What question did this study set out to answer?

To synthesize current knowledge on the structural, catalytic, and biological characteristics of human carboxylesterases CES1 and CES2 and their significance in xenobiotic metabolism and drug discovery.

June 25, 2018Acta Pharmaceutica Sinica BOpen Access

Human carboxylesterases: a comprehensive review

View Full Paper

Ask AI

Bookmark

Authors

DWDandan WangPeking University LZLi‐Wei ZouLinyi University QJQiang JinShanghai University of Traditional Chinese Medicine

Discussion

Member takes

Implication

Comprehensive review reveals the catalytic mechanisms and metabolic roles of CES1 and CES2 in humans, highlighting strategies for prodrug design and enzyme modulation.

Key Points

To synthesize current knowledge on the structural, catalytic, and biological characteristics of human carboxylesterases CES1 and CES2 and their significance in xenobiotic metabolism and drug discovery.
Synthesized findings regarding the structural features, catalytic mechanisms, and tissue distributions of human CES1 and CES2.
Evaluated genetic polymorphisms, substrate preferences, and inhibitor profiles governing both carboxylesterase isoforms.
Examined pharmacological advancements in developing isoform-selective modulators and prodrugs activated by carboxylesterases.
Demonstrated that CES1 and CES2 exhibit distinct tissue-expression profiles and complementary substrate specificities for endogenous lipids, ester-containing pharmaceuticals, and environmental toxicants.
Showed that genetic polymorphisms and selective chemical inhibition significantly alter carboxylesterase catalytic activity, driving inter-individual variability in drug efficacy and toxicity.
Identified isoform-specific structural determinants that enable medicinal chemistry approaches to design targeted prodrugs and selective therapeutic modulators.

Cite This Study

Wang et al. (2018) studied this question.

synapsesocial.com/papers/69efcaa4daa5208b6cb0bb58 https://doi.org/10.1016/j.apsb.2018.05.005

View Full Paper

Ask AI

Bookmark

June 25, 2018Acta Pharmaceutica Sinica BOpen Access

Human carboxylesterases: a comprehensive review

View Full Paper

Ask AI

Bookmark

Authors

DWDandan WangPeking University LZLi‐Wei ZouLinyi University QJQiang JinShanghai University of Traditional Chinese Medicine

Discussion

Member takes

Implication

Comprehensive review reveals the catalytic mechanisms and metabolic roles of CES1 and CES2 in humans, highlighting strategies for prodrug design and enzyme modulation.

Key Points

To synthesize current knowledge on the structural, catalytic, and biological characteristics of human carboxylesterases CES1 and CES2 and their significance in xenobiotic metabolism and drug discovery.
Synthesized findings regarding the structural features, catalytic mechanisms, and tissue distributions of human CES1 and CES2.
Evaluated genetic polymorphisms, substrate preferences, and inhibitor profiles governing both carboxylesterase isoforms.
Examined pharmacological advancements in developing isoform-selective modulators and prodrugs activated by carboxylesterases.
Demonstrated that CES1 and CES2 exhibit distinct tissue-expression profiles and complementary substrate specificities for endogenous lipids, ester-containing pharmaceuticals, and environmental toxicants.
Showed that genetic polymorphisms and selective chemical inhibition significantly alter carboxylesterase catalytic activity, driving inter-individual variability in drug efficacy and toxicity.
Identified isoform-specific structural determinants that enable medicinal chemistry approaches to design targeted prodrugs and selective therapeutic modulators.

Cite This Study

Wang et al. (2018) studied this question.

synapsesocial.com/papers/69efcaa4daa5208b6cb0bb58 https://doi.org/10.1016/j.apsb.2018.05.005

Also Consider

Synapse has enriched 4 closely related papers on similar clinical questions. Consider them for comparative context:

View Full Paper

Ask AI

Bookmark