Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Purine nucleoside phosphorylase: a target for drug design.

Literature DB >> 8483336

Purine nucleoside phosphorylase: a target for drug design.

J A Montgomery¹.

Abstract

Entities: Gene

Mesh：

Substances：

Year: 1993 PMID： 8483336 DOI： 10.1002/med.2610130302

Source DB: PubMed Journal: Med Res Rev ISSN： 0198-6325 Impact factor: 12.944

Keyword Cloud
Cited

× No keyword cloud information.

11 in total

1. Identification of the tautomeric form of formycin A in its complex with Escherichia coli purine nucleoside phosphorylase based on the effect of enzyme-ligand binding on fluorescence and phosphorescence.

Authors: Jakub Włodarczyk; Gerasim Stoychev Galitonov; Borys Kierdaszuk
Journal: Eur Biophys J Date: 2003-12-04 Impact factor: 1.733

2. Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues.

Authors: Agnes Rinaldo-Matthis; Corin Wing; Mahmoud Ghanem; Hua Deng; Peng Wu; Arti Gupta; Peter C Tyler; Gary B Evans; Richard H Furneaux; Steven C Almo; Ching C Wang; Vern L Schramm
Journal: Biochemistry Date: 2007-01-23 Impact factor: 3.162

Review 3. Structural analyses reveal two distinct families of nucleoside phosphorylases.

Authors: Matthew J Pugmire; Steven E Ealick
Journal: Biochem J Date: 2002-01-01 Impact factor: 3.857

4. A₃- and A₂B-fluorocorroles: synthesis, X-ray characterization and antiviral activity evaluation against human cytomegalovirus infection.

Authors: Sandrine Kappler-Gratias; Léo Bucher; Nicolas Desbois; Yoann Rousselin; Kerstin Bystricky; Claude P Gros; Franck Gallardo
Journal: RSC Med Chem Date: 2020-07-13

Purine nucleoside phosphorylase: a target for drug design.

1. Identification of the tautomeric form of formycin A in its complex with Escherichia coli purine nucleoside phosphorylase based on the effect of enzyme-ligand binding on fluorescence and phosphorescence.

2. Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues.

Review 3. Structural analyses reveal two distinct families of nucleoside phosphorylases.

4. A₃- and A₂B-fluorocorroles: synthesis, X-ray characterization and antiviral activity evaluation against human cytomegalovirus infection.

5. Structure of grouper iridovirus purine nucleoside phosphorylase.

Review 6. Enzymology of purine and pyrimidine antimetabolites used in the treatment of cancer.

Review 7. Enzymatic Transition States and Drug Design.

Review 8. Acyclic nucleosides as antiviral compounds.

9. Crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with acyclovir.

10. Cytomegalovirus protease targeted prodrug development.

Purine nucleoside phosphorylase: a target for drug design.

1. Identification of the tautomeric form of formycin A in its complex with Escherichia coli purine nucleoside phosphorylase based on the effect of enzyme-ligand binding on fluorescence and phosphorescence.

2. Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues.

Review 3. Structural analyses reveal two distinct families of nucleoside phosphorylases.

4. A3- and A2B-fluorocorroles: synthesis, X-ray characterization and antiviral activity evaluation against human cytomegalovirus infection.

5. Structure of grouper iridovirus purine nucleoside phosphorylase.

Review 6. Enzymology of purine and pyrimidine antimetabolites used in the treatment of cancer.

Review 7. Enzymatic Transition States and Drug Design.

Review 8. Acyclic nucleosides as antiviral compounds.

9. Crystal structure of Escherichia coli purine nucleoside phosphorylase complexed with acyclovir.

10. Cytomegalovirus protease targeted prodrug development.

4. A₃- and A₂B-fluorocorroles: synthesis, X-ray characterization and antiviral activity evaluation against human cytomegalovirus infection.