab13, Ras, Rap, and Rho6, all of which are prenylate... | Fluorescence Resonance Energy Transfer; GTP Phosphohydrolases; Immunohistochemistry | 2004 |
| 2 |
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Hendee, Shonn P.; Faour, Fouad A.; Christensen, Douglas A.; Patrick, Baharah; Durney, Carl H.; Blumenthal, Donald K. | Effects of weak extremely low frequency magnetic fields on calcium/calmodulin interactions. | Mechanisms by which weak electromagnetic fields may affect biological systems are of current interest because of their potential health effects. Lednev has proposed an ion parametric resonance hypothesis (Lednev, 1991, Bioelectromagnetics, 12:71-75), which predicts that when the ac, frequency of a c... | Electromagnetic Fields; Calcium-binding Proteins; Lednev's Theory | 1996-06 |
| 3 |
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Blumenthal, Donald K.; Wangsgard, Wendy P.; Meixell, Glenn E. | Activation and inhibition of phosphorylase kinase by monospecific antibodies raised against peptides from the regulatory domain of the gamma-subunit. | The C terminus of the catalytic gamma-subunit of phosphorylase kinase comprises a regulatory domain that contains regions important for subunit interactions and autoinhibitory functions. Monospecific antibodies raised against four synthetic peptides from this region, PhK1 (362-386), PhK5 (342-366), ... | Subunit Interaction; Autoinhibitory Functions; Immunology; Antagonists & Inhibitors | 1995-08-30 |
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