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Creator | Title | Description | Subject | Date |
| 26 |
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Blumenthal, Donald K. | Structure of Vardenafil in the active site of PDE5 | | | 2006-07-14 |
| 27 |
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Blumenthal, Donald K. | C subunits binding to the protein kinase A RI alpha dimer induce a large conformational change. | We present structural data on the RI alpha isoform of the cAMP-dependent protein kinase A that reveal, for the first time, a large scale conformational change within the RI alpha homodimer upon catalytic subunit binding. This result infers that the inhibition of catalytic subunit activity is not the... | Protein Kinase; cAMP | 2004-04-30 |
| 28 |
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Blumenthal, Donald K.; Underwood, Clayton J. | Adaptation of the protein kinase filter paper assay to a 96-well microtiter format. | The most widely used method for assaying protein kinase activities involves incorporation of radioactive phosphate into a protein or peptide substrate with subsequent binding or precipitaion of the radiolabeled substrate onto filter paper squares. We have adapted this assay for use with readily avai... | Protein Kinase Activities; Filter Papers; Radioactive Phosphate | 1999-02-01 |
| 29 |
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Blumenthal, Donald K. | Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain. | A synthetic peptide modeled after the calmodulin (CaM)-binding domain of rabbit skeletal muscle myosin light chain kinase, Lys-Arg-Arg-Trp-Lys5-Lys-Asn-Phe-Ile-Ala10-Val-Ser-Ala-Ala-+ ++Asn15-Arg-Phe-Glycyl amide (M5), inhibited the CaM-independent chymotryptic fragment of the enzyme, C35 (Edelman, ... | Synthetic Peptide | 1987-09-05 |
