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Nucleoside ester prodrug substrate specificity of liver carboxylesterase
Christopher P. Landowski
, Philip L. Lorenzi
, Xueqin Song
, Gordon L. Amidon
*
*
Corresponding author for this work
Not published at VTT
University of Michigan–Ann Arbor
Research output
:
Contribution to journal
›
Article
›
Scientific
›
peer-review
42
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Citations (Scopus)
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Keyphrases
Liver
100%
Substrate Specificity
100%
Nucleosides
100%
Carboxylesterase 1 (CES1)
100%
Ester Prodrug
100%
Prodrug
85%
Hydrolysis Rate
28%
Esters
28%
Binding Affinity
28%
Esterification
28%
Monoesters
28%
Nucleoside Analogues
28%
Floxuridine
28%
Promoiety
28%
Amino Acid Ester
28%
Hydrolytic Enzymes
14%
Amino Acids
14%
Esterase
14%
Broad-specificity
14%
Specific Activity
14%
Catalytic Efficiency
14%
High Catalytic Activity
14%
Bromo
14%
Therapeutic Action
14%
Initial Hydrolysis Rate
14%
Benzimidazole
14%
Porcine Liver
14%
Gemcitabine
14%
Structural Preference
14%
Amino Acid Ester Prodrug
14%
Gemcitabine Prodrug
14%
Prodrug Design
14%
Carbamate Prodrug
14%
INIS
substrates
100%
esters
100%
specificity
100%
liver
100%
nucleosides
100%
carboxylesterases
100%
enzymes
57%
amino acids
57%
hydrolysis
42%
efficiency
28%
affinity
28%
esterification
28%
comparative evaluations
14%
design
14%
esterases
14%
carbamates
14%
benzimidazoles
14%
Pharmacology, Toxicology and Pharmaceutical Science
Substrate Specificity
100%
Prodrug
100%
Carboxylesterase
100%
Nucleoside
100%
Amino Acid
36%
Floxuridine
18%
Aspartic Acid
18%
Gemcitabine
18%
Nucleoside Analog
18%
Esterase
9%
Hydrolase
9%
Carbamic Acid
9%
Proline Derivative
9%
Benzimidazole
9%
Combination Therapy
9%