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ProteomicsTRIM16 overexpression in HEK293T cells results in cell line-specific antiviral activity
In this paper we investigate one of the lesser studied TRIM family proteins, TRIM16, to determine if it might impact the ability of different viruses to replicate productively in host cells. TRIM16 is unique compared to other TRIM proteins in that it mediates E3 ligase activity despite lacking the c...
ORGANISM(S): Homo sapiens (Human) 
2023-06-21 | PXD039241 | Pride
Lc-ms Trim16 Antiviral 
ProteomicsLC-MS/MS identified the TRIM16-binding proteins
Vascular calcification (VC) is highly prevalent in patients with chronic kidney disease (CKD). To date, effective treatments for VC are still lacking since the underlying mechanisms remains elusive. RNA-sequencing analysis revealed that the E3 ubiquitin ligase Tripartite motif 16 (TRIM16) may be a k...
ORGANISM(S): Homo Sapiens 
2024-03-27 | PXD051036 |
Genomics
Liver tissue of Trim16-HKO and Trim16-Flox mice induced by HFHC diet for 16 weeks
PRJNA726824 | ENA
UnknownTRIM16 Overexpression in HEK293T Cells Results in Cell Line-Specific Antiviral Activity.
Not available
S-EPMC10301484 | biostudies-literature
UnknownTRIM16 inhibits neuroblastoma cell proliferation through cell cycle regulation and dynamic nuclear localization.
Not available
S-EPMC3637347 | biostudies-literature
UnknownTRIM16 inhibits proliferation and migration through regulation of interferon beta 1 in melanoma cells.
Not available
S-EPMC4259410 | biostudies-literature
UnknownTRIM16 facilitates SIRT-1-dependent regulation of antioxidant response to alleviate age-related sarcopenia.
Not available
S-EPMC11446700 | biostudies-literature
UnknownWithaferin A activates TRIM16 for its anti-cancer activity in melanoma.
Not available
S-EPMC7665169 | biostudies-literature
UnknownTRIM16 controls assembly and degradation of protein aggregates by modulating the p62-NRF2 axis and autophagy.
Not available
S-EPMC6138442 | biostudies-literature
UnknownTRIM16 promotes aerobic glycolysis and pancreatic cancer metastasis by modulating the NIK-SIX1 axis in a ligase-independent manner.
Not available
S-EPMC9729885 | biostudies-literature
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