About: Activation of protein phosphatase 1 by a selective phosphatase disrupting peptide reduces sarcoplasmic reticulum Ca leak in human heart failure

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About: Activation of protein phosphatase 1 by a selective phosphatase disrupting peptide reduces sarcoplasmic reticulum Ca leak in human heart failure Goto Sponge NotDistinct Permalink

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scientific article published on 07 September 2018

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description	wetenschappelijk artikel (nl) наукова стаття, опублікована у вересні 2018 (uk) article scientifique publié en 2018 (fr) im September 2018 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu en setiembre de 2018 (ast) scientific article published on 07 September 2018 (en)
publication date	wds:Q57159563-E8484FF7-AD42-4A04-96CA-AE6B1BB4DE6A
publication date	2018-09-07 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57159563-96E9EDF2-7799-4A50-8716-629874AB02F0
language of work or name	English
cites work	wds:Q57159563-033C731A-9A1B-4AD5-A611-5D45A2A9D44F wds:Q57159563-0BAA7D93-7778-4469-9658-3D44BA7D7A3E wds:Q57159563-113827CE-2C87-4DAB-927E-89958B08AB78 wds:Q57159563-15C6B5F9-6CCF-4428-AF70-6BF471B927F8 wds:Q57159563-19930FA0-BADD-43D3-97C2-5546B627EAAF wds:Q57159563-257F541E-DEC5-470E-9FFF-3F09EC73D94C wds:Q57159563-2AD909A8-8214-42FD-8209-B72222DB83DF wds:Q57159563-2B19D702-6894-49CD-81F7-42C515B593F3 wds:Q57159563-2BF2A680-AAFE-4EA7-B68C-0F870FE9E345 wds:Q57159563-3C53271C-A0A6-4423-A68A-D347F8028286 wds:Q57159563-49A616E1-E69B-4841-B4DA-764A96A08295 wds:Q57159563-57DD7BF7-979D-4A4A-8301-1CA379402ABB wds:Q57159563-631698D4-3BF8-42E8-A031-B28A8D8E27B6 wds:Q57159563-7109774D-E99C-422F-BFAE-6F00821A8934 wds:Q57159563-7795B728-DB00-47F1-8228-DD1FFDD49A96 wds:Q57159563-7FD298B5-20C6-4750-8419-243384E548AC wds:Q57159563-813F1893-935A-4800-9B8E-F876D5BACB7C wds:Q57159563-8728DFC2-E5F8-4A9E-9CFB-DC1987F8DFAE wds:Q57159563-87BCC6A0-89BF-4A21-9BFF-4BE928147F41 wds:Q57159563-87EA8D27-5EC1-4DD5-AA4B-E58A1CBCA034 wds:Q57159563-8EEB43BD-4014-4816-B46D-2E4A1E8A4E0F wds:Q57159563-A3453411-CA02-450E-8E39-38846BC6B781 wds:Q57159563-A8033FA1-0271-4C20-85F5-81539A5CE076 wds:Q57159563-AE29D687-DA48-47A3-B41F-6BB60FBA7DBA wds:Q57159563-AE8E4694-6878-49ED-8E77-78F222786092 wds:Q57159563-B4BDE6C3-2C4B-4D47-8A9A-178E95AEF391 wds:Q57159563-C0158755-F96E-420E-A050-92496A0B0729 wds:Q57159563-E4E782CA-07A8-4DC3-85C9-C634454514E9 wds:Q57159563-EA0A1524-7708-42A5-A43C-812CD6DC3133 wds:Q57159563-EA8F65E7-C319-454D-AC39-B5307E85BCC1 wds:Q57159563-EAF55135-74B6-4FAB-90C4-D7ED898082AF
cites work	Transgenic CaMKIIdeltaC overexpression uniquely alters cardiac myocyte Ca2+ handling: reduced SR Ca2+ load and activated SR Ca2+ release Turning enzymes ON with small molecules Inhibition of elevated Ca2+/calmodulin-dependent protein kinase II improves contractility in human failing myocardium beta-adrenergic receptor blockers restore cardiac calcium release channel (ryanodine receptor) structure and function in heart failure Ca2+/calmodulin-dependent protein kinase II and protein kinase A differentially regulate sarcoplasmic reticulum Ca2+ leak in human cardiac pathology. Calcium/calmodulin-dependent protein kinase II contributes to cardiac arrhythmogenesis in heart failure Enhancement of cardiac function and suppression of heart failure progression by inhibition of protein phosphatase 1 Decreased protein and phosphorylation level of the protein phosphatase inhibitor-1 in failing human hearts Regional expression of protein phosphatase type 1 and 2A catalytic subunit isoforms in the human heart Identification of the major protein phosphatases in mammalian cardiac muscle which dephosphorylate phospholamban Effects of a protein phosphatase inhibitor, okadaic acid, on membrane currents of isolated guinea-pig cardiac myocytes Reduced level of serine(16) phosphorylated phospholamban in the failing rat myocardium: a major contributor to reduced SERCA2 activity Targeting the untargetable: recent advances in the selective chemical modulation of protein phosphatase-1 activity. The ryanodine receptor provides high throughput Ca2+-release but is precisely regulated by networks of associated proteins: a focus on proteins relevant to phosphorylation. Physiology and pathophysiology of excitation-contraction coupling: the functional role of ryanodine receptor. Ca(2+) /calmodulin-dependent protein kinase II equally induces sarcoplasmic reticulum Ca(2+) leak in human ischaemic and dilated cardiomyopathy. Role of PP1 in the regulation of Ca cycling in cardiac physiology and pathophysiology Evidence for protein phosphatase inhibitor-1 playing an amplifier role in beta-adrenergic signaling in cardiac myocytes Protein phosphatase 2A affects myofilament contractility in non-failing but not in failing human myocardium Phosphatase inhibitor-1-deficient mice are protected from catecholamine-induced arrhythmias and myocardial hypertrophy Increased expression of cardiac phosphatases in patients with end-stage heart failure The PP1 binding code: a molecular-lego strategy that governs specificity Protein phosphatase 2A regulatory subunit B56α limits phosphatase activity in the heart Protein phosphatases decrease sarcoplasmic reticulum calcium content by stimulating calcium release in cardiac myocytes Development of a Peptide that Selectively Activates Protein Phosphatase-1 in Living Cells Regulation of ryanodine receptors via macromolecular complexes: a novel role for leucine/isoleucine zippers Cardiac-specific deletion of protein phosphatase 1β promotes increased myofilament protein phosphorylation and contractile alterations Impaired local regulation of ryanodine receptor type 2 by protein phosphatase 1 promotes atrial fibrillation. Metals in the active site of native protein phosphatase-1 Approaches to Study Phosphatases Miklós Bodanszky Award Lecture: Advances in the selective targeting of protein phosphatase-1 and phosphatase-2A with peptides
author name string	wds:Q57159563-0341295E-FA12-4532-A705-0FC3DB63624C wds:Q57159563-17B7FAAD-2C77-46BD-BB21-7E40147188B3 wds:Q57159563-21F34BC3-2DF2-4E26-8966-A01DCE38B642 wds:Q57159563-26B4DFD2-0D8A-4B5F-9A8F-A46FA6E69692 wds:Q57159563-29E0AE1A-69DC-4C14-BB58-5E898B0CA35E wds:Q57159563-36534C97-62BC-44F4-BF2A-60E6992709F5 wds:Q57159563-40ED8E4F-C4C1-4AE3-B765-B6E3F3AAA806 wds:Q57159563-4E85590A-409B-4134-AAA9-9445DB050D5F wds:Q57159563-4EC49446-C1E0-41B7-81A9-DF62A3A74C69 wds:Q57159563-4F73EB00-2CAC-437B-BAB9-7A7D006D73E0 wds:Q57159563-54DA86D2-8EC3-40EC-B4A4-FED313EDC8E5 wds:Q57159563-B9E75CEC-7160-4FEA-A4D9-825BAA18A2BC wds:Q57159563-E26D66FD-A1E5-4314-AC52-A83C738BA09B wds:Q57159563-EB5F1B03-E2B6-4015-BD8D-80E06CCF55EA
author name string	Lars S Maier Gerd Hasenfuß Ali El-Armouche Jan Gummert Thomas H Fischer Yansong Wang Samuel Sossalla Nataliya Dybkova Silvio Weber Theodor Tirilomis Steffen Pabel André Renner Jörg Eiringhaus

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