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Related Concept Videos

Phase I Reactions: Reductive Reactions01:27

Phase I Reactions: Reductive Reactions

Phase I biotransformation reductive reactions are chemical processes that modify drugs by introducing or revealing polar functional groups via reduction. Enzymes called reductases catalyze these reactions, playing a pivotal role in drug metabolism by transforming lipophilic drugs into more polar, water-soluble metabolites for easy excretion. An essential type of reductive reaction is the carbonyl group reduction, where aldehydes and ketones are reduced to alcohols. An example is the...
Reduction of Alkenes: Asymmetric Catalytic Hydrogenation02:17

Reduction of Alkenes: Asymmetric Catalytic Hydrogenation

Catalytic hydrogenation of alkenes is a transition-metal catalyzed reduction of the double bond using molecular hydrogen to give alkanes. The mode of hydrogen addition follows syn stereochemistry.
The metal catalyst used can be either heterogeneous or homogeneous. When hydrogenation of an alkene generates a chiral center, a pair of enantiomeric products is expected to form. However, an enantiomeric excess of one of the products can be facilitated using an enantioselective reaction or an...
Drug Metabolism: Phase I Reactions01:17

Drug Metabolism: Phase I Reactions

A phase I reaction is a biochemical process that introduces a functionally reactive polar group to a substance. This transformation predominantly occurs in the liver, facilitated by the cytochrome P450 system of hemoproteins situated in the lipophilic endoplasmic reticulum of cells. The metabolite generated through this process can have varying polarities. If it is sufficiently polar, it can be easily excreted in the urine due to its water compatibility. However, if the metabolite is nonpolar,...
Protein Modifications in the RER01:26

Protein Modifications in the RER

Modification of secretory and transmembrane proteins entering the rough ER begins in the ER lumen. These modifications aid in protein folding and stabilize the acquired tertiary structure. Protein modifications in the rough ER co-occur at different stages of protein folding.
Broadly, these modifications can be categorized into four main categories — glycosylation, formation of disulfide bonds, assembly of protein subunits, and specific proteolytic cleavages like removal of signal sequences.
Pharmacogenetics of Drug Targets: β₂-Adrenergic Receptors, Apo E, Thymidylate Synthase01:11

Pharmacogenetics of Drug Targets: β₂-Adrenergic Receptors, Apo E, Thymidylate Synthase

Genetic polymorphisms in drug targets have emerged as critical determinants of interindividual variability in drug response and toxicity. Pharmacogenomic investigations increasingly focus on identifying these variations to personalize and optimize therapeutic interventions. A drug target may be a receptor, enzyme, or signaling protein involved in pharmacologic responses or disease-related pathways. While early pharmacogenetic studies focused primarily on drug metabolism, current research...
Transducer Mechanism: Nuclear Receptors01:31

Transducer Mechanism: Nuclear Receptors

Nuclear receptors, or NRs, are unique transcription factors that regulate gene transcription and affect the cellular pathways involved in reproduction, development, or metabolism. Their ability to be stimulated by small lipophilic ligands and control vital cellular processes makes them ideal drug targets. Nearly 10-15% of currently prescribed drugs target these receptors.
About 48 different soluble family members of nuclear receptors are identified that can be divided into two main classes:

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Related Experiment Video

Updated: Jun 18, 2026

Systems Biology of Metabolic Regulation by Estrogen Receptor Signaling in Breast Cancer
10:36

Systems Biology of Metabolic Regulation by Estrogen Receptor Signaling in Breast Cancer

Published on: March 17, 2016

Sequence-function correlation of aromatase and its interaction with reductase.

Yanyan Hong1, Hongzhi Li, Yate-Ching Yuan

  • 1Division of Tumor Cell Biology, Beckman Research Institute of the City of Hope, Duarte, CA 91010, USA.

The Journal of Steroid Biochemistry and Molecular Biology
|December 1, 2009
PubMed
Summary

Investigating aromatase enzyme structure and its interaction with NADPH-cytochrome P450 reductase (CPR) is key for developing new breast cancer inhibitors. Understanding these relationships can lead to novel treatments targeting estrogen production.

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Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
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Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

Published on: December 19, 2018

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Last Updated: Jun 18, 2026

Systems Biology of Metabolic Regulation by Estrogen Receptor Signaling in Breast Cancer
10:36

Systems Biology of Metabolic Regulation by Estrogen Receptor Signaling in Breast Cancer

Published on: March 17, 2016

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay
09:07

Detecting the Ligand-binding Domain Dimerization Activity of Estrogen Receptor Alpha Using the Mammalian Two-Hybrid Assay

Published on: December 19, 2018

Area of Science:

  • Biochemistry
  • Enzymology
  • Molecular Biology

Background:

  • Aromatase, a cytochrome P450 enzyme, catalyzes androgen to estrogen conversion, crucial for estrogen-dependent breast tumor growth.
  • Estrogen's role in breast cancer necessitates understanding aromatase function and developing targeted therapies.
  • Aromatase interacts with NADPH-cytochrome P450 reductase (CPR) for its enzymatic activity.

Purpose of the Study:

  • To summarize current progress in analyzing the sequence-function relationship of the aromatase protein family.
  • To characterize the molecular interactions between aromatase and its partner, CPR.
  • To explore novel therapeutic strategies targeting the aromatase-CPR complex.

Main Methods:

  • Sequence-function correlation analysis of aromatase proteins.
  • Molecular characterization of the aromatase-CPR interaction.
  • Review of existing research on aromatase inhibitors.

Main Results:

  • Aromatase is conserved across vertebrates, with variations in catalytic efficiency (Km, Vmax) across species.
  • Detailed insights into the molecular mechanisms of aromatase-CPR complex formation.
  • Identification of potential targets for novel inhibitor development.

Conclusions:

  • Understanding aromatase structure-function and its interaction with CPR is vital for breast cancer therapy.
  • Novel inhibitors targeting the aromatase-CPR interaction could offer new treatment avenues.
  • Further research in this area promises advancements in combating estrogen-driven breast cancers.