Search Results - "van Petegem, Filip"
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Pathological conformations of disease mutant Ryanodine Receptors revealed by cryo-EM
Published in Nature communications (05-02-2021)“…Ryanodine Receptors (RyRs) are massive channels that release Ca 2+ from the endoplasmic and sarcoplasmic reticulum. Hundreds of mutations are linked to…”
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2
Disease Mutations in the Ryanodine Receptor Central Region: Crystal Structures of a Phosphorylation Hot Spot Domain
Published in Structure (London) (03-07-2012)“…Ryanodine Receptors (RyRs) are huge Ca2+ release channels in the endoplasmic reticulum membrane and form targets for phosphorylation and disease mutations. We…”
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3
Structural basis for diamide modulation of ryanodine receptor
Published in Nature chemical biology (01-11-2020)“…The diamide insecticide class is one of the top-selling insecticides globally. They are used to control a wide range of pests by targeting their ryanodine…”
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4
Structures of the junctophilin/voltage-gated calcium channel interface reveal hot spot for cardiomyopathy mutations
Published in Proceedings of the National Academy of Sciences - PNAS (08-03-2022)“…SignificanceIon channels have evolved the ability to communicate with one another, either through protein-protein interactions, or indirectly via intermediate…”
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5
Cryo-EM structures of the ABCA4 importer reveal mechanisms underlying substrate binding and Stargardt disease
Published in Nature communications (08-10-2021)“…ABCA4 is an ATP-binding cassette (ABC) transporter that flips N-retinylidene-phosphatidylethanolamine (N-Ret-PE) from the lumen to the cytoplasmic leaflet of…”
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6
Crystal structures of ryanodine receptor SPRY1 and tandem-repeat domains reveal a critical FKBP12 binding determinant
Published in Nature communications (06-08-2015)“…Ryanodine receptors (RyRs) form calcium release channels located in the membranes of the sarcoplasmic and endoplasmic reticulum. RyRs play a major role in…”
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Cardiac ryanodine receptor distribution is dynamic and changed by auxiliary proteins and post-translational modification
Published in eLife (09-01-2020)“…The effects of the immunophilins, FKBP12 and FKBP12.6, and phosphorylation on type II ryanodine receptor (RyR2) arrangement and function were examined using…”
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Catecholaminergic polymorphic ventricular tachycardia patients with multiple genetic variants in the PACES CPVT Registry
Published in PloS one (07-11-2018)“…Catecholaminergic polymorphic ventricular tachycardia (CPVT) is often a life-threatening arrhythmia disorder with variable penetrance and expressivity. Little…”
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9
Lobe-Specific Calmodulin Binding to Different Ryanodine Receptor Isoforms
Published in Biochemistry (Easton) (11-02-2014)“…Ryanodine receptors (RyRs) are large ion channels that are responsible for the release of Ca2+ from the sarcoplasmic/endoplasmic reticulum. Calmodulin (CaM) is…”
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10
Seeing the Forest through the Trees: towards a Unified View on Physiological Calcium Regulation of Voltage-Gated Sodium Channels
Published in Biophysical journal (05-12-2012)“…Voltage-gated sodium channels (NaVs) underlie the upstroke of the action potential in the excitable tissues of nerve and muscle. After opening, NaVs rapidly…”
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Ryanodine Receptors: Allosteric Ion Channel Giants
Published in Journal of molecular biology (16-01-2015)“…The endoplasmic reticulum (ER) and sarcoplasmic reticulum (SR) form major intracellular Ca2+ stores. Ryanodine receptors (RyRs) are large tetrameric ion…”
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12
RNA Polymerase II transcription independent of TBP in murine embryonic stem cells
Published in eLife (30-03-2023)“…Transcription by RNA Polymerase II (Pol II) is initiated by the hierarchical assembly of the pre-initiation complex onto promoter DNA. Decades of research have…”
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The Cardiac Ryanodine Receptor N-Terminal Region Contains an Anion Binding Site that Is Targeted by Disease Mutations
Published in Structure (London) (06-08-2013)“…Ryanodine receptors (RyRs) are calcium release channels located in the membrane of the endoplasmic and sarcoplasmic reticulum and play a major role in muscle…”
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14
The Deletion of Exon 3 in the Cardiac Ryanodine Receptor Is Rescued by β Strand Switching
Published in Structure (London) (08-06-2011)“…Mutations in the cardiac Ryanodine Receptor (RYR2) are linked to triggered arrhythmias. Removal of exon 3 results in a severe form of catecholaminergic…”
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15
A Novel RYR2 Loss-of-Function Mutation (I4855M) is Associated with Left Ventricular Non-compaction and Atypical Catecholaminergic Polymorphic Ventricular Tachycardia
Published in Journal of electrocardiology (01-03-2017)“…Abstract Background Catecholaminergic polymorphic ventricular tachycardia (CPVT) is an ion channelopathy usually caused by gain-of-function mutations ryanodine…”
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16
Calcium-release channels: structure and function of IP3 receptors and ryanodine receptors
Published in Physiological reviews (01-01-2022)“…Ca2+-release channels are giant membrane proteins that control the release of Ca2+ from the endoplasmic and sarcoplasmic reticulum. The two members, ryanodine…”
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Talin Autoinhibition Is Required for Morphogenesis
Published in Current biology (23-09-2013)“…The establishment of a multicellular body plan requires coordinating changes in cell adhesion and the cytoskeleton to ensure proper cell shape and position…”
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Characterization of Zebrafish Cardiac and Slow Skeletal Troponin C Paralogs by MD Simulation and ITC
Published in Biophysical journal (12-07-2016)“…Zebrafish, as a model for teleost fish, have two paralogous troponin C (TnC) genes that are expressed in the heart differentially in response to temperature…”
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Structure and function of STAC proteins: Calcium channel modulators and critical components of muscle excitation–contraction coupling
Published in The Journal of biological chemistry (01-07-2021)“…In skeletal muscle tissue, an intriguing mechanical coupling exists between two ion channels from different membranes: the L-type voltage-gated calcium channel…”
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Binary architecture of the Nav1.2-β2 signaling complex
Published in eLife (19-02-2016)“…To investigate the mechanisms by which β-subunits influence Nav channel function, we solved the crystal structure of the β2 extracellular domain at 1.35Å. We…”
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