Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination - Wikidata - wikimedia - TriplyDB

Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination

Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination

http://www.wikidata.org/entity/Q30432991

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Protein phosphatase 2A dysfunction in Alzheimer's disease Emerging role of Lys-63 ubiquitination in protein kinase and phosphatase activation and cancer development The biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificity Structural basis of protein phosphatase 2A stable latency Visualization of subunit interactions and ternary complexes of protein phosphatase 2A in mammalian cells Protein Phosphatase Methyl-Esterase PME-1 Protects Protein Phosphatase 2A from Ubiquitin/Proteasome Degradation XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.The E3 ubiquitin ligase- and protein phosphatase 2A (PP2A)-binding domains of the Alpha4 protein are both required for Alpha4 to inhibit PP2A degradation.Monoubiquitination promotes calpain cleavage of the protein phosphatase 2A (PP2A) regulatory subunit α4, altering PP2A stability and microtubule-associated protein phosphorylation.Essential roles of the Tap42-regulated protein phosphatase 2A (PP2A) family in wing imaginal disc development of Drosophila melanogaster.The ubiquitin E3 ligase NOSIP modulates protein phosphatase 2A activity in craniofacial development.Microcystin-LR (MCLR) induces a compensation of PP2A activity mediated by α4 protein in HEK293 cells.Cardamonin Suppresses TGF-β1-Induced Epithelial Mesenchymal Transition via Restoring Protein Phosphatase 2A Expression MID1 catalyzes the ubiquitination of protein phosphatase 2A and mutations within its Bbox1 domain disrupt polyubiquitination of alpha4 but not of PP2Ac.Molecular dynamics simulation reveals insights into the mechanism of unfolding by the A130T/V mutations within the MID1 zinc-binding Bbox1 domain.TNF-related apoptosis-inducing ligand (TRAIL) regulates midline-1, thymic stromal lymphopoietin, inflammation, and remodeling in experimental eosinophilic esophagitis Mid1/Mid2 expression in craniofacial development and a literature review of X-linked opitz syndrome.FAM122A, a new endogenous inhibitor of protein phosphatase 2A Quantitative proteomics reveals novel protein interaction partners of PP2A catalytic subunit in pancreatic β-cells Proteomic differences between white and brown adipocytes.Dynamic ubiquitin signaling in cell cycle regulation.α4 is highly expressed in carcinogen-transformed human cells and primary human cancers.Identification and characterization of an alternatively spliced isoform of the human protein phosphatase 2Aα catalytic subunit Expression and regulation of type 2A protein phosphatases and alpha4 signalling in cardiac health and hypertrophy Novel involvement of RhebL1 in sphingosylphosphorylcholine-induced keratin phosphorylation and reorganization: Binding to and activation of AKT1.The E3 ubiquitin ligase midline 1 promotes allergen and rhinovirus-induced asthma by inhibiting protein phosphatase 2A activity.Discovery of new substrates of the elongation factor-2 kinase suggests a broader role in the cellular nutrient response.Mechanism of midline defect-causing mutation P151L in MID1 revealed.Structural and functional observations of the P151L MID1 mutation reveal alpha4 plays a significant role in X-linked Opitz Syndrome.HEK293 cells exposed to microcystin-LR show reduced protein phosphatase 2A activity and more stable cytoskeletal structure when overexpressing α4 protein.YdjC chitooligosaccharide deacetylase homolog induces keratin reorganization in lung cancer cells: involvement of interaction between YDJC and CDC16.

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Alpha4 is a ubiquitin-binding protein that regulates protein serine/threonine phosphatase 2A ubiquitination

http://www.wikidata.org/entity/Q30432991

description

2010 nî lūn-bûn

@nan

2010 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի մարտին հրատարակված գիտական հոդված

@hy

2010年の論文

@ja

2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Alpha4 is a ubiquitin-binding ...... phosphatase 2A ubiquitination

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Alpha4 is a ubiquitin-binding ...... phosphatase 2A ubiquitination

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type

label

Alpha4 is a ubiquitin-binding ...... phosphatase 2A ubiquitination

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Alpha4 is a ubiquitin-binding ...... phosphatase 2A ubiquitination

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prefLabel

Alpha4 is a ubiquitin-binding ...... phosphatase 2A ubiquitination

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Alpha4 is a ubiquitin-binding ...... phosphatase 2A ubiquitination

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Alpha4 is a ubiquitin-binding ...... phosphatase 2A ubiquitination

@en

P2093

Benjamin W Spiller

http://www.w3.org/2001/XMLSchema#string

Brian E Wadzinski

http://www.w3.org/2001/XMLSchema#string

Guy R Watkins

http://www.w3.org/2001/XMLSchema#string

Heidi S Franz

http://www.w3.org/2001/XMLSchema#string

Jamie L McConnell

http://www.w3.org/2001/XMLSchema#string

Lisa R McCorvey

http://www.w3.org/2001/XMLSchema#string

Sarah E Soss

http://www.w3.org/2001/XMLSchema#string

Walter J Chazin

http://www.w3.org/2001/XMLSchema#string

P2860

Identification of a PP2A-interacting protein that functions as a negative regulator of phosphatase activity in the ATM/ATR signaling pathway

Structure of the protein phosphatase 2A holoenzyme

Phosphorylation and microtubule association of the Opitz syndrome protein mid-1 is regulated by protein phosphatase 2A via binding to the regulatory subunit alpha 4.

Structure and ubiquitin binding of the ubiquitin-interacting motif

Solution structure of Vps27 UIM-ubiquitin complex important for endosomal sorting and receptor downregulation

The structure of Tap42/alpha4 reveals a tetratricopeptide repeat-like fold and provides insights into PP2A regulation

MID1, mutated in Opitz syndrome, encodes an ubiquitin ligase that targets phosphatase 2A for degradation

TAB2 and TAB3 activate the NF-kappaB pathway through binding to polyubiquitin chains

Alpha4 is an essential regulator of PP2A phosphatase activity

Regulation of protein serine-threonine phosphatase type-2A by tyrosine phosphorylation

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1713-1718

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scholarly article

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10.1021/BI901837H

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8

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49

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2010-03-01T00:00:00Z

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41110391

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20092282

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P921

protein ubiquitination

P932

2832797

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