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| Creator | Title | Description | Subject | Date | ||
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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 |
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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 |
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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 |
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