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Creator | Title | Description | Subject | Date |
| 26 |
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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 |
| 27 |
 |
Keefe, Kristen A. | Introduction to autonomic pharmacology | | | 2006-09-12 |
| 28 |
 |
Blumenthal, Donald K. | Identification of molecular sites on factor VII which mediate its assembly and function in the extrinsic pathway activation complex. | Factor VII-VIIa, in association with tissue factor, participates in the complex which initiates blood coagulation through the extrinsic pathway. To identify functional domains on factor VII which mediate the activation of factor X, 16 synthetic peptides corresponding to 55% of the primary structure ... | Genetics; Biosynthesis; Pharmacology | 1991-01-15 |
| 29 |
 |
Bernstein, Paul S.; Gellermann, Werner | Nonmydriatic fluorescence-based quantitative imaging of human macular pigment distributions. | We have developed a CCD-camera-based nonmydriatic instrument that detects fluorescence from retinal lipofuscin chromophores ("autofluorescence") as a means to indirectly quantify and spatially image the distribution of macular pigment (MP). The lipofuscin fluorescence intensity is reduced at all ret... | Cytology; Sensitivity and Specificity | 2006-10 |
| 30 |
 |
Blumenthal, Donald K. | Structure of Vardenafil in the active site of PDE5 | | | 2006-07-14 |
| 31 |
 |
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 |
| 32 |
 |
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 |
| 33 |
 |
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 |
