Disease relevance of TRIAD3

• The possible mechanisms by which ZIN interferes with the early events of HIV-1 replication are discussed [1].
• It was further shown that cells infected with HIV NL4.3 virus stocks produced in the presence of exogenously expressed ZIN were impaired in viral DNA synthesis by twofold [1].

High impact information on TRIAD3

• Domain mapping experiments indicate that the RING-like zinc finger domains of ZIN are required for its interaction with RIP and inhibition of RIP-mediated NF-kappa B activation [2].
• Overexpression of ZIN also potentiates RIP- and TNF-induced apoptosis [2].
• We previously reported the isolation of a Vif-interacting ring finger protein, Triad 3, from a human leukocyte cDNA library, using the yeast two-hybrid system [1].
• RESULTS: Thus far 3 of these clones, spermine/spermidine N1-acetyltransferase, Triad 3 and a novel gene which we have termed 'novel Vif binding protein', have been characterised and represent attractive candidates for mediating Vif action during HIV replication [3].
• ZIN was associated with minimal pulpal changes and microbial microleakage, and differed little from the control material, Kalzinol [4].

Biological context of TRIAD3

• ZIN contains four RING-like zinc finger domains at the middle and a proline-rich domain at the C terminus [2].

Analytical, diagnostic and therapeutic context of TRIAD3

• Sequence analysis indicates that Triad 3 protein contains all four major ring-like motifs of ZIN [1].

References