about
The mitochondrial Ca2+ uniporter MCU is essential for glucose-induced ATP increases in pancreatic β-cellsQuercetin induces insulin secretion by direct activation of L-type calcium channels in pancreatic beta cellsSREBP1 is required for the induction by glucose of pancreatic beta-cell genes involved in glucose sensingSubplasmalemmal Ca(2+) measurements in mouse pancreatic beta cells support the existence of an amplifying effect of glucose on insulin secretionImaging a target of Ca2+ signalling: dense core granule exocytosis viewed by total internal reflection fluorescence microscopy.Control mechanisms of the oscillations of insulin secretion in vitro and in vivo.Hierarchy of the beta-cell signals controlling insulin secretion.Mechanisms of control of the free Ca2+ concentration in the endoplasmic reticulum of mouse pancreatic β-cells: interplay with cell metabolism and [Ca2+]c and role of SERCA2b and SERCA3.Insulin secretion in health and disease: genomics, proteomics and single vesicle dynamics.Ca2+ microdomains and the control of insulin secretion.Inhibition of the MAP3 kinase Tpl2 protects rodent and human β-cells from apoptosis and dysfunction induced by cytokines and enhances anti-inflammatory actions of exendin-4.Frequency-dependent mitochondrial Ca(2+) accumulation regulates ATP synthesis in pancreatic β cells.Tolbutamide controls glucagon release from mouse islets differently than glucose: involvement of K(ATP) channels from both α-cells and δ-cells.Insulin crystallization depends on zinc transporter ZnT8 expression, but is not required for normal glucose homeostasis in mice.Emerging roles for β-arrestin-1 in the control of the pancreatic β-cell function and mass: new therapeutic strategies and consequences for drug screening.Calcium signaling in pancreatic β-cells in health and in Type 2 diabetes.Sustained exposure to high glucose concentrations modifies glucose signaling and the mechanics of secretory vesicle fusion in primary rat pancreatic beta-cells.Glucose or insulin, but not zinc ions, inhibit glucagon secretion from mouse pancreatic alpha-cells.Glucose controls cytosolic Ca2+ and insulin secretion in mouse islets lacking adenosine triphosphate-sensitive K+ channels owing to a knockout of the pore-forming subunit Kir6.2.Loss of connexin36 channels alters beta-cell coupling, islet synchronization of glucose-induced Ca2+ and insulin oscillations, and basal insulin release.Glucose-dependent regulation of gamma-aminobutyric acid (GABA A) receptor expression in mouse pancreatic islet alpha-cells.Isolation and culture of mouse pancreatic islets for ex vivo imaging studies with trappable or recombinant fluorescent probes.Do oscillations of insulin secretion occur in the absence of cytoplasmic Ca2+ oscillations in beta-cells?The elevation of glutamate content and the amplification of insulin secretion in glucose-stimulated pancreatic islets are not causally related.Disorganization of cytoplasmic Ca(2+) oscillations and pulsatile insulin secretion in islets from ob/ obmice.Time and amplitude regulation of pulsatile insulin secretion by triggering and amplifying pathways in mouse islets.Dual mechanism of the potentiation by glucose of insulin secretion induced by arginine and tolbutamide in mouse islets.ERK1 is dispensable for mouse pancreatic beta cell function but is necessary for glucose-induced full activation of MSK1 and CREB.Proteasomal degradation of the histone acetyl transferase p300 contributes to beta-cell injury in a diabetes environment.β-Arrestin2 plays a key role in the modulation of the pancreatic beta cell mass in miceThe Oscillatory Behavior of Pancreatic Islets from Mice with Mitochondrial Glycerol-3-phosphate Dehydrogenase KnockoutOscillations of insulin secretion can be triggered by imposed oscillations of cytoplasmic Ca2+ or metabolism in normal mouse isletsMethods to Study Roles of β-Arrestins in the Regulation of Pancreatic β-Cell Function
P50
Q24294221-327EAA8B-CBD6-4662-BA08-3E829E408FF0Q24606210-635FD9D4-1D0B-4E4C-96C9-727B62C255B1Q28508474-7EDAE36F-722D-4DA9-B475-24E38CEA76FCQ29036821-6737EADF-C718-40AF-A5BA-3745340CFCF3Q33375889-52D4D9FD-48DD-448A-A189-83E4F423CDDCQ34508775-834E680E-23B8-42A3-9EB5-B51AA7219C06Q35202132-2147E19F-A89E-4572-9F6F-31C2DFC30C5DQ35227195-EDBF0149-9238-4FA3-A4BF-E99CD6850CC2Q36424302-27F042DC-C777-43DE-B436-17FE9CDA44D1Q36618699-664E3FBC-501A-4D2E-AF0C-CAD9D11CF75DQ36751764-617A53F0-E4D7-4D26-8F5C-3CE116EA5ADCQ36780471-AE3549A7-07B1-4B08-9BA1-FCDCA2638897Q36796117-7CF5E313-BD13-470A-BF88-18A364AC5E6AQ37329685-01914A4B-3D4C-47AF-8C3A-93B0C9444BE5Q37789852-0867D460-D117-4F5C-9F80-8D0893DF550CQ38252722-42044E7A-C93D-4AA5-98B7-8C77C0292DF8Q40299327-4EED89E8-516F-490C-BE7A-36F04991E1ADQ40416559-5B380C9F-6764-47DD-B11B-CBC63F56843AQ42441573-87CB3B46-D5D7-4A85-8940-3EC91668E52CQ42478852-6B41FD66-CB49-43D3-9D65-B3E178E3C376Q42507525-922679BD-F49E-4A4B-873E-868D41DF60D2Q43142217-D6F1CD94-16F4-40DC-BDBB-36868FBF7663Q43869365-F46AB2D7-87DA-4A89-B919-68E16C09FB2CQ44043453-1B5D0807-7A49-4710-A755-628D0D7FD6D4Q44110189-30ADDDBA-33D1-4411-B23B-8EA40ACF60F9Q44185100-E14D29E8-8D7A-449D-BBF2-55998AF204D8Q46774528-1E1371A5-D32E-4A4C-AF39-5D35497B613AQ50882981-1F1AAF2E-124F-418F-9D92-EC44B7BFA53DQ55248558-B3C8908F-A27B-491B-AD0F-8A655EB2720BQ61315205-D63EB490-5FAB-4EB8-986B-DC5442BBDE0AQ61315450-6D8C2B63-532F-4FC7-A863-9383D7F196FDQ61315468-57BA11B4-4069-4D2E-B787-8FC9555AA064Q92665100-10FF5908-A222-4507-946D-D0A796421D1F
P50
description
hulumtuese
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Magalie Ravier
@ast
Magalie Ravier
@en
Magalie Ravier
@es
Magalie Ravier
@nl
Magalie Ravier
@sl
type
label
Magalie Ravier
@ast
Magalie Ravier
@en
Magalie Ravier
@es
Magalie Ravier
@nl
Magalie Ravier
@sl
prefLabel
Magalie Ravier
@ast
Magalie Ravier
@en
Magalie Ravier
@es
Magalie Ravier
@nl
Magalie Ravier
@sl
P1053
N-6934-2017
P106
P21
P31
P3829
P496
0000-0001-6607-6559