The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
Chemical Compound Review

BVdUTP     [[[(2R,3S,5R)-5-[5-[(E)-2- bromoethenyl]-2...

Synonyms: BV(5)Dutp, AC1O5PMZ, 77222-61-8, (E)-5-(2-Bromovinyl)-dUTP, E-5-Bromovinyl-2'-deoxyuridine triphosphate
 
 
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.
 

Disease relevance of BVdUTP

  • The Km for dTTP and the Ki for the BVdUTP of the HSV-1 DNA polymerase were 0.66 and 0.25 microM, respectively [1].
  • FIACTP was the most, and ACVTP the least effective inhibitor; BVdUTP was of intermediary potency; araCTP and araTTP had a greater inhibitory effect on DHBV DNA polymerase than HBV or WHV DNA polymerase [2].
 

High impact information on BVdUTP

  • These studies indicate that the ability of BVdUTP to preferentially inhibit the HSV-1 DNA polymerase may contribute towards its selective inhibition of the viral DNA replication in infected cells [1].
  • For instance, as little as 1 microM BVdUTP inhibited the utilization of dTTP by HSV-1 DNA polymerase 50%, whereas the same concentration inhibited the DNA polymerase alpha and the DNA polymerase beta activities only 9% and 3%, respectively [1].
  • These results indicate the usefulness of BVdUTP as a potent inhibitor of TdT for elucidation of the reaction mechanism of this enzyme [3].
 

Biological context of BVdUTP

  • BVdUTP was not an efficient substrate of TdT, but it inhibited the incorporation of normal deoxynucleotide substrates in competitive fashion at the nucleotide binding site of TdT molecule [3].

References

  1. On the mechanism of selective inhibition of herpesvirus replication by (E)-5-(2-bromovinyl)-2'-deoxyuridine. Allaudeen, H.S., Kozarich, J.W., Bertino, J.R., De Clercq, E. Proc. Natl. Acad. Sci. U.S.A. (1981) [Pubmed]
  2. Main properties of duck hepatitis B virus DNA polymerase: comparison with the human and woodchuck hepatitis B virus DNA polymerases. Fourel, I., Hantz, O., Cova, L., Allaudeen, H.S., Trepo, C. Antiviral Res. (1987) [Pubmed]
  3. Inhibition of terminal deoxynucleotidyltransferase by (E)-5-(2-bromovinyl)-2'-deoxyuridine 5'-triphosphate. Ono, K., Nakane, H., Colla, L., De Clercq, E. Nucleic Acids Symp. Ser. (1983) [Pubmed]
 
WikiGenes - Universities