TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members - Wikidata - awgldk - TriplyDB

TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members

TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members

http://www.wikidata.org/entity/Q34281910

about

TRIM-mediated precision autophagy targets cytoplasmic regulators of innate immunity XLOS-observed mutations of MID1 Bbox1 domain cause domain unfolding.Subtractive screen of potential limb regeneration related genes from Pachytriton brevipes.TRIM16 overexpression induces apoptosis through activation of caspase-2 in cancer cells.TRIM16 inhibits neuroblastoma cell proliferation through cell cycle regulation and dynamic nuclear localization The MID1 E3 ligase catalyzes the polyubiquitination of Alpha4 (α4), a regulatory subunit of protein phosphatase 2A (PP2A): novel insights into MID1-mediated regulation of PP2A.TRIM25 Identification in the Chinese Goose: Gene Structure, Tissue Expression Profiles, and Antiviral Immune Responses In Vivo and In Vitro.Multifaceted roles of TRIM38 in innate immune and inflammatory responses.Regulation of the tumor suppressor PML by sequential post-translational modifications.TRIMmunity: the roles of the TRIM E3-ubiquitin ligase family in innate antiviral immunity.Bromodomains and their pharmacological inhibitors.TRIM family proteins: emerging class of RING E3 ligases as regulator of NF-κB pathway.Molecular basis for the fold organization and sarcomeric targeting of the muscle atrogin MuRF1 TRIM16 inhibits proliferation and migration through regulation of interferon beta 1 in melanoma cells.Ubiquitin enzymes in the regulation of immune responses.The TRIMendous Role of TRIMs in Virus-Host Interactions.TRIMs and Galectins Globally Cooperate and TRIM16 and Galectin-3 Co-direct Autophagy in Endomembrane Damage Homeostasis.Knockdown of TRIM65 inhibits lung cancer cell proliferation, migration and invasion: A therapeutic target in human lung cancer GM-CSF overexpression after influenza a virus infection prevents mortality and moderates M1-like airway monocyte/macrophage polarization.TRIM proteins in blood cancers.TRIM16 controls assembly and degradation of protein aggregates by modulating the p62-NRF2 axis and autophagy Structural and functional characterization of hMEX-3C Ring finger domain as an E3 ubiquitin ligase

P2860

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P2860

TRIM16 acts as an E3 ubiquitin ligase and can heterodimerize with other TRIM family members

http://www.wikidata.org/entity/Q34281910

description

2012 nî lūn-bûn

@nan

2012 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2012 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2012年の論文

@ja

2012年論文

@yue

2012年論文

@zh-hant

2012年論文

@zh-hk

2012年論文

@zh-mo

2012年論文

@zh-tw

2012年论文

@wuu

name

TRIM16 acts as an E3 ubiquitin ...... with other TRIM family members

@ast

TRIM16 acts as an E3 ubiquitin ...... with other TRIM family members

@en

TRIM16 acts as an E3 ubiquitin ...... with other TRIM family members

@nl

type

label

TRIM16 acts as an E3 ubiquitin ...... with other TRIM family members

@ast

TRIM16 acts as an E3 ubiquitin ...... with other TRIM family members

@en

TRIM16 acts as an E3 ubiquitin ...... with other TRIM family members

@nl

prefLabel

TRIM16 acts as an E3 ubiquitin ...... with other TRIM family members

@ast

TRIM16 acts as an E3 ubiquitin ...... with other TRIM family members

@en

TRIM16 acts as an E3 ubiquitin ...... with other TRIM family members

@nl

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JOURNAL.PONE.0037470

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P1476

TRIM16 acts as an E3 ubiquitin ...... with other TRIM family members

@en

P2093

Alena Malyukova

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

Belamy B Cheung

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

Glenn M Marshall

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

Jessica K Holien

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

Jessica Koach

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

Jessica L Bell

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

Maria Kavallaris

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

P2860

A RA-dependent, tumour-growth suppressive transcription complex is the target of the PML-RARalpha and T18 oncoproteins

The tripartite motif family identifies cell compartments.

TRIM16 acts as a tumour suppressor by inhibitory effects on cytoplasmic vimentin and nuclear E2F1 in neuroblastoma cells

Ret finger protein is a normal component of PML nuclear bodies and interacts directly with PML

The solution structure of the RING finger domain from the acute promyelocytic leukaemia proto-oncoprotein PML

The estrogen-responsive B box protein (EBBP) restores retinoid sensitivity in retinoid-resistant cancer cells via effects on histone acetylation

The estrogen-responsive B box protein is a novel regulator of the retinoid signal

Active transport of the ubiquitin ligase MID1 along the microtubules is regulated by protein phosphatase 2A

Solution structure of the MID1 B-box2 CHC(D/C)C(2)H(2) zinc-binding domain: insights into an evolutionarily conserved RING fold

Structure of the MID1 tandem B-boxes reveals an interaction reminiscent of intermolecular ring heterodimers

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e37470

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scholarly article

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10.1371/JOURNAL.PONE.0037470

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P407

P433

5

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P478

7

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P50

Michael W Parker

P577

2012-05-21T00:00:00Z

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

P5875

225061069

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22629402

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

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3357404

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