Zobrazeno 1 - 10
of 14
pro vyhledávání: '"Meike Kuschel"'
Publikováno v:
JALA: Journal of the Association for Laboratory Automation. 10:319-326
Microfluidic technology applied to on-chip electrophoresis provides high-throughput DNA or protein analysis in an automated, unattended mode, which is currently not possible with any other technology. The 5100 Automated Lab-on-a-Chip Platform automat
Sinoatrial Node Pacemaker Activity Requires Ca 2+ /Calmodulin-Dependent Protein Kinase II Activation
Autor:
Rui-Ping Xiao, Meike Kuschel, Tatiana M. Vinogradova, Ying-Ying Zhou, Konstantin Y. Bogdanov, Heping Cheng, Dongmei Yang
Publikováno v:
Circulation Research. 87:760-767
Abstract —Cardiac beating arises from the spontaneous rhythmic excitation of sinoatrial (SA) node cells. Here we report that SA node pacemaker activity is critically dependent on Ca 2+ /calmodulin-dependent protein kinase II (CaMKII). In freshly di
Autor:
Ying Ying Zhou, Peter Karczewski, Sheng Jun Zhang, Sabine Bartel, Meike Kuschel, Harold A. Spurgeon, Edward G. Lakatta, Ernst-Georg Krause, Rui-Ping Xiao
Publikováno v:
Circulation. 99:2458-2465
Background —Recent studies of β-adrenergic receptor (β-AR) subtype signaling in in vitro preparations have raised doubts as to whether the cAMP/protein kinase A (PKA) signaling is activated in the same manner in response to β 2 -AR versus β 1 -
Autor:
Sabine Bartel, Peter Karczewski, Wolfgang-Peter Schlegel, Petra Hempel, Meike Kuschel, Ernst-Georg Krause
Publikováno v:
American Journal of Physiology-Heart and Circulatory Physiology. 276:H1625-H1633
Phospholamban is a critical regulator of sarcoplasmic reticulum Ca2+-ATPase and myocardial contractility. To determine the extent of cross signaling between Ca2+and cAMP pathways, we have investigated the β-adrenergic-induced phosphorylation of Ser1
Publikováno v:
Basic Research in Cardiology. 92:37-43
Phospholamban (PLB), the regulator of the cardiac sarcoplasmic reticulum (SR) Ca2+ pump is specifically phosphorylated at Ser16 and Thr17 by cAMP-dependent protein kinase (PKA) and Ca2+/calmodulin-dependent protein kinase (CaMK), respectively. The re
Autor:
Louise Sanders, Meike Kuschel, James A. Lynham, Ernst-Georg Krause, Peter Karczewski, Alberto J. Kaumann, Sabine Bartel
Publikováno v:
Molecular and Cellular Biochemistry. :113-123
Evidence from ventricular preparations of cat, sheep, rat and dog suggests that both beta 1-adrenoceptors (beta 1AR) and beta 2-adrenoceptors (beta 2AR) mediate positive inotropic effects but that only beta 1AR do it through activation of a cAMP path
Publikováno v:
Journal of biomolecular techniques : JBT. 13(3)
The performance of the Agilent 2100 bioanalyzer, the first commercial lab-on-a-chip system, and the Protein 200 Plus LabChip kit is compared with conventional protein analysis techniques such as SDS-PAGE, Lowry, or Bradford. Lab-on-a-chip technology
Publikováno v:
ESACT Proceedings ISBN: 1402027915
A universal task involved in protein characterization is purification, quantitation and identification. For example, protein quantitation is required to calculate and monitor the protein yield after various enrichment or purification processes as wel
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::eca90e0cd09a07cada98906ca3b79b65
https://doi.org/10.1007/1-4020-3103-3_78
https://doi.org/10.1007/1-4020-3103-3_78
Autor:
Ye Chen-Izu, Meike Kuschel, Harold A. Spurgeon, Leighton T. Izu, Heping Cheng, Edward G. Lakatta, Rui-Ping Xiao
A plausible determinant of the specificity of receptor signaling is the cellular compartment over which the signal is broadcast. In rat heart, stimulation of beta(1)-adrenergic receptor (beta(1)-AR), coupled to G(s)-protein, or beta(2)-AR, coupled to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::eefef97dd9f860f75125a1955df35d46
https://europepmc.org/articles/PMC1301137/
https://europepmc.org/articles/PMC1301137/
Publikováno v:
The Journal of biological chemistry. 275(29)
Both Ser(16) and Thr(17) of phospholamban (PLB) are phosphorylated, respectively, by cAMP-dependent protein kinase (PKA) and Ca(2+)/calmodulin-dependent protein kinase II (CaMKII). PLB phosphorylation relieves cardiac sarcoplasmic reticulum Ca(2+) pu