Literature DB >> 11333162

A phosphodiesterase from ascites carcinoma Krebs II cells specifically cleaves the bond between VPg and RNA of encephalomyocarditis virus.

A Y Gulevich1, R A Yusupova, Y F Drygin.   

Abstract

The substrate specificity of the "unlinking" enzyme from ascite carcinoma Krebs II cells has been investigated. The enzyme specifically splits the interpolymeric phosphodiester bond between Kp and the 5;-terminal phosphate group of the uridylic acid residue in the Kp-pUpUpGp complex.

Entities:  

Mesh:

Substances:

Year:  2001        PMID: 11333162     DOI: 10.1023/a:1010220401336

Source DB:  PubMed          Journal:  Biochemistry (Mosc)        ISSN: 0006-2979            Impact factor:   2.487


  2 in total

1.  VPg unlinkase/TDP2 in cardiovirus infected cells: Re-localization and proteolytic cleavage.

Authors:  Sonia Maciejewski; Wendy Ullmer; Bert L Semler
Journal:  Virology       Date:  2018-01-30       Impact factor: 3.616

2.  An RNA virus hijacks an incognito function of a DNA repair enzyme.

Authors:  Richard Virgen-Slane; Janet M Rozovics; Kerry D Fitzgerald; Tuan Ngo; Wayne Chou; Gerbrand J van der Heden van Noort; Dmitri V Filippov; Paul D Gershon; Bert L Semler
Journal:  Proc Natl Acad Sci U S A       Date:  2012-08-20       Impact factor: 11.205

  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.