Search Results - "Blumenthal, D K"

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    The γ-Subunit of Skeletal Muscle Phosphorylase Kinase Contains Two Noncontiguous Domains That Act in Concert to Bind Calmodulin by Dasgupta, M, Honeycutt, T, Blumenthal, D K

    Published in The Journal of biological chemistry (15-10-1989)
    “…Phosphorylase kinase is a Ca2+-regulated, multisubunit enzyme that contains calmodulin as an integral subunit (termed the δ-subunit). Ca2+-dependent activity…”
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    Dephosphorylation of cAMP-dependent protein kinase regulatory subunit (type II) by calmodulin-dependent protein phosphatase. Determinants of substrate specificity by Blumenthal, D K, Takio, K, Hansen, R S, Krebs, E G

    Published in The Journal of biological chemistry (25-06-1986)
    “…Calmodulin-dependent protein phosphatase purified from bovine cardiac muscle catalyzed the rapid dephosphorylation of Ser-95 of bovine cardiac cAMP-dependent…”
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    Identification of the Calmodulin-Binding Domain of Skeletal Muscle Myosin Light Chain Kinase by Blumenthal, Donald K., Takio, Koji, Edelman, Arthur M., Charbonneau, Harry, Titani, Koiti, Walsh, Kenneth A., Krebs, Edwin G.

    “…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…”
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    Cellular and morphological changes during neointimal hyperplasia development in a porcine arteriovenous graft model by Li, Li, Terry, Christi M., Blumenthal, Donald K., Kuji, Tadashi, Masaki, Takahisa, Kwan, Bonnie C. H., Zhuplatov, Ilya, Leypoldt, John K., Cheung, Alfred K.

    Published in Nephrology, dialysis, transplantation (01-11-2007)
    “…Background. Implantation of a haemodialysis arteriovenous graft is often followed by the development of neointimal hyperplasia (NH) at the venous anastomosis…”
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    Changes in the structure of calmodulin induced by a peptide based on the calmodulin-binding domain of myosin light chain kinase by Heidorn, D. B, Seeger, P. A, Rokop, S. E, Blumenthal, D. K, Means, A. R, Crespi, H, Trewhella, Jill

    Published in Biochemistry (Easton) (08-08-1989)
    “…Small-angle X-ray and neutron scattering data were used to study the solution structure of calmodulin complexed with a synthetic peptide corresponding to…”
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    Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain by Kennelly, P J, Edelman, A M, Blumenthal, D K, Krebs, E G

    Published in The Journal of biological chemistry (05-09-1987)
    “…A synthetic peptide modeled after the calmodulin (CaM)-binding domain of rabbit skeletal muscle myosin light chain kinase,…”
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    The effects of deletions in the central helix of calmodulin on enzyme activation and peptide binding by Persechini, A, Blumenthal, D K, Jarrett, H W, Klee, C B, Hardy, D O, Kretsinger, R H

    Published in The Journal of biological chemistry (15-05-1989)
    “…Using site-directed mutagenesis we have expressed in Escherichia coli three engineered calmodulins (CaM) containing deletions in the solvent-exposed region of…”
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    Common components of patch-clamp internal recording solutions can significantly affect protein kinase A activity by Vargas, Gricelly, Yeh, Tsung-Yin J, Blumenthal, Donald K, Lucero, Mary T

    Published in Brain research (15-05-1999)
    “…Common components of whole-cell internal recording solutions were tested both in vitro and in patch-clamp experiments for their effects on the activity of…”
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    Small-angle scattering studies show distinct conformations of calmodulin in its complexes with two peptides based on the regulatory domain of the catalytic subunit of phosphorylase kinase by Trewhella, Jill, Blumenthal, D. K, Rokop, S. E, Seeger, P. A

    Published in Biochemistry (Easton) (01-10-1990)
    “…Small-angle X-ray and neutron scattering have been used to study the solution structures of calmodulin complexed with synthetic peptides corresponding to…”
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    Efficacy of local dipyridamole therapy in a porcine model of arteriovenous graft stenosis by Kuji, T., Masaki, T., Goteti, K., Li, L., Zhuplatov, S., Terry, C.M., Zhu, W., Leypoldt, J.K., Rathi, R., Blumenthal, D.K., Kern, S.E., Cheung, A.K.

    Published in Kidney international (01-06-2006)
    “…Perivascular delivery of antiproliferative drugs has been proposed as an approach to prevent neointimal hyperplasia associated with hemodialysis…”
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    Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase by Edelman, A M, Takio, K, Blumenthal, D K, Hansen, R S, Walsh, K A, Titani, K, Krebs, E G

    Published in The Journal of biological chemistry (15-09-1985)
    “…Limited proteolysis has been utilized to study the structural organization of rabbit skeletal muscle myosin light chain kinase. The enzyme (Mr approximately…”
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    Characterization of the phosphotyrosyl protein phosphatase activity of calmodulin-dependent protein phosphatase by Chan, C P, Gallis, B, Blumenthal, D K, Pallen, C J, Wang, J H, Krebs, E G

    Published in The Journal of biological chemistry (25-07-1986)
    “…Calmodulin-dependent protein phosphatase from bovine brain and heart was assayed for phosphotyrosine and phosphoserine phosphatase activity using several…”
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    Conformational Differences Among Solution Structures of the Type Iα, IIα and IIβ Protein Kinase A Regulatory Subunit Homodimers: Role of the Linker Regions by Vigil, Dominico, Blumenthal, Donald K., Heller, William T., Brown, Simon, Canaves, Jaume M., Taylor, Susan S., Trewhella, Jill

    Published in Journal of molecular biology (09-04-2004)
    “…The regulatory (R) subunits of the cAMP-dependent protein kinase (protein kinase A or PKA) are multi-domain proteins responsible for conferring cAMP-dependence…”
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    Evidence for domain organization within the 61-kDa calmodulin-dependent cyclic nucleotide phosphodiesterase from bovine brain by Charbonneau, Harry, Kumar, Santosh, Novack, Jeffrey P, Blumenthal, Donald K, Griffin, Patrick R, Shabanowitz, Jeffrey, Hunt, Donald F, Beavo, Joseph A, Walsh, Kenneth A

    Published in Biochemistry (Easton) (13-08-1991)
    “…The complete amino acid sequence of the 61-kDa calmodulin-dependent, cyclic nucleotide phosphodiesterase (CaM-PDE) from bovine brain has been determined. The…”
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    Identification of molecular sites on factor VII which mediate its assembly and function in the extrinsic pathway activation complex by Kumar, A, Blumenthal, D K, Fair, D S

    Published in The Journal of biological chemistry (15-01-1991)
    “…Factor VII-VIIa, in association with tissue factor, participates in the complex which initiates blood coagulation through the extrinsic pathway. To identify…”
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    Interaction of calmodulin and a calmodulin-binding peptide from myosin light chain kinase: major spectral changes in both occur as the result of complex formation by Klevit, Rachel E, Blumenthal, Donald K, Wemmer, David E, Krebs, Edwin G

    Published in Biochemistry (Easton) (01-12-1985)
    “…Many different enzymes are activated by direct interaction with calmodulin; this interaction is thought to occur through a distinct calmodulin-binding domain…”
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    Amino acid sequence of rabbit skeletal muscle myosin light chain kinase by Takio, Koji, Blumenthal, Donald K, Walsh, Kenneth A, Titani, Koiti, Krebs, Edwin G

    Published in Biochemistry (Easton) (02-12-1986)
    “…The amino acid sequence of the amino-terminal, 235-residue segment of rabbit skeletal muscle myosin light chain kinase has been determined. Together with the…”
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    Amino acid sequence of an active fragment of rabbit skeletal muscle myosin light chain kinase by Takio, Koji, Blumenthal, Donald K, Edelman, Arthur M, Walsh, Kenneth A, Krebs, Edwin G, Titani, Koiti

    Published in Biochemistry (Easton) (01-10-1985)
    “…The amino acid sequence of a 368-residue segment at the carboxyl-terminus of rabbit skeletal muscle myosin light chain kinase (MLCK) has been determined. The…”
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