Results 1 to 10 of about 5,785,343 (209)

TRIM proteins in hepatocellular carcinoma [PDF]

open access: yesJournal of Biomedical Science, 2022
The tripartite motif (TRIM) protein family is a highly conserved group of E3 ligases with 77 members known in the human, most of which consist of a RING-finger domain, one or two B-box domains, and a coiled-coil domain.
Kan Lu   +5 more
doaj   +5 more sources

TRIM proteins: New players in virus-induced autophagy. [PDF]

open access: yesPLoS Pathogens, 2018
Autophagy is an evolutionarily conserved and intricately regulated cellular process in which damaged or aggregated proteins, organelles, and pathogen-derived components are engulfed by double-membrane structures, termed autophagosomes, and targeted for ...
Konstantin M J Sparrer, Michaela U Gack
doaj   +7 more sources

TRIMming Down Hormone-Driven Cancers: The Biological Impact of TRIM Proteins on Tumor Development, Progression and Prognostication [PDF]

open access: yesCells, 2021
The tripartite motif (TRIM) protein family is attracting increasing interest in oncology. As a protein family based on structure rather than function, a plethora of biological activities are described for TRIM proteins, which are implicated in multiple ...
Eleonora Pauletto   +4 more
doaj   +3 more sources

The Role and Mechanism of TRIM Proteins in Gastric Cancer [PDF]

open access: yesCells
Tripartite motif (TRIM) family proteins, distinguished by their N-terminal region that includes a Really Interesting New Gene (RING) domain with E3 ligase activity, two B-box domains, and a coiled-coil region, have been recognized as significant ...
Wangxi Wu   +4 more
doaj   +3 more sources

Exploring TRIM proteins’ role in antiviral defense against influenza A virus and respiratory coronaviruses [PDF]

open access: yesFrontiers in Cellular and Infection Microbiology
Numerous tripartite motif (TRIM) proteins, identified as E3 ubiquitin ligases, participate in various viral infections through ubiquitylation, ISGylation, and SUMOylation processes.
Ying Wei   +20 more
doaj   +3 more sources

Multipronged regulation of autophagy and apoptosis: emerging role of TRIM proteins [PDF]

open access: yesCellular & Molecular Biology Letters
TRIM proteins are characterized by their conserved N-terminal RING, B-box, and coiled-coil domains. These proteins are efficient regulators of autophagy, apoptosis, and innate immune responses and confer immunity against viruses and bacteria.
Nuzhat Ahsan   +5 more
doaj   +3 more sources

TRIM proteins: A 'swiss army knife' of antiviral immunity. [PDF]

open access: yesPLoS Pathogens
With their modular structure and E3 ubiquitin ligase activity, Tripartite motif (TRIM) proteins interact with a wide range of cellular and viral substrates. This review summarizes how they have emerged as key players in the antiviral response.
Elise Chabot   +2 more
doaj   +3 more sources

TRIM Proteins: Key Regulators of Immunity to Herpesvirus Infection [PDF]

open access: yesViruses
Herpesviruses are ubiquitous DNA viruses that can establish latency and cause a range of mild to life-threatening diseases in humans. Upon infection, herpesviruses trigger the activation of several host antiviral defense programs that play critical roles
Zuberwasim Sayyad   +2 more
doaj   +3 more sources

TRIM Proteins and Antiviral Microtubule Reorganization: A Novel Component in Innate Immune Responses? [PDF]

open access: yesViruses
TRIM proteins are a family of innate immune factors that play diverse roles in innate immunity and protect the cell against viral and bacterial aggression.
Charlotte Vadon   +2 more
doaj   +3 more sources

Identification and characterization of multiple TRIM proteins that inhibit hepatitis B virus transcription. [PDF]

open access: yesPLoS ONE, 2013
Tripartite motif (TRIM) proteins constitute a family of over 100 members that share conserved tripartite motifs and exhibit diverse biological functions. Several TRIM proteins have been shown to restrict viral infections and regulate host cellular innate
Shijian Zhang   +3 more
doaj   +3 more sources

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