Results 41 to 50 of about 4,709 (168)

OVERVIEW OF CLASS-I TRIPARTITE MOTIF (TRIM) PROTEINS SPECIFICALLY TRIM67

open access: yesPakistan Journal of Agriculture, Agricultural Engineering and Veterinary Sciences
The TRIM family is a group of genes expressed during embryogenesis. This review emphasized data on Class-I TRIM genes, including TRIM1, TRIM9, TRIM36, TRIM46, TRIM67, TRIM18, and TRIM76. This article will discuss the structure and function of these genes and their roles in various physiological processes such as embryonic development, and immune ...
S. N. Panhwar   +6 more
openaire   +2 more sources

TRIM47 Regulates Energy Metabolism via Glycolytic Reprogramming to Drive Hepatocellular Carcinoma Progression and Represents an Efficient Therapeutic Target

open access: yesAdvanced Science, EarlyView.
This study identifies TRIM47 as a key driver of liver cancer progression by promoting glycolysis through ubiquitin‐mediated degradation of the gluconeogenic enzyme FBP1. TRIM47 enhances glucose uptake, lactate and ATP production, and tumor growth and metastasis.
Weijie Sun   +17 more
wiley   +1 more source

TRIM E3 ligases interfere with early and late stages of the retroviral life cycle.

open access: yesPLoS Pathogens, 2008
Members of the TRIpartite interaction Motif (TRIM) family of E3 ligases have been shown to exhibit antiviral activities. Here we report a near comprehensive screen for antiretroviral activities of 55 TRIM proteins (36 human, 19 mouse).
Pradeep D Uchil   +4 more
doaj   +1 more source

Dysfunctional TRIM31 of POMC Neurons Provokes Hypothalamic Injury and Peripheral Metabolic Disorder under Long‐Term Fine Particulate Matter Exposure

open access: yesAdvanced Science, EarlyView.
Particulate matter ≤2.5 µm (PM2.5) elevates risks of neurological and chronic metabolic diseases, but the underlying mechanisms linking PM2.5‐induced central nervous system (CNS) injury to metabolic dysfunction remain unclear. Hypothalamic pro‐opiomelanocortin‐expressing (POMC+) neurons regulate systemic metabolic homeostasis, and tripartite motif ...
Chenxu Ge   +21 more
wiley   +1 more source

TRIM proteins as emerging regulators of immune pathways: potential therapeutic targets in immune-related disorders

open access: yesFrontiers in Immunology
Tripartite motif (TRIM) proteins constitute a versatile family of E3 ubiquitin ligases that regulate key signaling pathways governing innate and adaptive immune responses.
Bilal Jawed   +13 more
doaj   +1 more source

TRIM21-dependent target protein ubiquitination mediates cell-free Trim-Away

open access: yesCell Reports, 2023
Summary: Tripartite motif-containing protein 21 (TRIM21) is a cytosolic antibody receptor and E3 ubiquitin ligase that promotes destruction of a broad range of pathogens.
Tycho E.T. Mevissen   +2 more
doaj   +1 more source

TRIM38 Suppresses Breast Cancer Progression via Modulating SQSTM1 Ubiquitination and Autophagic Flux

open access: yesAdvanced Science, EarlyView.
TRIM38, an E3 ubiquitin ligase, suppresses breast cancer progression by inhibiting proliferation, migration, and invasion. Downregulated in breast tumor, its loss correlates with poor prognosis. Mechanistically, TRIM38 mediates K63‐linked ubiquitination of SQSTM1/p62 at K420, disrupting SQSTM1‐LC3 interaction and blocking autophagic flux.
Shan Jiang   +14 more
wiley   +1 more source

Emerging roles of tripartite motif family proteins (TRIMs) in breast cancer

open access: yesCancer Medicine
AbstractBreast cancer (BC) is the most common malignant tumor worldwide. Despite enormous progress made in the past decades, the underlying mechanisms of BC remain further illustrated. Recently, TRIM family proteins proved to be engaged in BC progression through regulating various aspects.
Jianing Cao   +4 more
openaire   +3 more sources

Cleavage‐Resistant CYLD Protects Against Autoimmune Hepatitis

open access: yesAdvanced Science, EarlyView.
Proteolytic cleavage of the deubiquitinase CYLD emerges as a critical driver of autoimmune hepatitis. TNFα‐induced CYLD loss in macrophages amplifies S100A9‐triggered MAPK activation, leading to excessive chemokine production and hepatic inflammation. Pharmacological inhibition of MEK signaling effectively attenuates experimental disease, highlighting ...
Han Liu   +13 more
wiley   +1 more source

Functional Replacement of the RING, B-Box 2, and Coiled-Coil Domains of Tripartite Motif 5α (TRIM5α) by Heterologous TRIM Domains [PDF]

open access: yesJournal of Virology, 2006
ABSTRACT Tripartite motif 5α (TRIM5α) restricts some retroviruses, including human immunodeficiency virus type 1 (HIV-1), from infecting the cells of particular species. TRIM5α is a member of the TRIM family of proteins, which contain RING, B-box, coiled-coil (CC), and, in some cases, B30.2(SPRY) domains. Here we investigated the
Xing, Li   +6 more
openaire   +2 more sources

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