Lehnart, Stephan Elmar

[["dc.bibliographiccitation.firstpage","829"],["dc.bibliographiccitation.issue","7"],["dc.bibliographiccitation.journal","Cell"],["dc.bibliographiccitation.lastpage","840"],["dc.bibliographiccitation.volume","113"],["dc.contributor.author","Wehrens, Xander H. T."],["dc.contributor.author","Lehnart, Stephan E."],["dc.contributor.author","Huang, Fannie"],["dc.contributor.author","Vest, John A."],["dc.contributor.author","Reiken, Steven R."],["dc.contributor.author","Mohler, Peter J."],["dc.contributor.author","Sun, Jie"],["dc.contributor.author","Guatimosim, Silvia"],["dc.contributor.author","Song, Long-Sheng"],["dc.contributor.author","Rosemblit, Nora"],["dc.contributor.author","Marks, Andrew R."],["dc.date.accessioned","2022-03-01T11:45:29Z"],["dc.date.available","2022-03-01T11:45:29Z"],["dc.date.issued","2003"],["dc.description.abstract","Arrhythmias, a common cause of sudden cardiac death, can occur in structurally normal hearts, although the mechanism is not known. In cardiac muscle, the ryanodine receptor (RyR2) on the sarcoplasmic reticulum releases the calcium required for muscle contraction. The FK506 binding protein (FKBP12.6) stabilizes RyR2, preventing aberrant activation of the channel during the resting phase of the cardiac cycle. We show that during exercise, RyR2 phosphorylation by cAMP-dependent protein kinase A (PKA) partially dissociates FKBP12.6 from the channel, increasing intracellular Ca2+ release and cardiac contractility. FKBP12.6−/− mice consistently exhibited exercise-induced cardiac ventricular arrhythmias that cause sudden cardiac death. Mutations in RyR2 linked to exercise-induced arrhythmias (in patients with catecholaminergic polymorphic ventricular tachycardia [CPVT]) reduced the affinity of FKBP12.6 for RyR2 and increased single-channel activity under conditions that simulate exercise. These data suggest that “leaky” RyR2 channels can trigger fatal cardiac arrhythmias, providing a possible explanation for CPVT."],["dc.identifier.doi","10.1016/S0092-8674(03)00434-3"],["dc.identifier.gro","3142431"],["dc.identifier.pii","S0092867403004343"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/103347"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.notes.status","final"],["dc.relation.issn","0092-8674"],["dc.title","FKBP12.6 Deficiency and Defective Calcium Release Channel (Ryanodine Receptor) Function Linked to Exercise-Induced Sudden Cardiac Death"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","919"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","The Journal of Cell Biology"],["dc.bibliographiccitation.lastpage","928"],["dc.bibliographiccitation.volume","160"],["dc.contributor.author","Reiken, Steven"],["dc.contributor.author","Lacampagne, Alain"],["dc.contributor.author","Zhou, Hua"],["dc.contributor.author","Kherani, Aftab"],["dc.contributor.author","Lehnart, Stephan Elmar"],["dc.contributor.author","Ward, Chris"],["dc.contributor.author","Huang, Fannie"],["dc.contributor.author","Gaburjakova, Marta"],["dc.contributor.author","Gaburjakova, Jana"],["dc.contributor.author","Rosemblit, Nora"],["dc.contributor.author","Warren, Michelle S."],["dc.contributor.author","He, Kun-lun"],["dc.contributor.author","Yi, Geng-hua"],["dc.contributor.author","Wang, Jie"],["dc.contributor.author","Burkhoff, Daniel"],["dc.contributor.author","Vassort, Guy"],["dc.contributor.author","Marks, Andrew R."],["dc.date.accessioned","2018-04-23T11:48:49Z"],["dc.date.available","2018-04-23T11:48:49Z"],["dc.date.issued","2003"],["dc.description.abstract","The type 1 ryanodine receptor (RyR1) on the sarcoplasmic reticulum (SR) is the major calcium (Ca2+) release channel required for skeletal muscle excitation–contraction (EC) coupling. RyR1 function is modulated by proteins that bind to its large cytoplasmic scaffold domain, including the FK506 binding protein (FKBP12) and PKA. PKA is activated during sympathetic nervous system (SNS) stimulation. We show that PKA phosphorylation of RyR1 at Ser2843 activates the channel by releasing FKBP12. When FKB12 is bound to RyR1, it inhibits the channel by stabilizing its closed state. RyR1 in skeletal muscle from animals with heart failure (HF), a chronic hyperadrenergic state, were PKA hyperphosphorylated, depleted of FKBP12, and exhibited increased activity, suggesting that the channels are “leaky.” RyR1 PKA hyperphosphorylation correlated with impaired SR Ca2+ release and early fatigue in HF skeletal muscle. These findings identify a novel mechanism that regulates RyR1 function via PKA phosphorylation in response to SNS stimulation. PKA hyperphosphorylation of RyR1 may contribute to impaired skeletal muscle function in HF, suggesting that a generalized EC coupling myopathy may play a role in HF."],["dc.identifier.doi","10.1083/jcb.200211012"],["dc.identifier.gro","3142432"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13578"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0021-9525"],["dc.title","PKA phosphorylation activates the calcium release channel (ryanodine receptor) in skeletal muscle: defective regulation in heart failure"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2325"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Circulation"],["dc.bibliographiccitation.lastpage","2345"],["dc.bibliographiccitation.volume","116"],["dc.contributor.author","Lehnart, Stephan Elmar"],["dc.contributor.author","Ackerman, Michael J."],["dc.contributor.author","Benson, D. Woodrow"],["dc.contributor.author","Brugada, Ramon"],["dc.contributor.author","Clancy, Colleen"],["dc.contributor.author","Donahue, J. Kevin"],["dc.contributor.author","George, Alfred L."],["dc.contributor.author","Grant, Augustus O."],["dc.contributor.author","Groft, Stephen C."],["dc.contributor.author","January, Craig T."],["dc.contributor.author","Lathrop, David A."],["dc.contributor.author","Lederer, W. Jonathan"],["dc.contributor.author","Makielski, Jonathan C."],["dc.contributor.author","Mohler, Peter J."],["dc.contributor.author","Moss, Arthur"],["dc.contributor.author","Nerbonne, Jeanne M."],["dc.contributor.author","Olson, Timothy M."],["dc.contributor.author","Przywara, Dennis A."],["dc.contributor.author","Towbin, Jeffrey A."],["dc.contributor.author","Wang, Lan-Hsiang"],["dc.contributor.author","Marks, Andrew R."],["dc.date.accessioned","2018-05-09T14:00:10Z"],["dc.date.available","2018-05-09T14:00:10Z"],["dc.date.issued","2007"],["dc.description.abstract","The National Heart, Lung, and Blood Institute and Office of Rare Diseases at the National Institutes of Health organized a workshop (September 14 to 15, 2006, in Bethesda, Md) to advise on new research directions needed for improved identification and treatment of rare inherited arrhythmias. These included the following: (1) Na+ channelopathies; (2) arrhythmias due to K+ channel mutations; and (3) arrhythmias due to other inherited arrhythmogenic mechanisms. Another major goal was to provide recommendations to support, enable, or facilitate research to improve future diagnosis and management of inherited arrhythmias. Classifications of electric heart diseases have proved to be exceedingly complex and in many respects contradictory. A new contemporary and rigorous classification of arrhythmogenic cardiomyopathies is proposed. This consensus report provides an important framework and overview to this increasingly heterogeneous group of primary cardiac membrane channel diseases. Of particular note, the present classification scheme recognizes the rapid evolution of molecular biology and novel therapeutic approaches in cardiology, as well as the introduction of many recently described diseases, and is unique in that it incorporates ion channelopathies as a primary cardiomyopathy in consensus with a recent American Heart Association Scientific Statement."],["dc.identifier.gro","3142414"],["dc.identifier.pmid","17998470"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13558"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.doi","10.1161/CIRCULATIONAHA.107.711689"],["dc.relation.eissn","1524-4539"],["dc.relation.issn","1524-4539"],["dc.relation.issn","0009-7322"],["dc.title","Inherited arrhythmias: a National Heart, Lung, and Blood Institute and Office of Rare Diseases workshop consensus report about the diagnosis, phenotyping, molecular mechanisms, and therapeutic approaches for primary cardiomyopathies of gene mutations affecting ion channel function"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","7906"],["dc.bibliographiccitation.issue","20"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences"],["dc.bibliographiccitation.lastpage","7910"],["dc.bibliographiccitation.volume","103"],["dc.contributor.author","Lehnart, Stephan Elmar"],["dc.contributor.author","Terrenoire, Cecile"],["dc.contributor.author","Reiken, Steven"],["dc.contributor.author","Wehrens, Xander H. T."],["dc.contributor.author","Song, Long-Sheng"],["dc.contributor.author","Tillman, Erik J."],["dc.contributor.author","Mancarella, Salvatore"],["dc.contributor.author","Coromilas, James"],["dc.contributor.author","Lederer, W. J."],["dc.contributor.author","Kass, Robert S."],["dc.contributor.author","Marks, Andrew R."],["dc.date.accessioned","2018-04-23T11:48:42Z"],["dc.date.available","2018-04-23T11:48:42Z"],["dc.date.issued","2006"],["dc.description.abstract","Catecholaminergic polymorphic ventricular tachycardia is a form of exercise-induced sudden cardiac death that has been linked to mutations in the cardiac Ca2+ release channel/ryanodine receptor (RyR2) located on the sarcoplasmic reticulum (SR). We have shown that catecholaminergic polymorphic ventricular tachycardia-linked RyR2 mutations significantly decrease the binding affinity for calstabin-2 (FKBP12.6), a subunit that stabilizes the closed state of the channel. We have proposed that RyR2-mediated diastolic SR Ca2+ leak triggers ventricular tachycardia (VT) and sudden cardiac death. In calstabin-2-deficient mice, we have now documented diastolic SR Ca2+ leak, monophasic action potential alternans, and bidirectional VT. Calstabin-deficient cardiomyocytes exhibited SR Ca2+ leak-induced aberrant transient inward currents in diastole consistent with delayed after-depolarizations. The 1,4-benzothiazepine JTV519, which increases the binding affinity of calstabin-2 for RyR2, inhibited the diastolic SR Ca2+ leak, monophasic action potential alternans and triggered arrhythmias. Our data suggest that calstabin-2 deficiency is as a critical mediator of triggers that initiate cardiac arrhythmias."],["dc.identifier.doi","10.1073/pnas.0602133103"],["dc.identifier.gro","3142418"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13562"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0027-8424"],["dc.title","Stabilization of cardiac ryanodine receptor prevents intracellular calcium leak and arrhythmias"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","366"],["dc.bibliographiccitation.issue","1"],["dc.bibliographiccitation.journal","Annals of the New York Academy of Sciences"],["dc.bibliographiccitation.lastpage","375"],["dc.bibliographiccitation.volume","1047"],["dc.contributor.author","Wehrens, Xander H.T."],["dc.contributor.author","Lehnart, Stephan Elmar"],["dc.contributor.author","Marks, Andrew R."],["dc.date.accessioned","2018-04-23T11:48:47Z"],["dc.date.available","2018-04-23T11:48:47Z"],["dc.date.issued","2005"],["dc.description.abstract","Cardiac arrhythmia is an important cause of death in patients with heart failure (HF) and inherited arrhythmia syndromes, such as catecholaminergic polymorphic ventricular tachycardia (CPVT). Alterations in intracellular calcium handling play a prominent role in the generation of arrhythmias in the failing heart. Diastolic calcium leak from the sarcoplasmic reticulum (SR) via cardiac ryanodine receptors (RyR2) may initiate delayed afterdepolarizations and triggered activity leading to arrhythmias. Similarly, SR Ca2+ leak through mutant RyR2 channels may cause triggered activity during exercise in patients with CPVT. Novel therapeutic approaches, based on recent advances in the understanding of the cellular mechanisms underlying arrhythmias in HF and CPVT, are currently being evaluated to specifically correct defective Ca2+ release in these lethal syndromes."],["dc.identifier.doi","10.1196/annals.1341.032"],["dc.identifier.gro","3142423"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13568"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","0077-8923"],["dc.title","Ryanodine Receptor-Targeted Anti-Arrhythmic Therapy"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","677"],["dc.bibliographiccitation.issue","5"],["dc.bibliographiccitation.journal","Expert Opinion on Therapeutic Targets"],["dc.bibliographiccitation.lastpage","688"],["dc.bibliographiccitation.volume","10"],["dc.contributor.author","Lehnart, Stephan Elmar"],["dc.contributor.author","Marks, Andrew R."],["dc.date.accessioned","2018-04-23T11:48:42Z"],["dc.date.available","2018-04-23T11:48:42Z"],["dc.date.issued","2006"],["dc.description.abstract","Stimulation of several G-protein-coupled receptors (GPCRs) promotes intracellular production of cyclic adenosine 3′,5′-monophosphate (cAMP) and subsequently activates protein kinase A (PKA). In the heart, β-adrenergic receptor (β-AR) stimulation increases contractile performance and heart rate as part of the ‘fight-or-flight’ stress response. Molecular organisation of PKA-effector association occurs by A kinase anchoring proteins (AKAPs), which target kinase action to specific intracellular sites. Some AKAPs interact directly with specific cAMP-hydrolysing phosphodiesterase (PDE) isoforms allowing for the assembly of multi-protein complexes that create focal points of intracellular cAMP signalling. Certain PDE isoforms co-localise with PKA as part of negative feedback mechanisms which may protect from excess β-AR stimulation of Ca2+ transporters during cardiac excitation–contraction coupling. Pharmacological PDE inhibition increases intracellular cAMP concentrations and augments excitation–contraction coupling in heart failure. However, chronic PDE inhibitor treatment causes severe cardiac side effects and increases mortality. Moreover, cAMP hydrolysing PDE activity was found decreased in heart failure which may contribute to disease progression via chronic PKA-dependent dysregulation of Ca2+ transport proteins. The authors review the contribution of PDE activity in the heart to contractile stress adaptation, the significance of altered cAMP signalling in heart failure, and the effects of PDE inhibition in heart disease."],["dc.identifier.doi","10.1517/14728222.10.5.677"],["dc.identifier.gro","3142417"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13561"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","final"],["dc.relation.issn","1472-8222"],["dc.title","Phosphodiesterase 4D and heart failure: a cautionary tale"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","2198"],["dc.bibliographiccitation.issue","6"],["dc.bibliographiccitation.journal","Proceedings of the National Academy of Sciences of the United States of America"],["dc.bibliographiccitation.lastpage","2202"],["dc.bibliographiccitation.volume","105"],["dc.contributor.author","Bellinger, Andrew M."],["dc.contributor.author","Reiken, Steven"],["dc.contributor.author","Dura, Miroslav"],["dc.contributor.author","Murphy, Peter W"],["dc.contributor.author","Deng, Shi-Xian"],["dc.contributor.author","Landry, Donald W."],["dc.contributor.author","Nieman, David"],["dc.contributor.author","Lehnart, Stephan Elmar"],["dc.contributor.author","Samaru, Mahendranauth"],["dc.contributor.author","LaCampagne, Alain"],["dc.contributor.author","Marks, Andrew R."],["dc.date.accessioned","2018-05-09T12:57:35Z"],["dc.date.available","2018-05-09T12:57:35Z"],["dc.date.issued","2008"],["dc.description.abstract","During exercise, defects in calcium (Ca2+) release have been proposed to impair muscle function. Here, we show that during exercise in mice and humans, the major Ca2+ release channel required for excitation-contraction coupling (ECC) in skeletal muscle, the ryanodine receptor (RyR1), is progressively PKA-hyperphosphorylated, S-nitrosylated, and depleted of the phosphodiesterase PDE4D3 and the RyR1 stabilizing subunit calstabin1 (FKBP12), resulting in \"leaky\" channels that cause decreased exercise tolerance in mice. Mice with skeletal muscle-specific calstabin1 deletion or PDE4D deficiency exhibited significantly impaired exercise capacity. A small molecule (S107) that prevents depletion of calstabin1 from the RyR1 complex improved force generation and exercise capacity, reduced Ca2+-dependent neutral protease calpain activity and plasma creatine kinase levels. Taken together, these data suggest a possible mechanism by which Ca2+ leak via calstabin1-depleted RyR1 channels leads to defective Ca2+ signaling, muscle damage, and impaired exercise capacity."],["dc.identifier.doi","10.1073/pnas.0711074105"],["dc.identifier.gro","3142413"],["dc.identifier.pmid","18268335"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/13557"],["dc.language.iso","en"],["dc.notes.intern","lifescience updates Crossref Import"],["dc.notes.status","zu prüfen"],["dc.relation.doi","10.1073/pnas.0711074105"],["dc.relation.eissn","1091-6490"],["dc.relation.issn","0027-8424"],["dc.title","Remodeling of ryanodine receptor complex causes leaky channels: a molecular mechanism for decreased exercise capacity"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dc.type.peerReviewed","no"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","4388"],["dc.bibliographiccitation.issue","12"],["dc.bibliographiccitation.journal","Journal of Clinical Investigation"],["dc.bibliographiccitation.lastpage","4398"],["dc.bibliographiccitation.volume","120"],["dc.contributor.author","Shan, Jian"],["dc.contributor.author","Kushnir, Alexander"],["dc.contributor.author","Betzenhauser, Matthew J."],["dc.contributor.author","Reiken, Steven"],["dc.contributor.author","Li, Jingdong"],["dc.contributor.author","Lindegger, Nicolas"],["dc.contributor.author","Mongillo, Marco"],["dc.contributor.author","Mohler, Peter J."],["dc.contributor.author","Marks, Andrew R."],["dc.contributor.author","Lehnart, Stephan E."],["dc.date.accessioned","2021-11-22T14:31:51Z"],["dc.date.available","2021-11-22T14:31:51Z"],["dc.date.issued","2010"],["dc.description.abstract","During the classic “fight-or-flight” stress response, sympathetic nervous system activation leads to catecholamine release, which increases heart rate and contractility, resulting in enhanced cardiac output. Catecholamines bind to β-adrenergic receptors, causing cAMP generation and activation of PKA, which phosphorylates multiple targets in cardiac muscle, including the cardiac ryanodine receptor/calcium release channel (RyR2) required for muscle contraction. PKA phosphorylation of RyR2 enhances channel activity by sensitizing the channel to cytosolic calcium (Ca2+). Here, we found that mice harboring RyR2 channels that cannot be PKA phosphorylated (referred to herein as RyR2-S2808A+/+ mice) exhibited blunted heart rate and cardiac contractile responses to catecholamines (isoproterenol). The isoproterenol-induced enhancement of ventricular myocyte Ca2+ transients and fractional shortening (contraction) and the spontaneous beating rate of sinoatrial nodal cells were all blunted in RyR2-S2808A+/+ mice. The blunted cardiac response to catecholamines in RyR2-S2808A+/+ mice resulted in impaired exercise capacity. RyR2-S2808A+/+ mice were protected against chronic catecholaminergic-induced cardiac dysfunction. These studies identify what we believe to be new roles for PKA phosphorylation of RyR2 in both the heart rate and contractile responses to acute catecholaminergic stimulation."],["dc.identifier.doi","10.1172/JCI32726"],["dc.identifier.fs","576355"],["dc.identifier.gro","3142407"],["dc.identifier.purl","https://resolver.sub.uni-goettingen.de/purl?gs-1/7564"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/93408"],["dc.language.iso","en"],["dc.notes.intern","Migrated from goescholar"],["dc.notes.status","final"],["dc.relation.doi","10.1172/JCI32726"],["dc.relation.eissn","1558-8238"],["dc.relation.issn","0021-9738"],["dc.relation.issn","1558-8238"],["dc.rights.access","openAccess"],["dc.subject","fight-or-flight stress response; β-AR stimulation"],["dc.title","Phosphorylation of the ryanodine receptor mediates the cardiac fight or flight response in mice"],["dc.type","journal_article"],["dc.type.internalPublication","yes"],["dc.type.peerReviewed","yes"],["dc.type.version","published_version"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","746"],["dc.bibliographiccitation.issue","8"],["dc.bibliographiccitation.journal","Circulation Research"],["dc.bibliographiccitation.lastpage","749"],["dc.bibliographiccitation.volume","101"],["dc.contributor.author","Lehnart, Stephan Elmar"],["dc.contributor.author","Marks, Andrew R."],["dc.date.accessioned","2018-05-09T13:36:41Z"],["dc.date.available","2018-05-09T13:36:41Z"],["dc.date.issued","2007"],["dc.identifier.doi","10.1161/CIRCRESAHA.107.162479"],["dc.identifier.pmid","17932330"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/14650"],["dc.language.iso","en"],["dc.notes.status","final"],["dc.relation.doi","10.1161/CIRCRESAHA.107.162479"],["dc.relation.eissn","1524-4571"],["dc.relation.issn","1524-4571"],["dc.title","Regulation of ryanodine receptors in the heart"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]

[["dc.bibliographiccitation.firstpage","3342"],["dc.bibliographiccitation.issue","25"],["dc.bibliographiccitation.journal","Circulation"],["dc.bibliographiccitation.lastpage","3346"],["dc.bibliographiccitation.volume","111"],["dc.contributor.author","Lehnart, Stephan E."],["dc.contributor.author","Wehrens, Xander H.T."],["dc.contributor.author","Marks, Andrew R."],["dc.date.accessioned","2022-03-01T11:43:51Z"],["dc.date.available","2022-03-01T11:43:51Z"],["dc.date.issued","2005"],["dc.identifier.doi","10.1161/CIRCULATIONAHA.105.551861"],["dc.identifier.uri","https://resolver.sub.uni-goettingen.de/purl?gro-2/102860"],["dc.language.iso","en"],["dc.notes.intern","DOI-Import GROB-531"],["dc.relation.eissn","1524-4539"],["dc.relation.issn","0009-7322"],["dc.title","Defective Ryanodine Receptor Interdomain Interactions May Contribute to Intracellular Ca 2+ Leak"],["dc.title.alternative","A Novel Therapeutic Target in Heart Failure"],["dc.type","journal_article"],["dc.type.internalPublication","unknown"],["dspace.entity.type","Publication"]]