Functional interactions between ubiquitin E2 enzymes and TRIM proteins. - Wikidata - awgldk - TriplyDB

Functional interactions between ubiquitin E2 enzymes and TRIM proteins.

Functional interactions between ubiquitin E2 enzymes and TRIM proteins.

http://www.wikidata.org/entity/Q39807649

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Rapid-throughput skeletal phenotyping of 100 knockout mice identifies 9 new genes that determine bone strength TRIM27 negatively regulates NOD2 by ubiquitination and proteasomal degradation Tripartite motif containing protein 27 negatively regulates CD4 T cells by ubiquitinating and inhibiting the class II PI3K-C2β Ubiquitylation as a Rheostat for TCR Signaling: From Targeted Approaches Toward Global Profiling Role of E2-Ub-conjugating enzymes during skeletal muscle atrophy TRIM3 regulates the motility of the kinesin motor protein KIF21B The ability of TRIM3 to induce growth arrest depends on RING-dependent E3 ligase activity Functional role of TRIM E3 ligase oligomerization and regulation of catalytic activity.Skeletal muscle atrophy and the E3 ubiquitin ligases MuRF1 and MAFbx/atrogin-1 TRIM38 negatively regulates TLR3-mediated IFN-β signaling by targeting TRIF for degradation.The E3 ubiquitin ligase MID1 catalyzes ubiquitination and cleavage of Fu.The RNA helicase DDX6 regulates cell-fate specification in neural stem cells via miRNAs.TRIM32 Senses and Restricts Influenza A Virus by Ubiquitination of PB1 Polymerase Satellite cell senescence underlies myopathy in a mouse model of limb-girdle muscular dystrophy 2H.Loss of TRIM62 expression is an independent adverse prognostic factor in acute myeloid leukemia Duck TRIM27-L enhances MAVS signaling and is absent in chickens and turkeys.TRIM32 modulates pluripotency entry and exit by directly regulating Oct4 stability Nrdp1S, short variant of Nrdp1, inhibits human glioma progression by increasing Nrdp1-mediated ErbB3 ubiquitination and degradation Tripartite motif ligases catalyze polyubiquitin chain formation through a cooperative allosteric mechanism.UBE2B is implicated in myofibrillar protein loss in catabolic C2C12 myotubes.Disuse-induced muscle wasting.Oligomerization of the Nrdp1 E3 ubiquitin ligase is necessary for efficient autoubiquitination but not ErbB3 ubiquitination.TRIM family: Pleiotropy and diversification through homomultimer and heteromultimer formation.TRIMmunity: the roles of the TRIM E3-ubiquitin ligase family in innate antiviral immunity.Midline2 is overexpressed and a prognostic indicator in human breast cancer and promotes breast cancer cell proliferation in vitro and in vivo.Upregulated Expression of TRIM32 Is Involved in Schwann Cell Differentiation, Migration and Neurite Outgrowth After Sciatic Nerve Crush.Overlapping and distinct molecular determinants dictating the antiviral activities of TRIM56 against flaviviruses and coronavirus.Targeted deep resequencing identifies MID2 mutation for X-linked intellectual disability with varied disease severity in a large kindred from India.The E3-ligase TRIM family of proteins regulates signaling pathways triggered by innate immune pattern-recognition receptors The TRIMendous Role of TRIMs in Virus-Host Interactions.The ND10 Component Promyelocytic Leukemia Protein Acts as an E3 Ligase for SUMOylation of the Major Immediate Early Protein IE1 of Human Cytomegalovirus.Phosphatidylinositol-3-kinase C2β and TRIM27 function to positively and negatively regulate IgE receptor activation of mast cells.A muscle-specific MuRF1-E2 network requires stabilization of MuRF1-E2 complexes by telethonin, a newly identified substrate.TRIM8: Making the Right Decision between the Oncogene and Tumour Suppressor Role.Conserved structural and functional aspects of the tripartite motif gene family point towards therapeutic applications in multiple diseases.Role of the tripartite motif protein 27 in cancer development.Deletion of TRIM32 protects mice from anxiety- and depression-like behaviors under mild stress.Structural and functional characterization of hMEX-3C Ring finger domain as an E3 ubiquitin ligase

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P2860

Functional interactions between ubiquitin E2 enzymes and TRIM proteins.

http://www.wikidata.org/entity/Q39807649

description

2011 nî lūn-bûn

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2011年の論文

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2011年学术文章

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2011年学术文章

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2011年学术文章

@zh-hans

2011年学术文章

@zh-my

2011年学术文章

@zh-sg

2011年學術文章

@yue

2011年學術文章

@zh

2011年學術文章

@zh-hant

name

Functional interactions between ubiquitin E2 enzymes and TRIM proteins.

@en

Functional interactions between ubiquitin E2 enzymes and TRIM proteins.

@nl

type

label

Functional interactions between ubiquitin E2 enzymes and TRIM proteins.

@en

Functional interactions between ubiquitin E2 enzymes and TRIM proteins.

@nl

prefLabel

Functional interactions between ubiquitin E2 enzymes and TRIM proteins.

@en

Functional interactions between ubiquitin E2 enzymes and TRIM proteins.

@nl

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Biochemical Journal

P1476

Functional interactions between ubiquitin E2 enzymes and TRIM proteins

@en

P2093

Ellis G Jaffray

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

Germana Meroni

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

P2860

Genomic analysis of the TRIM family reveals two groups of genes with distinct evolutionary properties

RET finger protein is a transcriptional repressor and interacts with enhancer of polycomb that has dual transcriptional functions

The tripartite motif family identifies cell compartments.

E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1)

E2-BRCA1 RING interactions dictate synthesis of mono- or specific polyubiquitin chain linkages

The interaction of Piasy with Trim32, an E3-ubiquitin ligase mutated in limb-girdle muscular dystrophy type 2H, promotes Piasy degradation and regulates UVB-induced keratinocyte apoptosis through NFkappaB

Autoantigen Ro52 is an E3 ubiquitin ligase

TRIM11 binds to and destabilizes a key component of the activator-mediated cofactor complex (ARC105) through the ubiquitin-proteasome system

TRIM32 is an E3 ubiquitin ligase for dysbindin

An altered-specificity ubiquitin-conjugating enzyme/ubiquitin-protein ligase pair

P304

309-319

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scholarly article

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10.1042/BJ20101487

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2

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434

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Luisa Maria Rosaria Napolitano

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2011-03-01T00:00:00Z

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21143188

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