Influence of the Membrane Lipophilic Environment on the Structure and on the Substrate Access/Egress Routes of the Human Aromatase Enzyme. A Computational Study-Reference-Cited by-同舟云学术

Influence of the Membrane Lipophilic Environment on the Structure and on the Substrate Access/Egress Routes of the Human Aromatase Enzyme. A Computational Study

Published:2012-06-06 Issue:6 Volume:52 Page:1595-1606
ISSN:1549-9596
Container-title:Journal of Chemical Information and Modeling
language:en
Short-container-title:J. Chem. Inf. Model.

Author:

Sgrignani Jacopo¹,Magistrato Alessandra¹

Affiliation:

1. CNR-IOM-Democritos National Simulation Center c/o International Studies for Advanced Studies (SISSA/ISAS), via Bonomea 265, 34165 Trieste (TS), Italy

Publisher

American Chemical Society (ACS)

Subject

Library and Information Sciences,Computer Science Applications,General Chemical Engineering,General Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/ci300151h

Reference100 articles.

1. Engineering cytochrome P450 biocatalysts for biotechnology, medicine and bioremediation

2. Epitope Characterization of an Aromatase Monoclonal Antibody Suitable for the Assessment of Intratumoral Aromatase Activity

3. History of Aromatase: Saga of an Important Biological Mediator and Therapeutic Target

4. Aromatase Inhibitors in Breast Cancer: An Overview

Cited by 61 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. Influence of tumor microenvironment on the different breast cancer subtypes and applied therapies;Biochemical Pharmacology;2024-05

2. Structures and functions of human placental aromatase and steroid sulfatase, two key enzymes in estrogen biosynthesis;Steroids;2023-08

3. A Theoretical Study of Organotin Binding in Aromatase;International Journal of Molecular Sciences;2023-05-18

4. Key regulators in the architecture of substrate access/egress channels in mammalian cytochromes P450 governing flexibility in substrate oxyfunctionalization;Journal of Inorganic Biochemistry;2023-04

5. Single-digit nanomolar inhibitors lock the aromatase active site via a dualsteric targeting strategy;European Journal of Medicinal Chemistry;2022-12