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Phosphorylation of DARPP-32 by Cdk5 modulates dopamine signalling in neuronsDARPP-32 mediates the actions of multiple drugs of abuseMethylphenidate-induced dendritic spine formation and DeltaFosB expression in nucleus accumbensStriatal dysregulation of Cdk5 alters locomotor responses to cocaine, motor learning, and dendritic morphologyA calcium- and calmodulin-dependent kinase Ialpha/microtubule affinity regulating kinase 2 signaling cascade mediates calcium-dependent neurite outgrowthSpinophilin directs protein phosphatase 1 specificity by blocking substrate binding sitesRegulation of synaptojanin 1 by cyclin-dependent kinase 5 at synapsesProtein phosphatase 2C binds selectively to and dephosphorylates metabotropic glutamate receptor 3Abeta-mediated NMDA receptor endocytosis in Alzheimer's disease involves ubiquitination of the tyrosine phosphatase STEP61Protein phosphatases and Alzheimer's diseasePhosphodiesterase 4 inhibition enhances the dopamine D1 receptor/PKA/DARPP-32 signaling cascade in frontal cortex.Twenty-one-base-pair insertion polymorphism creates an enhancer element and potentiates SLC6A1 GABA transporter promoter activityCharacterization of the interaction between DARPP-32 and protein phosphatase 1 (PP-1): DARPP-32 peptides antagonize the interaction of PP-1 with binding proteinsRole of Striatal-Enriched Tyrosine Phosphatase in Neuronal FunctionThe PsychENCODE projectGenetic reduction of striatal-enriched tyrosine phosphatase (STEP) reverses cognitive and cellular deficits in an Alzheimer's disease mouse modelRecent advances in quantitative neuroproteomicsThe role of ventral striatal cAMP signaling in stress-induced behaviors.APP intracellular domain-WAVE1 pathway reduces amyloid-β production.Inhibition of the tyrosine phosphatase STEP61 restores BDNF expression and reverses motor and cognitive deficits in phencyclidine-treated mice.Crystal structure of the atypical protein kinase domain of a TRP channel with phosphotransferase activityCrystal structure of a tetradecameric assembly of the association domain of Ca2+/calmodulin-dependent kinase IIStructural basis for spinophilin-neurabin receptor interactionUnderstanding the antagonism of retinoblastoma protein dephosphorylation by PNUTS provides insights into the PP1 regulatory codeStriatal-enriched protein tyrosine phosphatase in Alzheimer's disease.Inhibition of the Ca2+/calmodulin-dependent protein kinase I cascade by cAMP-dependent protein kinasePhylogenetically conserved CK-II phosphorylation site of the murine homeodomain protein Hoxb-6STEP61 is a substrate of the E3 ligase parkin and is upregulated in Parkinson's diseasePhosphorylation of DARPP-32 at Threonine-34 is required for cocaine actionDARPP-32, a dopamine- and adenosine 3':5'-monophosphate-regulated neuronal phosphoprotein. II. Comparison of the kinetics of phosphorylation of DARPP-32 and phosphatase inhibitor 1Purification and characterization of calmodulin-dependent protein kinase III from rabbit reticulocytes and rat pancreasCharacterization of the mechanism of regulation of Ca2+/ calmodulin-dependent protein kinase I by calmodulin and by Ca2+/calmodulin-dependent protein kinase kinaseThe regulatory region of calcium/calmodulin-dependent protein kinase I contains closely associated autoinhibitory and calmodulin-binding domainsDisruption of reelin signaling attenuates methamphetamine-induced hyperlocomotionPP1gamma2 and PPP1R11 are parts of a multimeric complex in developing testicular germ cells in which their steady state levels are reciprocally relatedA phosphatase cascade by which rewarding stimuli control nucleosomal response.Inhibitor of the tyrosine phosphatase STEP reverses cognitive deficits in a mouse model of Alzheimer's diseasePKC-alpha regulates cardiac contractility and propensity toward heart failureModulation of a calcium/calmodulin-dependent protein kinase cascade by retinoic acid during neutrophil maturationMammalian brain phosphoproteins as substrates for calcineurin
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Q22010952-E97A26C3-D130-4154-BBBC-230AEFE11D5BQ22241668-F4197F6D-8CF0-4F4B-A16D-8E18E25DBE53Q22248089-C3FFA0CF-21BC-4683-99BA-6B363A7DAA90Q23912227-FB1D7E2F-7EA1-41DD-A8CC-7A6FA5FB629FQ24303452-98710846-A871-4271-8263-53540AF3471DQ24304144-EC07B007-DB29-4186-84AD-5CC2C5DC60E6Q24597922-3CD73854-5E56-4EEC-A987-A1C5B821671DQ24616083-56B95DAE-C07A-4634-9861-9954327D1065Q24620404-AC7BB066-B390-4090-9CCE-AD153FFAB892Q24632495-9C478C65-6359-401E-8AA8-3CDA1DDC933AQ24633622-AB3F154B-0187-49DA-9CBA-17E59E9A941AQ24643332-50E31412-1254-46B4-8F09-8138A6CA3C5CQ24670906-8FB4ED67-BA43-4A2F-9196-E17C58E86C2FQ26748710-259EDE4B-971E-489A-AF97-B2851976690AQ26775498-70864C9A-5DFF-4B3B-A2D1-8ED46077E250Q26781974-0C6586E7-D118-4167-9522-CFD926846F3DQ27000073-7F29D119-1C52-4599-BFA4-2187A378246BQ27312156-CCBBF54F-888E-4217-B058-C09AD7E64107Q27315195-ABFD9CA9-37D9-4CCB-A988-D68E2BFA7163Q27327213-668B6827-EB0C-476F-ACBF-EDB631548E52Q27632346-DED8666A-451D-41E3-BB51-F4851CA86DCCQ27641331-6D4DB72B-633F-4198-82FE-35D77706E4B2Q27643749-ACE179FD-0962-49D2-BEBB-81BF755B7A0CQ27681976-A635A762-5D8F-4AA1-9128-B199B4501303Q27687325-63C5A69E-6438-48AF-81BD-D2DABC00C259Q28140472-1D27D146-704F-4DE8-B520-93AB2619AD60Q28143991-032B8221-CD05-44FE-AFF4-9C7575F3CCB2Q28255428-070BA126-95FB-416C-807F-7CE62BAF0F0FQ28269125-851B207D-46EA-4C37-8770-BB09EBE45313Q28269654-64D689CB-5C9D-49E1-B954-808853AC92D9Q28270230-90C44CA6-4B99-4BCA-AC05-CF2C5CD90648Q28279720-0F119C11-EC17-4E20-8E59-720007848CA1Q28289472-B286D8FD-FFA9-40D3-AA3C-855D9A6EB50DQ28305243-79FED207-C187-47CE-B800-9975E9222416Q28475039-C64102B0-A2B3-486C-8428-9235FC9ABEB5Q28508656-C12573F7-6AC9-4440-BBD1-1CA6F1EA8B0CQ28541603-4DD3285F-C6FD-4B13-837A-83FABD039EEBQ28589911-E54F7435-686E-4E0C-8D20-6B369150A083Q28594503-6204DAFF-7BFC-4C74-B6DC-A5A4E82CCDE0Q28643957-65D64785-168B-4E26-86C2-AC15D349BA60
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description
hulumtues
@sq
researcher
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wetenschapper
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հետազոտող
@hy
name
Angus C Nairn
@nl
Angus C Nairn
@sl
Angus C. Nairn
@en
Angus C. Nairn
@es
type
label
Angus C Nairn
@nl
Angus C Nairn
@sl
Angus C. Nairn
@en
Angus C. Nairn
@es
prefLabel
Angus C Nairn
@nl
Angus C Nairn
@sl
Angus C. Nairn
@en
Angus C. Nairn
@es
P106
P108
P1153
35448395500
P21
P31
P496
0000-0002-7075-0195