about
Ankrd2/ARPP is a novel Akt2 specific substrate and regulates myogenic differentiation upon cellular exposure to H(2)O(2)Ankrd2 is a modulator of NF-κB-mediated inflammatory responses during muscle differentiationPotential therapeutic effects of the MTOR inhibitors for preventing ageing and progeria-related disordersAssociation of emerin with nuclear and cytoplasmic actin is regulated in differentiating myoblastsLaminopathies and lamin-associated signaling pathways.Rapamycin treatment of Mandibuloacral dysplasia cells rescues localization of chromatin-associated proteins and cell cycle dynamicsAutophagic degradation of farnesylated prelamin A as a therapeutic approach to lamin-linked progeria.Altered chromatin organization and SUN2 localization in mandibuloacral dysplasia are rescued by drug treatment.Familial partial lipodystrophy, mandibuloacral dysplasia and restrictive dermopathy feature barrier-to-autointegration factor (BAF) nuclear redistribution.Barrier-to-autointegration factor (BAF) involvement in prelamin A-related chromatin organization changes.A-type lamins and signaling: the PI 3-kinase/Akt pathway moves forward.Laminopathies and A-type lamin-associated signalling pathways.Diverse lamin-dependent mechanisms interact to control chromatin dynamics. Focus on laminopathiesEmery-Dreifuss Muscular Dystrophy-Associated Mutant Forms of Lamin A Recruit the Stress Responsive Protein Ankrd2 into the Nucleus, Affecting the Cellular Response to Oxidative Stress.Lamin A Ser404 is a nuclear target of Akt phosphorylation in C2C12 cells.Sensitization of multidrug resistant human ostesarcoma cells to Apo2 Ligand/TRAIL-induced apoptosis by inhibition of the Akt/PKB kinase.Insulin activates protein kinases C-zeta and C-lambda by an autophosphorylation-dependent mechanism and stimulates their translocation to GLUT4 vesicles and other membrane fractions in rat adipocytes.Interleukin-1-receptor-associated kinase 2 (IRAK2)-mediated interleukin-1-dependent nuclear factor kappaB transactivation in Saos2 cells requires the Akt/protein kinase B kinase.Regulation of novel protein kinase C epsilon by phosphorylation.Prelamin A-mediated recruitment of SUN1 to the nuclear envelope directs nuclear positioning in human muscle.Altered pre-lamin A processing is a common mechanism leading to lipodystrophy.Lamins are rapamycin targets that impact human longevity: a study in centenarians.Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: altered intermolecular interaction with emerin and implications for gene transcription.Targeting of the Akt/PKB kinase to the actin skeleton.Letter to the editor: Comments on Wette et al. (2017): "Characterization of muscle ankyrin repeat proteins in human skeletal muscle".Mandibuloacral dysplasia: A premature ageing disease with aspects of physiological ageing.Lamin A precursor induces barrier-to-autointegration factor nuclear localization.Pre-Lamin A processing is linked to heterochromatin organization.Implications for nuclear organization and gene transcription of lamin A/C specific mutationsPhosphatidylinositol 3-kinase is recruited to a specific site in the activated IL-1 receptor IThe Cutting Edge: The Role of mTOR Signaling in LaminopathiesAnkrd2 in Mechanotransduction and Oxidative Stress Response in Skeletal Muscle: New Cues for the Pathogenesis of Muscular LaminopathiesEmerin Phosphorylation during the Early Phase of the Oxidative Stress Response Influences Emerin-BAF Interaction and BAF Nuclear Localization
P50
Q24311740-6817E9C0-97A2-42BB-A4F0-15F40C6F1453Q24321224-30757851-E886-4A78-B241-67A03D35C2ACQ28067037-87C4BA37-067E-44FD-8E93-8B2C7119C13CQ28187977-AF360513-7EF9-4A06-8474-7C9463A3539DQ34170514-C827B3BE-B192-4487-B541-97F52E49EB6BQ34520717-EEBEC1D8-2703-44E4-9C91-2F9C6F118AECQ35771419-EF1FA5CA-53AF-4C97-AC74-D20EB5DAC794Q36205365-189C8105-D29D-4A8D-B3C7-02531C790785Q36338746-FC8717DF-14B1-4DAC-AC6D-F678BC61CE7EQ37085852-5F0095EE-5271-47D2-8E65-D92C71B3B04BQ37500299-D41EF87C-A6EE-44C1-8675-DFF4857E206DQ37633657-E92FFE6A-670C-4415-97A2-0BE7AE6338BCQ38284300-3E027A6C-8672-4EF2-8115-87E1D87D283CQ38770767-06A09C68-4740-4D3B-BAFA-B721D84F57D6Q39937276-723E2525-08F0-4983-B7F7-2D34A4369649Q40491145-415EBFFD-2807-4FCA-A38E-51FDE2A5AE3BQ40932884-55343151-B02C-4667-B64E-6E083FA1277BQ41767872-8441EDE9-83A7-4328-80C7-A4163137F23EQ42242103-197B9AE6-08DA-4538-BD21-1EF7C15345D9Q42735850-C7DD709F-5852-4416-B39F-62804BD80423Q42815664-599749AC-D469-4523-AAB3-F67E3B17A97EQ44421915-1AFCBD2B-196C-4C69-BFAE-DB520FBA9709Q44641885-EC432E03-7800-4249-AD3D-D54787425257Q44699627-202AA5EC-F4C1-45E9-B522-560AF747F638Q47675014-5CC55158-7E75-4424-A14E-98B249A1D743Q50059432-43DCF1DD-82E3-42C5-9954-DBC8AF407EB7Q53316358-1CB7E7E5-4F71-4A12-A0E0-65542D7D4623Q53538268-412E4201-4696-402D-B2E2-D9DF7E3AC60BQ57000570-493BD5DC-3481-4139-9C76-AB6CA23550F1Q59235656-41483B6B-89BD-491F-A007-E360ADEC0B41Q64256257-054645DC-F971-4A77-8910-821D525DA118Q92713440-F6B16B93-2511-4DEF-AFDB-1624D7FBC6FEQ96226421-82F0486E-8C10-452B-B1E4-A11EAFCDC91C
P50
description
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Vittoria Cenni
@ast
Vittoria Cenni
@en
Vittoria Cenni
@es
Vittoria Cenni
@nl
Vittoria Cenni
@sl
type
label
Vittoria Cenni
@ast
Vittoria Cenni
@en
Vittoria Cenni
@es
Vittoria Cenni
@nl
Vittoria Cenni
@sl
prefLabel
Vittoria Cenni
@ast
Vittoria Cenni
@en
Vittoria Cenni
@es
Vittoria Cenni
@nl
Vittoria Cenni
@sl
P106
P31
P496
0000-0001-8062-1840