Tripartite Motif Containing 22 (TRIM22) ELISA Kits

Rhesus Monkey Tripartite Motif Containing 22 (TRIM22) interaction partners

1. Data show that RNA interference abolished IFN-gamma-induced TRIM22 expression, indicating an IRF-1-dependent expression of TRIM22.

2. Study shows that human and rhesus TRIM22 localise to different subcellular compartments and that this difference can be assigned to the positively selected B30.2 domain.

Human Tripartite Motif Containing 22 (TRIM22) interaction partners

1. trim22 is a broad and multifunctional host anti-viral factor induced by interferons.

2. TRIM22 may act as epigenetic inhibitor of HIV-1 transcription by preventing the binding of the host cell transcription factor Sp1 to the viral promoter.

3. Upregulation of TRIM22 triggers the expression and oligomerization of Bak and subsequently leads to cytochrome c release in a caspase-9- and caspase-3-dependent manner. Both the RING domain and the SPRY domain of the TRIM22 molecule are associated with its pro-apoptotic function.

4. miR-215 facilitated HCV replication via inactivation of the NF-kappaB pathway by inhibiting TRIM22, providing a novel potential target for HCV infection.

5. Suppression of interferon-mediated anti-HBV response by single CpG methylation in the 5'-UTR of TRIM22.

6. Wthis study identified a genetic variation (rs7935564 G allele) in TRIM22 gene, which encodes TRIM22 protein acting like a HIV restriction factor, as being associated with good response to dendritic cell-based immunotherapy

7. TRIM5 and TRIM22 single nucleotide polymorphisms are associated to increased odds of significant liver fibrosis and sustained virological response after pegIFNalpha/RBV therapy in human immunodeficiency virus/hepatitis C virus coinfected patients.

8. Infant with severe IBD characterized by granulomatous colitis and severe perianal disease, we identified a homozygous variant of TRIM22 that affects the ability of its product to regulate NOD2.

9. Interferon-alpha-induced TRIM22 interrupts hepatitis c virus replication by ubiquitinating NS5A.

10. regulation of FoxO4 protein expression and cell survival by TRIM22 controls TLR3-mediated IFN type I gene induction, preventing excessive antiviral response through dsRNA-induced apoptosis.

11. TRIM22 could interact with IkappaB kinase (IKK)alpha but not IKKbeta and could increase the level and phosphorylation of IKKalpha through its really interesting new gene (RING) and spla-ryanodine receptor (SPRY) domains.

12. Demonstrated that TRIM22 acts as a negative regulator of HIV-1 replication via inhibition of basal Sp1-driven proviral transcription.

13. propose that TRIM22 is a direct target gene of PR and that it can mediate progesterone actions in uterine cells

14. Data show that capsid protein p24-DsRed-Monomer was co-localized with tripartite motif containing 22 (TRIM22)-EGFP in HEK293T cells.

15. A number of putative structural and functional residues, including several sites that undergo post-translational modification, were also identified in TRIM22.

16. our data characterize the extensive genetic variation in TRIM22 and identify rs1063303:G>C as a highly prevalent SNP that influences its function.

17. Upregulation of TRIM22 may be associated with responsiveness to Peg-IFNalpha-2a/RBV combination therapy in hepatitis C.

18. TRIM5alpha and TRIM22 have differential transcriptional regulation and distinct anti-HIV roles according to infection phase.

19. Data report that markers in two TRIMs, TRIM5 and TRIM22 and a marker in BST2, associated statistically with the risk of getting MS.

20. TRIM22 genetic diversity affects HIV-1 replication in vitro and it is a potentially novel determinant of HIV-1 disease severity