About: Changes in the intrinsic electrocatalytic nature of Na /K ATPase reflect structural changes on ATP-binding: Electrochemical label-free approach

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About: Changes in the intrinsic electrocatalytic nature of Na /K ATPase reflect structural changes on ATP-binding: Electrochemical label-free approach Goto Sponge NotDistinct Permalink

An Entity of Type : http://linked.opendata.cz/ontology/domain/vavai/Vysledek, within Data Space : linked.opendata.cz associated with source document(s)

Attributes	Values
rdf:type	skos:Concept http://linked.opendata.cz/ontology/domain/vavai/Vysledek
rdfs:seeAlso	http://www.sciencedirect.com/science/article/pii/S1388248112005024
Description	Chronopotentiometric stripping (CPS) analysis was used to show that transmembrane protein Na+/K+-ATPase (NKA) structural changes can be observed in the presence of ATP. The ATP-induced structural changes lead to modulation of NKA ability to catalyze the hydrogen evolution on Hg-electrode. The electrochemical data on NKA are compared to monitoring of changes in intrinsic fluorescence and discussed with respect to crystallographic structures of homologous sarco/endoplasmic reticulum Ca2+-ATPase (SERCA). The results show that CPS analysis of intrinsic electroactivity (label-free approach) could be applied for monitoring of structural changes and molecular interactions of membrane proteins, such as NKA. Chronopotentiometric stripping (CPS) analysis was used to show that transmembrane protein Na+/K+-ATPase (NKA) structural changes can be observed in the presence of ATP. The ATP-induced structural changes lead to modulation of NKA ability to catalyze the hydrogen evolution on Hg-electrode. The electrochemical data on NKA are compared to monitoring of changes in intrinsic fluorescence and discussed with respect to crystallographic structures of homologous sarco/endoplasmic reticulum Ca2+-ATPase (SERCA). The results show that CPS analysis of intrinsic electroactivity (label-free approach) could be applied for monitoring of structural changes and molecular interactions of membrane proteins, such as NKA. (en)
Title	Changes in the intrinsic electrocatalytic nature of Na /K ATPase reflect structural changes on ATP-binding: Electrochemical label-free approach Changes in the intrinsic electrocatalytic nature of Na /K ATPase reflect structural changes on ATP-binding: Electrochemical label-free approach (en)
skos:prefLabel	Changes in the intrinsic electrocatalytic nature of Na /K ATPase reflect structural changes on ATP-binding: Electrochemical label-free approach Changes in the intrinsic electrocatalytic nature of Na /K ATPase reflect structural changes on ATP-binding: Electrochemical label-free approach (en)
skos:notation	RIV/61989592:15310/13:33143456!RIV14-MZ0-15310___
http://linked.open...avai/predkladatel	Přírodovědecká fakulta
http://linked.open...avai/riv/aktivita	P
http://linked.open...avai/riv/aktivity	P(GD303/09/H048), P(NT11071)
http://linked.open...iv/cisloPeriodika	FEB
http://linked.open...vai/riv/dodaniDat	2014
http://linked.open...aciTvurceVysledku	Kubala, Martin Janovská, Marika
http://linked.open.../riv/druhVysledku	J - Článek v odborném periodiku
http://linked.open...iv/duvernostUdaju	S - Úplné a pravdivé údaje nepodléhající ochraně podle zvláštních právních předpisů
http://linked.open...titaPredkladatele	Univerzita Palackého v Olomouci / Přírodovědecká fakulta
http://linked.open...dnocenehoVysledku	64942
http://linked.open...ai/riv/idVysledku	RIV/61989592:15310/13:33143456
http://linked.open...riv/jazykVysledku	eng - angličtina
http://linked.open.../riv/klicovaSlova	Structural changes; Sodium-potassium pum; Membrane protein; Mercury electrode; Chronopotentiometry; Electroanalysis (en)
http://linked.open.../riv/klicoveSlovo	Mercury electrode Chronopotentiometry Sodium-potassium pum Structural changes Membrane protein Electroanalysis
http://linked.open...odStatuVydavatele	US - Spojené státy americké
http://linked.open...ontrolniKodProRIV	[C4740016F2EC]
http://linked.open...i/riv/nazevZdroje	Electrochemistry Communications
http://linked.open...in/vavai/riv/obor	CG
http://linked.open...ichTvurcuVysledku	2 (xsd:int)
http://linked.open...cetTvurcuVysledku	5 (xsd:int)
http://linked.open...vavai/riv/projekt	Molecular mechanisms of selected pathological processes in the cell Interaction of cisplatin with the Na+/K+-ATPase
http://linked.open...UplatneniVysledku	2013
http://linked.open...v/svazekPeriodika	27
http://linked.open...iv/tvurceVysledku	Ulrichová, Jitka Vacek, Jan Kubala, Martin Zatloukalová, Martina Havlíková, Marika
issn	1388-2481
number of pages	4 (xsd:int)
http://localhost/t...ganizacniJednotka	15310

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