Atomic structure at 2.5 Å resolution of uridine phosphorylase fromE. colias refined in the monoclinic crystal lattice-Reference-Cited by-同舟云学术

Atomic structure at 2.5 Å resolution of uridine phosphorylase fromE. colias refined in the monoclinic crystal lattice

Published:1995-06-26 Issue:2 Volume:367 Page:183-187
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Morgunova E.Yu.,Mikhailov A.M.,Popov A.N.,Blagova E.V.,Smirnova E.A.,Vainshtein B.K.,Mao Ch.,Armstrong Sh.R.,Ealick S.E.,Komissarov A.A.,Linkova E.V.,Burlakova A.A.,Mironov A.S.,Debabov V.G.

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(95)00489-V/fullpdf

Reference24 articles.

1. Uridine Phosphorylase from Escherichia coli. Physical and Chemical Characterization

2. Differential effects of 2,2'-anhydro-5-ethyluridine, a uridine phosphorylase inhibitor, on the antitumor activity of 5-fluorouridine and 5-fluoro-2'-deoxyuridine

3. Inhibition of uridine phosphorylase by pyrimidine nucleoside analogs and consideration of substrate binding to the enzyme based on solution conformation as seen by NMR spectroscopy

4. New analogues of benzylacyclouridines, specific and potent inhibitors of uridine phosphorylase from human and mouse livers

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