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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Tripartite motif containing 38

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1 and a B-box type 2, and a coiled-coil region. The function of this protein has not been identified. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Trim, Ubiquitin, HAD, TLR3, Phosphogluconate Dehydrogenase
Papers on RNF15
Primary Sjögren's syndrome patients with autoantibodies against TRIM38 show greater severity of disease.
Deshmukh et al., Bogotá, Colombia. In Arthritis Rheumatol, Jan 2016
This study investigates the frequency of anti-TRIM38 in pSjS patients and evaluates its association with different clinical measures of the disease.
TRIM38 Negatively Regulates TLR3/4-Mediated Innate Immune and Inflammatory Responses by Two Sequential and Distinct Mechanisms.
Shu et al., Wuhan, China. In J Immunol, Dec 2015
In this study, we show that Trim38 deficiency markedly increased TLR3- and TLR4-mediated induction of type I IFNs and proinflammatory cytokines, such as TNF-α, IL-1β, and IL-6, in immune cells and in vivo.
TRIM38 inhibits TNFα- and IL-1β-triggered NF-κB activation by mediating lysosome-dependent degradation of TAB2/3.
Shu et al., Wuhan, China. In Proc Natl Acad Sci U S A, 2014
Here, we identify tripartite-motif protein 38 (TRIM38) as a critical negative regulator of TNFα- and IL-1β-triggered signaling.
Tripartite motif-containing protein 38 negatively regulates TLR3/4- and RIG-I-mediated IFN-β production and antiviral response by targeting NAP1.
Gao et al., Jinan, China. In J Immunol, 2012
In the current study, we identified a member of the tripartite motif (TRIM) family, TRIM38, as a negative regulator in TLR3/4- and RIG-I-mediated IFN-β signaling.
E3 ubiquitin ligase tripartite motif 38 negatively regulates TLR-mediated immune responses by proteasomal degradation of TNF receptor-associated factor 6 in macrophages.
Gao et al., Jinan, China. In J Immunol, 2012
TRIM38 was induced by TLR stimulation in an NF-κB-dependent manner in macrophages.
TRIM38 negatively regulates TLR3-mediated IFN-β signaling by targeting TRIF for degradation.
Hung et al., Beijing, China. In Plos One, 2011
Although it has been shown that TRIM38 negatively regulates innate immunity, the mechanisms by which it does so have not been fully addressed.
[Identification A novel protein TRIM38 that activate NF-kappaB signaling pathways].
Hong et al., Beijing, China. In Zhonghua Shi Yan He Lin Chuang Bing Du Xue Za Zhi, 2011
NF-kappaB is activated in response to TRIM38.
Enterovirus 71 induces degradation of TRIM38, a potential E3 ubiquitin ligase.
Hung et al., Beijing, China. In Virol J, 2010
Enterovirus 71 infection induces degradation of TRIM38.
Quantitative analysis of human tissue-specific differences in methylation.
Nagase et al., Tokyo, Japan. In Biochem Biophys Res Commun, 2008
However, a positive correlation was seen at tDMRs located near the TRIM38 and CASZ1 genes.
The 52 000 MW Ro/SS-A autoantigen in Sjögren's syndrome/systemic lupus erythematosus (Ro52) is an interferon-gamma inducible tripartite motif protein associated with membrane proximal structures.
Trowsdale et al., Cambridge, United Kingdom. In Immunology, 2002
The majority of these autoimmune sera also immunoprecipitated the Ro52-related molecule RNF15.
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