Viral Protein Functions Study by Affinity Modification

Authors: Morozova O.V.; Safronov I.V.

Source: Mini Reviews in Medicinal Chemistry, Volume 1, Number 3, September 2001 , pp. 283-291(10)

Publisher: Bentham Science Publishers

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Abstract:

The knowledge of virus reproduction is necessary to design new safe drugs for inhibition of infections. Ultra-violet irradiation of virus proteins with labeled virus genome fragments permits to identify specific nucleic acid binding proteins. Affinity modification of enzymes with nucleotide derivatives could help to determine NTP-binding proteins and those involved in viral genome replication. Photoreactive analogues of nucleic acids are among the tools used to detect elongation subunits of replicative complexes. Affinity modification approach has already resulted in successful treatment of virus diseases.

Keywords: Viral Genomes; Proteins; Infuenza Virus trasnscriptase; Hiv reverse transcriptase; Avian myeloblastosis; Hiv reverse transcriptase

Language: English

Document Type: Review article

DOI: http://dx.doi.org/10.2174/1389557013406945

Publication date: 2001-09-01

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The aim of Mini-Reviews in Medicinal Chemistry is to publish short reviews on the important recent developments in medicinal chemistry and allied disciplines.

The scope of Mini-Reviews in Medicinal Chemistry will cover all areas of medicinal chemistry including developments in rational drug design, synthetic chemistry, bioorganic chemistry, high-throughput screening, combinatorial chemistry, drug targets, and natural product research and structure-activity relationship studies.

Mini-Reviews in Medicinal Chemistry is an essential journal for every medicinal and pharmaceutical chemist who wishes to be kept informed and up-to-date with the latest and most important developments.