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Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα HoloenzymeLocalization and quaternary structure of the PKA RI holoenzymePKA RIα Homodimer Structure Reveals an Intermolecular Interface with Implications for Cooperative cAMP Binding and Carney Complex DiseaseThe roles of the RIIβ linker and N-terminal cyclic nucleotide-binding domain in determining the unique structures of the type IIβ protein kinase A: a small angle x-ray and neutron scattering study.In vivo evaluation of the delivery and efficacy of a sirolimus-laden polymer gel for inhibition of hyperplasia in a porcine model of arteriovenous hemodialysis graft stenosis.PDGF-induced proliferation in human arterial and venous smooth muscle cells: molecular basis for differential effects of PDGF isoforms.A kinase interacting protein (AKIP1) is a key regulator of cardiac stress.Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory.Sensing domain dynamics in protein kinase A-I{alpha} complexes by solution X-ray scattering.Development and characterization of fluorescently-labeled myosin light chain kinase calmodulin-binding domain peptides.Conformational differences among solution structures of the type Ialpha, IIalpha and IIbeta protein kinase A regulatory subunit homodimers: role of the linker regions.Differential effects of substrate on type I and type II PKA holoenzyme dissociation.The conformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding.Solution scattering reveals large differences in the global structures of type II protein kinase A isoforms.C subunits binding to the protein kinase A RI alpha dimer induce a large conformational change.Efficacy of local dipyridamole therapy in a porcine model of arteriovenous graft stenosis.An N-terminally truncated form of cyclic GMP-dependent protein kinase Iα (PKG Iα) is monomeric, autoinhibited, and provides a model for activation.Troponin I Inhibitory Peptide (96−115) Has an Extended Conformation When Bound to Skeletal Muscle Troponin C†Calmodulin Binding to Myosin Light Chain Kinase Begins at Substoichiometric Ca2+Concentrations: A Small-Angle Scattering Study of Binding and Conformational Transitions†Preparation and properties of the calmodulin-binding domain of skeletal muscle myosin light chain kinaseMyosin light chain kinases and myosin phosphorylation in skeletal muscleSynthetic peptides based on the calmodulin-binding domain of myosin light chain kinase inhibit activation of other calmodulin-dependent enzymesActivation and inhibition of phosphorylase kinase by monospecific antibodies raised against peptides from the regulatory domain of the gamma-subunitRegulation of myosin phosphorylationIdentification of the substrate and pseudosubstrate binding sites of phosphorylase kinase gamma-subunitLight chain phosphorylation alters the conformation of skeletal muscle myosinRegulation of contraction by myosin phosphorylation. A comparison between smooth and skeletal musclesAntipeptide antibodies as probes of subunit-dependent structural changes in the regulatory domain of the gamma-subunit of phosphorylase kinaseAdaptation of the protein kinase filter paper assay to a 96-well microtiter formatMechanism of dipyridamole's action in inhibition of venous and arterial smooth muscle cell proliferationDifferential effects of imatinib on PDGF-induced proliferation and PDGF receptor signaling in human arterial and venous smooth muscle cellsEvaluation of histological techniques for quantifying haemodialysis arteriovenous (AV) graft hyperplasiaCellular and morphological changes during neointimal hyperplasia development in a porcine arteriovenous graft modelDifferent signaling responses to anti-proliferative agents in human aortic and venous smooth muscle cellsDifferential gene expression patterns in vein regions susceptible versus resistant to neointimal hyperplasiaRational design, synthesis, and evaluation of uncharged, "smart" bis-oxime antidotes of organophosphate-inhibited human acetylcholinesteraseProductive reorientation of a bound oxime reactivator revealed in room temperature X-ray structures of native and VX-inhibited human acetylcholinesterase
P50
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P50
description
researcher ORCID ID = 0000-0002-8614-1167
@en
name
Donald K Blumenthal
@ast
Donald K Blumenthal
@en
Donald K Blumenthal
@es
Donald K Blumenthal
@nl
type
label
Donald K Blumenthal
@ast
Donald K Blumenthal
@en
Donald K Blumenthal
@es
Donald K Blumenthal
@nl
prefLabel
Donald K Blumenthal
@ast
Donald K Blumenthal
@en
Donald K Blumenthal
@es
Donald K Blumenthal
@nl
P1006
P214
P1006
P1153
7201929311
P214
P31
P496
0000-0002-8614-1167
P735
P7859
lccn-n87142162