About: Donald K Blumenthal

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

researcher ORCID ID = 0000-0002-8614-1167

Attributes	Values
rdf:type	Item
description	ikertzailea (eu) 研究者 (ja) araştırmacı (tr) باحت (ary) 研究者 (zh) onderzoeker (nl) researcher ORCID ID = 0000-0002-8614-1167 (en)
rdfs:label	Donald K Blumenthal (en) Donald K Blumenthal (es) Donald K Blumenthal (nl) Donald K Blumenthal (ast)
skos:prefLabel	Donald K Blumenthal (en) Donald K Blumenthal (es) Donald K Blumenthal (nl) Donald K Blumenthal (ast)
name	Donald K Blumenthal (en) Donald K Blumenthal (es) Donald K Blumenthal (nl) Donald K Blumenthal (ast)
Scopus author ID	wds:Q60169003-80D70429-B5C0-435C-92D7-1930880BA32A
Scopus author ID	7201929311
given name	wds:Q60169003-B840CFB3-9103-469A-A81F-6CD4A011B5A6
given name	Donald
instance of	wds:Q60169003-CD5A093A-4F74-4910-AB3E-4895436D7283
instance of	Homo sapiens
skos:altLabel	Donald Blumenthal (en)
Nationale Thesaurus voor Auteursnamen ID	wds:Q60169003-7bef1c99-b97c-4648-a661-503d4f9194bf
occupation	wds:Q60169003-A647A5C4-D80C-445A-B036-5E2844011DF6
employer	wds:Q60169003-98C7E917-07AA-4392-B535-6734D9E3B71F
sex or gender	wds:Q60169003-64F7D418-C93C-4FE1-A84F-BC10C23B8AB9
VIAF ID	wds:Q60169003-2FEF3E7A-0B00-41B7-9814-3F481C1DBD21
GND ID	wds:Q60169003-bcd0e9a4-58a1-4b06-ae81-50e89260a709
date of birth	wds:Q60169003-F171AA3C-C3EA-4300-B541-CC435DCB0198
educated at	wds:Q60169003-61975BDB-9782-49C7-AA6A-A9E7DB5BFA9C
PLWABN ID	wds:Q60169003-0809C9FD-A297-487D-91B3-4BE0049E7A2A
family name	wds:Q60169003-241A2312-71E0-477D-B5C9-91E07F2B4226
WorldCat Identities ID (superseded)	wds:Q60169003-D86F4666-C131-4DE2-A50E-213F67237BE9
National Library of Israel J9U ID	wds:Q60169003-3F3C5AA6-5556-437B-B705-9A33833FD539
Nationale Thesaurus voor Auteursnamen ID	http://data.bibliotheken.nl/id/thes/p305318403
VIAF ID	http://viaf.org/viaf/161947204
GND ID	https://d-nb.info/gnd/1151163473
Nationale Thesaurus voor Auteursnamen ID	305318403
occupation	researcher
employer	University of Utah
sex or gender	male
VIAF ID	161947204
GND ID	1151163473
date of birth	1953-01-01 00:00:00Z (xsd:dateTime)
educated at	University of California, San Diego
PLWABN ID	9810558889605606
family name	Blumenthal
WorldCat Identities ID (superseded)	lccn-n87142162
National Library of Israel J9U ID	987007325557105171
ORCID iD	wds:Q60169003-3286A63A-633E-4AE0-A0CF-10F52D3D2E03
ORCID iD	https://orcid.org/0000-0002-8614-1167
ORCID iD	0000-0002-8614-1167
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q60169003
is author of	Myosin light chain kinases and myosin phosphorylation in skeletal muscle Regulation of myosin phosphorylation Localization and quaternary structure of the PKA RI holoenzyme A kinase interacting protein (AKIP1) is a key regulator of cardiac stress. Troponin I Inhibitory Peptide (96−115) Has an Extended Conformation When Bound to Skeletal Muscle Troponin C† Activation and inhibition of phosphorylase kinase by monospecific antibodies raised against peptides from the regulatory domain of the gamma-subunit Isoform Specific Differences in Binding of a Dual-Specificity A-Kinase Anchoring Protein to Type I and Type II Regulatory Subunits of PKA The 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. 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 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. PDGF-induced proliferation in human arterial and venous smooth muscle cells: molecular basis for differential effects of PDGF isoforms. Sensing domain dynamics in protein kinase A-I{alpha} complexes by solution X-ray scattering. Cellular and morphological changes during neointimal hyperplasia development in a porcine arteriovenous graft model Efficacy of local dipyridamole therapy in a porcine model of arteriovenous graft stenosis. Realizing the Allosteric Potential of the Tetrameric Protein Kinase A RIα Holoenzyme PKA RIα Homodimer Structure Reveals an Intermolecular Interface with Implications for Cooperative cAMP Binding and Carney Complex Disease Differential effects of imatinib on PDGF-induced proliferation and PDGF receptor signaling in human arterial and venous smooth muscle cells Mechanism of dipyridamole's action in inhibition of venous and arterial smooth muscle cell proliferation Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory. Light chain phosphorylation alters the conformation of skeletal muscle myosin Identification of the substrate and pseudosubstrate binding sites of phosphorylase kinase gamma-subunit Regulation of contraction by myosin phosphorylation. A comparison between smooth and skeletal muscles Calmodulin Binding to Myosin Light Chain Kinase Begins at Substoichiometric Ca2+Concentrations: A Small-Angle Scattering Study of Binding and Conformational Transitions† Different signaling responses to anti-proliferative agents in human aortic and venous smooth muscle cells Synthetic peptides based on the calmodulin-binding domain of myosin light chain kinase inhibit activation of other calmodulin-dependent enzymes The conformationally dynamic C helix of the RIalpha subunit of protein kinase A mediates isoform-specific domain reorganization upon C subunit binding Evaluation of histological techniques for quantifying haemodialysis arteriovenous (AV) graft hyperplasia Antipeptide antibodies as probes of subunit-dependent structural changes in the regulatory domain of the gamma-subunit of phosphorylase kinase Differential gene expression patterns in vein regions susceptible versus resistant to neointimal hyperplasia Preparation and properties of the calmodulin-binding domain of skeletal muscle myosin light chain kinase Adaptation of the protein kinase filter paper assay to a 96-well microtiter format An N-terminally truncated form of cyclic GMP-dependent protein kinase Iα (PKG Iα) is monomeric, autoinhibited, and provides a model for activation. Development and characterization of fluorescently-labeled myosin light chain kinase calmodulin-binding domain peptides. 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. Rational design, synthesis, and evaluation of uncharged, "smart" bis-oxime antidotes of organophosphate-inhibited human acetylcholinesterase Productive reorientation of a bound oxime reactivator revealed in room temperature X-ray structures of native and VX-inhibited human acetylcholinesterase
is author of	wds:Q30365578-9D47668C-9192-47E5-9C18-5B6BDDF24C68 wds:Q44437436-749280A8-5677-44AB-B92B-2F69484B300C wds:Q72132115-DDDD3078-AF91-46C4-8685-F667F85A98AD wds:Q72867382-3E3AF07D-6986-4FF5-A2A5-1E7123870943

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