Literature summary for 3.1.13.2 extracted from

Li, N.; Wang, Y.; Pothukuchy, A.; Syrett, A.; Husain, N.; Gopalakrisha, S.; Kosaraju, P.; Ellington, A.D.
Aptamers that recognize drug-resistant HIV-1 reverse transcriptase (2008), Nucleic Acids Res., 36, 6739-6751.

Search for more literature for 3.1.13.2

Protein Variants

Protein Variants	Comment	Organism
additional information	mutations in the polymerase domain can affect RNase H activity by affecting the position of the template-primer or the structure of the RNase H domain itself. Aptamer inhibition of RNase H activity. Aptamer 12.01 and Aptamer M302 at varying concentrations (0, 50, 200, 1000 nM) are incubated with radiolabeled primer and an RNA template. Aptamers do not inhibit the RNase H activity of wild-type HIV-1 reverse transcriptase	Human immunodeficiency virus 1

Organism

Organism	UniProt	Comment	Textmining
Human immunodeficiency virus 1	P03366	-	-

Synonyms

Synonyms	Comment	Organism
RNase H	wild-type HIV-1 reverse transcriptase has both DNA polymerase activity and RNase H activity	Human immunodeficiency virus 1

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)