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| Creator | Title | Description | Subject | Date | ||
|---|---|---|---|---|---|---|
| 1 |
 | 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 |
| 2 |
 | Blumenthal, Donald K.; Trewhella, Jill | Conformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding. | Different isoforms of the full-length protein kinase A (PKA) regulatory subunit homodimer (R2) and the catalytic (C) subunit-bound holoenzyme (R2C2) have very different global structures despite similar molecular weights and domain organization within their primary sequences. To date, it has been th... | Protein Isoforms; Global Structures; cAMP | 2005-10-21 |
| 3 |
 | Blumenthal, Donald K. | Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory. | Phosphorylase kinase is a multimeric protein kinase (alpha 4 beta 4 gamma 4 delta 4) whose enzymatic activity is conferred by its gamma-subunit. A library of 18 overlapping synthetic peptides spanning residues 277-386 of the gamma-subunit has been prepared to use in identifying important regulatory ... | Metabolism; Phosphorylase Kinase | 1995-09-22 |
| 4 |
 | 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 |
| 5 |
 | 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 |
| 6 |
 | Poulter, Charles Dale | Prenyltransferase. Kinetic studies of the 1'-4 coupling reaction with avian liver enzyme. | Prenyltransferase catalyzes the sequential, irreversible 1'-4 condensation of isopentenyl-PP with dimethylallyl-PP and geranyl-PP to yield farnesyl-PP. A kinetic study shows substrate inhibition by isopentenyl-PP at concentrations above 0.7 microM when the concentration of geranyl-PP is 1.0 microM o... | Birds; Kinetics; Structure-Activity Relationship; Substrate Specificity | 1979-10-10 |
| 7 |
 | Blumenthal, Donald K. | Identification of the substrate and pseudosubstrate binding sites of phosphorylase kinase gamma-subunit. | Using site-directed mutagenesis, we proposed that an autoinhibitory domain(s) is located at the C-terminal region (301-386) of the phosphorylase kinase gamma-subunit (Huang, C.-Y.F., Yuan C.-J., Livanova, N.B., and Graves, D.J. (1993) Mol. Cell. Biochem. 127/128, 7-18). Removal of the putative inhib... | Mutagenesis; Autoinhibitory Domain; Peptides | 1995-03-31 |
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