| Creator | Title | Description | Subject | Date | ||
|---|---|---|---|---|---|---|
| 26 |
 |
Blumenthal, Donald K. | Structure of Vardenafil in the active site of PDE5 | 2006-07-14 | ||
| 27 |
 |
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 |
| 28 |
 |
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 |
| 29 |
 |
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 |