Filters: Department: "Biomedical Informatics" Format: "application/pdf" School Or College: "College of Pharmacy" Collection: "ir_uspace"
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| Creator | Title | Description | Subject | Date | ||
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Blumenthal, Donald K. | Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase. | Limited proteolysis has been utilized to study the structural organization of rabbit skeletal muscle myosin light chain kinase. The enzyme (Mr approximately 89,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis) consists of an amino-terminal, protease-susceptible region of unidentified... | Enzymology; Skeletal Muscle; Proteolysis, Peptide Fragments | 1995-09-15 |
| 2 |
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Blumenthal, Donald K. | Characterization of the phosphotyrosyl protein phosphatase activity of calmodulin-dependent protein phosphatase. | Calmodulin-dependent protein phosphatase from bovine brain and heart was assayed for phosphotyrosine and phosphoserine phosphatase activity using several substrates: 1) smooth muscle myosin light chain (LC20) phosphorylated on tyrosine or serine residues, 2) angiotensin I phosphorylated on tyrosine,... | Metabolism; Phosphatase Activity | 1986-07-25 |
| 3 |
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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 |
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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 |
| 5 |
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Blumenthal, Donald K. | Dephosphorylation of cAMP-dependent protein kinase regulatory subunit (type II) by calmodulin-dependent protein phosphatase. Determinants of substrate specificity. | Calmodulin-dependent protein phosphatase purified from bovine cardiac muscle catalyzed the rapid dephosphorylation of Ser-95 of bovine cardiac cAMP-dependent protein kinase regulatory subunit (RII). The kinetic constants determined for the reaction (Km = 20 microM; Vmax = 2 mumol min-1 mg-1) are com... | Metabolism; High Pressure Liquid; Enzymology | 1985-06-25 |
| 6 |
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Blumenthal, Donald K. | Effects of deletions in the central helix of calmodulin on enzyme activation and peptide binding. | Using site-directed mutagenesis we have expressed in Escherichia coli three engineered calmodulins (CaM) containing deletions in the solvent-exposed region of the central helix. These are CaM delta 84, Glu-84 removed; CaM delta 83-84, Glu-83 and Glu-84 removed; and CaM delta 81-84, Ser-81 through Gl... | Drug Effects; Genetics; Metabolism | 1989-05-15 |
| 7 |
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Blumenthal, Donald K. | Gamma-subunit of skeletal muscle phosphorylase kinase contains two noncontiguous domains that act in concert to bind calmodulin. | Phosphorylase kinase is a Ca2+-regulated, multisubunit enzyme that contains calmodulin as an integral subunit (termed the delta-subunit). Ca2+-dependent activity of the enzyme is thought to be regulated by direct interaction of the delta-subunit with the catalytic subunit (the gamma-subunit) in the ... | Pharmacology; Metabolism; Enzymology | 1989-10-15 |
| 8 |
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Blumenthal, Donald K. | Identification of the calmodulin-binding domain of skeletal muscle myosin light | In the course of determining the primary structure of rabbit skeletal muscle myosin light chain kinase (MLCK; ATP:protein phosphotransferase, EC 2.7.1.37) a peptide fragment was obtained that appears to represent the calmodulin-binding domain of this enzyme. Low concentrations of the peptide inhibit... | Peptides; Enzymes; Protein sequence | 1985-05 |
| 9 |
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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 |
| 10 |
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Blumenthal, Donald K. | Phosphorylation of cardiac troponin by guanosine 3':5'-monophosphate-dependent protein kinase. | Homogeneous cGMP-dependent protein kinase catalyzes the rapid incorporation of phosphate, specifically into the inhibitory subunit of purified cardiac troponin with a maximal incorporation of 1 mol of phosphate/mol of troponin. When troponin was incubated in the presence of both cGMP- and cAMP-depen... | Protein Kinases | 1978-01-25 |
| 11 |
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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 |
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