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This process is done by another enzyme carried in the virus called integrase.
There are several ways to target integrase but strand transfer inhibition is the most common one.
The crystal structure of human foamy virus integrase has been examined successfully.
The integrase class of enzymes catalyse this particular reaction.
Other integrase inhibitors, like one from Gilead Sciences, are also under development.
MK-2048, a second generation integrase inhibitor, that appears to have a duration of action up to 4 times longer than raltegravir.
It is more potent than other previously known integrase inhibitors as well as causing less side effects.
Selective drug design is a possibility as HIV-1 integrase has no known cellular equivalent.
Studies have shown dolutegravir to be effective in patients with resistance to the integrase inhibitor, raltegravir.
Raltegravir is known as an integrase inhibitor.
It acts as an integrase inhibitor.
This new DNA is then incorporated into the host's genome by an integrase enzyme.
Each HIV particle has an estimated 40 to 100 copies of the integrase enzyme.
The translational frameshifting that produces the reverse transcriptase and integrase of a retrovirus.
DCM205, is a small molecule based on L-chicoric acid, an integrase inhibitor.
Another target is integrase, which splices the synthesized DNA into the host cell genome.
MK-2048 is a second generation integrase inhibitor, intended to be used against HIV infection.
During the integration process, the HIV integrase enzyme performs two key catalytic reactions.
Another clinically approved integrase inhibitor is Elvitegravir .
Initial treatment against HIV targets three key enzymes - reverse transcriptase, protease, and integrase.
Viral proteins involved in early stages of replication include Reverse Transcriptase and Integrase.
The first integrase inhibitor, raltegravir, was approved in 2007 and other drugs were in clinical trials in 2011.
Raltegravir and elvitegravir share the same mechanism of action against integrase which is to bind to the active site of Mg ions.
The C-terminus of the Ty retrotransposon's integrase contains an extension not seen in the retroviruses.
This reaction is the key step to for the synthesis of a HIV integrase inhibitor, Crixivan.