about
Regulation of epidermal growth factor receptor traffic by the small GTPase rhoBFGF-2 protects small cell lung cancer cells from apoptosis through a complex involving PKCepsilon, B-Raf and S6K2PKCzetaII is a target for degradation through the tumour suppressor protein pVHLThe regulated assembly of a PKCepsilon complex controls the completion of cytokinesisPRK1 is targeted to endosomes by the small GTPase, RhoBRegulatory domain selectivity in the cell-type specific PKN-dependence of cell migrationPtdIns-specific MPR pathway association of a novel WD40 repeat protein, WIPI49Regulated binding of the protein kinase C substrate GAP-43 to the V0/C2 region of protein kinase C-deltaRecognition of an intra-chain tandem 14-3-3 binding site within PKCepsilon14-3-3 proteins interact with a hybrid prenyl-phosphorylation motif to inhibit G proteinsPhosphorylation of GAP-43 (growth-associated protein of 43 kDa) by conventional, novel and atypical isotypes of the protein kinase C gene family: differences between oligopeptide and polypeptide phosphorylationSite-directed perturbation of protein kinase C- integrin interaction blocks carcinoma cell chemotaxis.Protein kinase C phosphorylates ribosomal protein S6 kinase betaII and regulates its subcellular localization.A selective PIKfyve inhibitor blocks PtdIns(3,5)P(2) production and disrupts endomembrane transport and retroviral budding.An aPKC-exocyst complex controls paxillin phosphorylation and migration through localised JNK1 activationBeta 1-integrin-c-Met cooperation reveals an inside-in survival signalling on autophagy-related endomembranes.Molecular dissection of the interaction between the small G proteins Rac1 and RhoA and protein kinase C-related kinase 1 (PRK1)Adenosine-binding motif mimicry and cellular effects of a thieno[2,3-d]pyrimidine-based chemical inhibitor of atypical protein kinase C isoenzymesSAC1 encodes a regulated lipid phosphoinositide phosphatase, defects in which can be suppressed by the homologous Inp52p and Inp53p phosphatases.Svp1p defines a family of phosphatidylinositol 3,5-bisphosphate effectors.Calmodulin controls organization of the actin cytoskeleton via regulation of phosphatidylinositol (4,5)-bisphosphate synthesis in Saccharomyces cerevisiaeMSS4, a phosphatidylinositol-4-phosphate 5-kinase required for organization of the actin cytoskeleton in Saccharomyces cerevisiae.Rho GTPase control of protein kinase C-related protein kinase activation by 3-phosphoinositide-dependent protein kinaseGab1 phosphorylation: a novel mechanism for negative regulation of HGF receptor signalingDephosphorylation of PKCdelta by protein phosphatase 2Ac and its inhibition by nucleotidesTyrosine phosphorylation and relocation of SHIP are integrin-mediated in thrombin-stimulated human blood plateletsSpecific proteolysis of the kinase protein kinase C-related kinase 2 by caspase-3 during apoptosis. Identification by a novel, small pool expression cloning strategyPIKfyve negatively regulates exocytosis in neurosecretory cellsMultiple interactions of PRK1 with RhoA. Functional assignment of the Hr1 repeat motifPRK1 phosphorylates MARCKS at the PKC sites: serine 152, serine 156 and serine 163The PtdIns-PLC superfamily and signal transductionProtein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1The SH2 domain containing inositol 5-phosphatase SHIP2 displays phosphatidylinositol 3,4,5-trisphosphate and inositol 1,3,4,5-tetrakisphosphate 5-phosphatase activityIsoenzyme specificity of bisindolylmaleimides, selective inhibitors of protein kinase CHER2 oncogenic function escapes EGFR tyrosine kinase inhibitors via activation of alternative HER receptors in breast cancer cellsRole of a novel PH-kinase domain interface in PKB/Akt regulation: structural mechanism for allosteric inhibitionHER2 phosphorylation is maintained by a PKB negative feedback loop in response to anti-HER2 herceptin in breast cancerThe identification and characterization of novel PKCepsilon phosphorylation sites provide evidence for functional cross-talk within the PKC superfamilyTSPO interacts with VDAC1 and triggers a ROS-mediated inhibition of mitochondrial quality controlPKCepsilon-mediated phosphorylation of vimentin controls integrin recycling and motility
P50
Q22010605-BA332FB2-4F8A-4997-8789-97DEF1A356AFQ24295106-34F44EB9-01B5-497F-8605-60910146A84FQ24299736-AACF6432-1C51-4A36-9B0D-D6FBDB8E56A3Q24310255-0B3630AA-78D8-47A4-B259-528D87031F0FQ24312153-1DB25D69-E3BD-4A82-BE2B-A857D98DAAC6Q24314028-49EE5B0E-FC56-4F51-B886-42771AFC9ED9Q24316670-F44A07A3-6721-4343-BE2F-830DF6B41242Q24318797-3C4AEC3F-F2C0-452C-97D2-0DDD6B5703C9Q24321733-55F43EB2-6F32-489A-8B1E-321A1BFCB436Q24339259-8524290F-F295-420D-81D8-9D81E2DB9B99Q24529846-750EAA4A-5946-426B-B4D1-CFC6A7D0F1B4Q24537649-16F1BC38-06D7-4879-B77A-A7A24311F6F5Q24540893-DB0FDBBE-2B89-48D8-80A1-9E1E64313B63Q24645971-9544F744-088D-4D10-B603-0B6FE60C4E22Q27325523-0E3D8DC0-37B6-4710-BFB1-C4728E62964BQ27342529-60B5B7AB-1C81-48D1-A99E-8707441754EFQ27642233-A2646A74-AADF-4DA3-AF1A-6182DEF988C9Q27684030-8D10BF03-086B-48CC-AC5A-F6BEF497A0ABQ27930732-1BDE2C93-C4ED-42D5-9537-DFBD7157F95DQ27936381-3C3C7A87-2D89-4DDE-A4D3-175DE8FAD3E3Q27936815-B62F2F74-C40E-4407-B31A-32197141B954Q27939032-75B5E49F-6069-4029-B8A3-F6BF5EAC034FQ28141177-E23C7433-5408-4D08-842D-B08C5B8D7E82Q28213808-3AE1D2C7-C792-403C-852A-8B25F58854CDQ28215036-599AF980-E1A5-4567-927C-5F2B56207636Q28252099-48B8E7A3-90C9-414B-B056-7098CFAD992DQ28254596-87F8676D-A55E-4D33-BEA4-C007C3BB0086Q28258731-09025B80-2F9F-41D2-B1E9-E04337A8B017Q28260212-60D49A68-3D9B-4243-8C0D-C2CCFD07D783Q28272935-A18B1E91-D5EC-4DE3-8538-19642E34842AQ28280640-DF360EE5-3515-43AB-9172-92DEFF8E387BQ28283323-E693E91F-7FE8-4964-AF6D-521D80A7F40AQ28289470-C33C2373-C53D-4B06-ABCC-ED78DE97BEADQ28378609-4D3C37D6-FD92-48C1-8717-F17C5472AA9DQ28473274-FA89FC3C-4117-456D-A39F-007C25E5A50AQ28474624-8E153405-6B83-4637-B987-F2440F4348BDQ28476604-DBF3D6DE-D0A0-4CEB-BC8C-167528F31D50Q28507878-A71D17CA-F29F-4F24-B49B-AD25E5329BA6Q28508394-8337370F-EF84-4273-8C0C-46F27DB80D25Q28512303-3322AA4B-0E39-4348-9809-22D65D577F9A
P50
description
researcher
@en
ricercatore
@it
wetenschapper
@nl
հետազոտող
@hy
name
Peter Parker
@ast
Peter Parker
@en
Peter Parker
@es
Peter Parker
@nl
type
label
Peter Parker
@ast
Peter Parker
@en
Peter Parker
@es
Peter Parker
@nl
prefLabel
Peter Parker
@ast
Peter Parker
@en
Peter Parker
@es
Peter Parker
@nl
P106
P1153
7202013506
P21
P214
6816155044791072520008
P31
P496
0000-0002-6218-2933