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AKAP18δ Anchors and Regulates CaMKII Activity at Phospholamban-SERCA2 and RYR

Circulation Research(2021)10.1161/circresaha.120.317976Source: DataRank Database

AKAP18δ Anchors and Regulates CaMKII Activity at Phospholamban-SERCA2 and RYR is a research paper published in Circulation Research (2021). On theSindex it has a DataRank of 0. It has been cited 59 times.

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Open Access59 citations

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›Methodology & internals

datarank_citation_only_1hop_v6· scope data_onlyMethodology

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Enrichment:Funding (19 grants)Impact (FWCI 6.87)OA: hybridTopics (110)Linked Datasets (12)DataCite Reuse (12)IDs (PubMed, PMC, OpenAlex)SDGs (1)

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Context only (not used in score)

Findable (2/2)

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Accessible (1/2)

Open Access

Interoperable (2/2)

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Reusable (0/3)

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Authors (22)

Jan Magnus Aronsen ORCID,Anna Bergan-Dahl ORCID,Marie Christine Moutty,Marianne Lunde,Per Lunde

Live enrichment

PubMed:34814703 PMC:PMC9500498 OpenAlex:https://openalex.org/W3216867216

HHS | National Institutes of Health

Grant: R01- HL133832

HHS | National Institutes of Health

Grant: R01-HL142282

Deutsche Forschungsgemeinschaft

Grant: KL1415/7-1

Deutsche Forschungsgemeinschaft

Grant: 394046635 - SFB 1365

the Bundesministerium für Bildung und Forschung

Grant: 16GW0179K

the German Israeli Foundation

Grant: I-1452-203/13-2018

NHLBI NIH HHS

Grant: R01 HL142282

NHLBI NIH HHS

Grant: R01 HL092097

NHLBI NIH HHS

Grant: R01 HL133832

Deutsche Forschungsgemeinschaft

Grant: 394046635/SFB 1365

Renoprotection

National Institutes of Health

Grant: 5R01HL133832-02

AKAP-dependent regulation of Cardiac SR Ca handling

Deutsche Forschungsgemeinschaft

Grant: unidentified

unidentified

National Institutes of Health

Grant: 5R01HL142282-03

CaMKII activation and regulation in adult cardiac myocytes

Anders Jahres Fond til Vitenskapens Fremme

Nasjonalforeningen for Folkehelsen

UNIFOR-FRIMED

South-Eastern Norway Regional Health Authority

Stiftelsen Kristian Gerhard Jebsen

The Research Council of Norway

FWCI

6.87

Citation Percentile

1.0%

Influential Citations

Citation Trend

2022

2023

2024

2025

2026

hybridLicense: cc-by-nc-nd

journalhttps://www.ahajournals.org/doi/pdf/10.1161/CIRCRESAHA.120.317976

HYBRIDhttps://www.ahajournals.org/doi/pdf/10.1161/CIRCRESAHA.120.317976

publisherhttps://www.ahajournals.org/doi/pdf/10.1161/CIRCRESAHA.120.317976

publisherhttps://www.ahajournals.org/doi/full/10.1161/CIRCRESAHA.120.317976

journalhttps://doi.org/10.1161/circresaha.120.317976

Fields of Study

Cardiac electrophysiology and arrhythmiasProtein Kinase Regulation and GTPase SignalingCongenital heart defects researchMedicineBiology0303 health sciences03 medical and health sciencesAdaptor Proteins, Signal TransducingAnimalsBinding SitesCalcium SignalingCalcium-Binding ProteinsCalcium-Calmodulin-Dependent Protein Kinase Type 2Cells, CulturedHEK293 CellsHumansMyocytes, CardiacProtein BindingRatsRats, WistarRyanodine Receptor Calcium Release ChannelSarcoplasmic Reticulum Calcium-Transporting ATPasesPhospholamban

MeSH Terms

PhospholambanAnimalsBinding SitesCalcium-Binding ProteinsCells, CulturedHumansProtein BindingRats, WistarRyanodine Receptor Calcium Release ChannelCalcium SignalingMyocytes, CardiacAdaptor Proteins, Signal TransducingRatsSarcoplasmic Reticulum Calcium-Transporting ATPasesCalcium-Calmodulin-Dependent Protein Kinase Type 2HEK293 Cells

Keywords

PhospholambanRyanodine receptorSERCAEndoplasmic reticulumChemistryCell biologyPhosphorylationProtein kinase ACalmodulinSignal transductionBiophysicsBiologyBiochemistryATPaseMyocytes, cardiacCalcium-calmodulin-dependent Protein Kinase Type 2Sarcoplasmic Reticulum Calcium-transporting AtpasesMedical PhysiologyWistarCardiorespiratory Medicine and Haematology3208 Medical Physiology (for-2020)Sarcoplasmic Reticulum Calcium-Transporting ATPases (mesh)1103 Clinical Sciences (for)Protein Binding (mesh)Animals (mesh)32 Biomedical and Clinical Sciences (for-2020)Cells, CulturedHumans (mesh)CulturedCalcium-Binding Proteins (mesh)Adaptor Proteins3201 Cardiovascular medicine and haematology (for-2020)Calcium Signaling (mesh)Rats (mesh)[SDV] Life Sciences [q-bio]CardiacCultured (mesh)Protein Binding5701.1 Normal biological development and functioningCellsClinical Sciences610Binding Sites (mesh)Cardiovascular medicine and haematologySignal Transducing (mesh)1102 Cardiorespiratory Medicine and Haematology (for)AnimalsHumansCalcium SignalingCardiovascular System & Hematology (science-metrix)Rats, WistarAdaptor Proteins, Signal Transducing1.1 Normal biological development and functioning (hrcs-rac)HEK293 Cells (mesh)Calcium-Calmodulin-Dependent Protein Kinase Type 2 (mesh)MyocytesBinding SitesBiomedical and Clinical SciencesCalcium-Binding ProteinsSignal TransducingRyanodine Receptor Calcium Release Channel3202 Clinical sciences (for-2020)Cardiac (mesh)Ryanodine Receptor Calcium Release Channel (mesh)RatsHEK293 CellsCardiovascular System & HematologyWistar (mesh)Cardiovascular and Metabolic DiseasesTopic 2: Molecular Processes and Therapies

Sustainable Development Goals

SDG 3: 3. Good health

Additional file 1 of M-type pyruvate kinase 2 (PKM2) tetramerization alleviates the progression of right ventricle failure by regulating oxidative stress and mitochondrial dynamics

10.6084/m9.figshare.26650767.v1figshare

Additional file 1 of M-type pyruvate kinase 2 (PKM2) tetramerization alleviates the progression of right ventricle failure by regulating oxidative stress and mitochondrial dynamics

10.6084/m9.figshare.26650767figshare

Additional file 2 of M-type pyruvate kinase 2 (PKM2) tetramerization alleviates the progression of right ventricle failure by regulating oxidative stress and mitochondrial dynamics

10.6084/m9.figshare.26650770.v1figshare

Additional file 2 of M-type pyruvate kinase 2 (PKM2) tetramerization alleviates the progression of right ventricle failure by regulating oxidative stress and mitochondrial dynamics

10.6084/m9.figshare.26650770figshare

Additional file 3 of M-type pyruvate kinase 2 (PKM2) tetramerization alleviates the progression of right ventricle failure by regulating oxidative stress and mitochondrial dynamics

10.6084/m9.figshare.26650773.v1figshare

Additional file 3 of M-type pyruvate kinase 2 (PKM2) tetramerization alleviates the progression of right ventricle failure by regulating oxidative stress and mitochondrial dynamics

10.6084/m9.figshare.26650773figshare

Additional file 4 of M-type pyruvate kinase 2 (PKM2) tetramerization alleviates the progression of right ventricle failure by regulating oxidative stress and mitochondrial dynamics

10.6084/m9.figshare.26650776.v1figshare

Additional file 4 of M-type pyruvate kinase 2 (PKM2) tetramerization alleviates the progression of right ventricle failure by regulating oxidative stress and mitochondrial dynamics

10.6084/m9.figshare.26650776figshare

Additional file 6 of M-type pyruvate kinase 2 (PKM2) tetramerization alleviates the progression of right ventricle failure by regulating oxidative stress and mitochondrial dynamics

10.6084/m9.figshare.26650782.v1figshare

Additional file 6 of M-type pyruvate kinase 2 (PKM2) tetramerization alleviates the progression of right ventricle failure by regulating oxidative stress and mitochondrial dynamics

10.6084/m9.figshare.26650782figshare

Additional file 5 of M-type pyruvate kinase 2 (PKM2) tetramerization alleviates the progression of right ventricle failure by regulating oxidative stress and mitochondrial dynamics

10.6084/m9.figshare.26650779.v1figshare

Additional file 5 of M-type pyruvate kinase 2 (PKM2) tetramerization alleviates the progression of right ventricle failure by regulating oxidative stress and mitochondrial dynamics

10.6084/m9.figshare.26650779figshare