Direct monitoring of the conformational equilibria of the activation loop in the mitogen-activated protein kinase p38α
Lade...
Dateien
Zu diesem Dokument gibt es keine Dateien.
Datum
2018
Autor:innen
Herausgeber:innen
ISSN der Zeitschrift
Electronic ISSN
ISBN
Bibliografische Daten
Verlag
Schriftenreihe
Auflagebezeichnung
DOI (zitierfähiger Link)
Internationale Patentnummer
Angaben zur Forschungsförderung
Projekt
Open Access-Veröffentlichung
Sammlungen
Core Facility der Universität Konstanz
Titel in einer weiteren Sprache
Publikationstyp
Zeitschriftenartikel
Publikationsstatus
Published
Erschienen in
Chemical Communications : ChemComm. 2018, 54(85), pp. 12057-12060. ISSN 1359-7345. eISSN 1364-548X. Available under: doi: 10.1039/c8cc06128a
Zusammenfassung
Conformational transitions in protein kinases are crucial for the biological function of these enzymes. Here, we characterize and assess conformational equilibria of the activation loop and the effect of small molecule inhibitors in the MAP kinase p38α. Our work experimentally revealed the existence of a two-state equilibrium for p38α while the addition of inhibitors shifts the equilibrium between these two states.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
540 Chemie
Schlagwörter
Konferenz
Rezension
undefined / . - undefined, undefined
Zitieren
ISO 690
ROSER, Patrick, Jörn WEISNER, Jeffrey R. SIMARD, Daniel RAUH, Malte DRESCHER, 2018. Direct monitoring of the conformational equilibria of the activation loop in the mitogen-activated protein kinase p38α. In: Chemical Communications : ChemComm. 2018, 54(85), pp. 12057-12060. ISSN 1359-7345. eISSN 1364-548X. Available under: doi: 10.1039/c8cc06128aBibTex
@article{Roser2018-10-23Direc-43852, year={2018}, doi={10.1039/c8cc06128a}, title={Direct monitoring of the conformational equilibria of the activation loop in the mitogen-activated protein kinase p38α}, number={85}, volume={54}, issn={1359-7345}, journal={Chemical Communications : ChemComm}, pages={12057--12060}, author={Roser, Patrick and Weisner, Jörn and Simard, Jeffrey R. and Rauh, Daniel and Drescher, Malte} }
RDF
<rdf:RDF xmlns:dcterms="http://purl.org/dc/terms/" xmlns:dc="http://purl.org/dc/elements/1.1/" xmlns:rdf="http://www.w3.org/1999/02/22-rdf-syntax-ns#" xmlns:bibo="http://purl.org/ontology/bibo/" xmlns:dspace="http://digital-repositories.org/ontologies/dspace/0.1.0#" xmlns:foaf="http://xmlns.com/foaf/0.1/" xmlns:void="http://rdfs.org/ns/void#" xmlns:xsd="http://www.w3.org/2001/XMLSchema#" > <rdf:Description rdf:about="https://kops.uni-konstanz.de/server/rdf/resource/123456789/43852"> <dcterms:issued>2018-10-23</dcterms:issued> <dc:creator>Roser, Patrick</dc:creator> <dc:contributor>Weisner, Jörn</dc:contributor> <dc:contributor>Roser, Patrick</dc:contributor> <dcterms:available rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2018-11-15T13:38:39Z</dcterms:available> <dc:creator>Drescher, Malte</dc:creator> <bibo:uri rdf:resource="https://kops.uni-konstanz.de/handle/123456789/43852"/> <dc:contributor>Rauh, Daniel</dc:contributor> <dc:language>eng</dc:language> <dc:creator>Simard, Jeffrey R.</dc:creator> <dc:date rdf:datatype="http://www.w3.org/2001/XMLSchema#dateTime">2018-11-15T13:38:39Z</dc:date> <dcterms:isPartOf rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/> <dspace:isPartOfCollection rdf:resource="https://kops.uni-konstanz.de/server/rdf/resource/123456789/29"/> <void:sparqlEndpoint rdf:resource="http://localhost/fuseki/dspace/sparql"/> <dc:creator>Rauh, Daniel</dc:creator> <dc:contributor>Drescher, Malte</dc:contributor> <dc:contributor>Simard, Jeffrey R.</dc:contributor> <dc:creator>Weisner, Jörn</dc:creator> <dcterms:title>Direct monitoring of the conformational equilibria of the activation loop in the mitogen-activated protein kinase p38α</dcterms:title> <foaf:homepage rdf:resource="http://localhost:8080/"/> <dcterms:abstract xml:lang="eng">Conformational transitions in protein kinases are crucial for the biological function of these enzymes. Here, we characterize and assess conformational equilibria of the activation loop and the effect of small molecule inhibitors in the MAP kinase p38α. Our work experimentally revealed the existence of a two-state equilibrium for p38α while the addition of inhibitors shifts the equilibrium between these two states.</dcterms:abstract> </rdf:Description> </rdf:RDF>
Interner Vermerk
xmlui.Submission.submit.DescribeStep.inputForms.label.kops_note_fromSubmitter
Prüfungsdatum der Dissertation
Finanzierungsart
Kommentar zur Publikation
Allianzlizenz
Corresponding Authors der Uni Konstanz vorhanden
Internationale Co-Autor:innen
Universitätsbibliographie
Ja
Begutachtet
Ja