about
Phosphoinositides are essential coactivators for p21-activated kinase 1BIN1/M-Amphiphysin2 induces clustering of phosphoinositides to recruit its downstream partner dynamin.Structure-based discovery of an inhibitor of Arf activation by Sec7 domains through targeting of protein-protein complexesRegulation of the DH-PH tandem of guanine nucleotide exchange factor for Rho GTPases by phosphoinositides.Phosphatidylinositol 5-phosphate: a nuclear stress lipid and a tuner of membranes and cytoskeleton dynamics.Phosphoinositides: Important lipids in the coordination of cell dynamics.An allosteric kinase inhibitor binds the p21-activated kinase autoregulatory domain covalently.Cdc42-dependent F-actin dynamics drive structuration of the demarcation membrane system in megakaryocytes.[Phosphoinositides: the lipids coordinating cell dynamics].A dual role for the class III PI3K, Vps34, in platelet production and thrombus growth.Protein-Lipid Interaction by Fluorescence (PLIF) to Characterize and Screen for Inhibitors of Protein-Phosphoinositide Interactions.The MTM1-UBQLN2-HSP complex mediates degradation of misfolded intermediate filaments in skeletal muscle.CIP4 controls CCL19-driven cell steering and chemotaxis in chronic lymphocytic leukemia.Mass Assays to Quantify Bioactive PtdIns3P and PtdIns5P During Autophagic Responses.Phosphatidylinositol 5-phosphate regulates invasion through binding and activation of Tiam1.Identification of allosteric inhibitors of p21-activated kinase.The lipid products of phosphoinositide 3-kinase isoforms in cancer and thrombosis.Profiling of phosphoinositide molecular species in human and mouse platelets identifies new species increasing following stimulationStructure-activity relationships of Bak derived peptides: affinity and specificity modulations by amino acid replacementProfilin 1-mediated cytoskeletal rearrangements regulate integrin function in mouse plateletsPLIF: A rapid, accurate method to detect and quantitatively assess protein-lipid interactionsDifferences and similarities in the effects of ibrutinib and acalabrutinib on platelet functions
P50
Q28298123-B4F3DA80-1C16-45F3-9ED4-84710FADE8B9Q30009259-138041BA-60BF-4ACE-B9DD-F59BBCCD6F2FQ30480025-824B53ED-5FB2-4D2C-9910-18A02BF69A48Q38025268-E861AE49-7BED-4A11-B335-E329A74F68BCQ38174542-2528E459-2F3C-4639-A372-4EC8650A682DQ38590544-5390F55D-0C70-497D-BE94-A425CE50E59BQ39805071-7ABF2B0F-8003-460D-B00B-E53E90FD2B59Q39909113-35BA5EF2-84E0-460D-97A5-E71712425847Q40906812-538577ED-9F8C-4CC6-A371-38B2546ABD57Q42515014-93BA4FCC-B210-466B-A723-3C225E02BCF7Q48005329-083996AF-FEC5-4CED-B71E-DCA26329317BQ48190393-B6E87493-D3F9-4BCF-888B-087274FBE387Q51019240-B87E0ED5-C82C-4335-9F43-4FF02FF16A45Q51114929-60E1F9A3-4069-456B-B1D7-E4990C446176Q54346614-95B16151-5E76-44F9-ABD8-A3150D975E0DQ54485685-5A577CED-5B3E-43CB-B546-6128F8A11853Q54977034-AEC1274A-7E54-4D6E-B04A-12EB0CAF95CBQ57162589-D066E62E-0F30-4C27-8C5C-CB893BB7CC5CQ80782606-10FB8852-6629-4601-9C6D-75F2D431FC08Q88608196-B7C6A3F2-2FFB-4111-91EA-2367938DB609Q89082655-3AF0C47B-E14F-4652-824A-F5213836E906Q92022508-E77DB30B-6478-4230-B248-4422BF59E031
P50
description
chercheur
@fr
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Julien Viaud
@ast
Julien Viaud
@en
Julien Viaud
@es
Julien Viaud
@fr
Julien Viaud
@nl
Julien Viaud
@sl
type
label
Julien Viaud
@ast
Julien Viaud
@en
Julien Viaud
@es
Julien Viaud
@fr
Julien Viaud
@nl
Julien Viaud
@sl
prefLabel
Julien Viaud
@ast
Julien Viaud
@en
Julien Viaud
@es
Julien Viaud
@fr
Julien Viaud
@nl
Julien Viaud
@sl
P106
P21
P31
P496
0000-0003-4406-5642
P569
2000-01-01T00:00:00Z