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Relevant bibliographies by topics / Estrogen Molecular structures

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Academic literature on the topic 'Estrogen Molecular structures'

Author: Grafiati

Published: 4 June 2021

Last updated: 13 February 2022

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Journal articles on the topic "Estrogen Molecular structures"

1

Nilsson, Stefan, Sari Mäkelä, Eckardt Treuter, et al. "Mechanisms of Estrogen Action." Physiological Reviews 81, no. 4 (2001): 1535–65. http://dx.doi.org/10.1152/physrev.2001.81.4.1535.

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Our appreciation of the physiological functions of estrogens and the mechanisms through which estrogens bring about these functions has changed during the past decade. Just as transgenic mice were produced in which estrogen receptors had been inactivated and we thought that we were about to understand the role of estrogen receptors in physiology and pathology, it was found that there was not one but two distinct and functional estrogen receptors, now called ERα and ERβ. Transgenic mice in which each of the receptors or both the receptors are inactive have revealed a much broader role for estro

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2

TERENTIEV, ALEXANDER A., NURBUBU T. MOLDOGAZIEVA, OLGA V. LEVTSOVA, DMITRY M. MAXIMENKO, DENIS A. BOROZDENKO, and KONSTANTIN V. SHAITAN. "MODELING OF THREE DIMENSIONAL STRUCTURE OF HUMAN ALPHA-FETOPROTEIN COMPLEXED WITH DIETHYLSTILBESTROL: DOCKING AND MOLECULAR DYNAMICS SIMULATION STUDY." Journal of Bioinformatics and Computational Biology 10, no. 02 (2012): 1241012. http://dx.doi.org/10.1142/s0219720012410120.

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It has been long experimentally demonstrated that human alpha-fetoprotein (HAFP) has an ability to bind immobilized estrogens with the most efficiency for synthetic estrogen analog — diethylstilbestrol (DES). However, the question remains why the human AFP (HAFP), unlike rodent AFP, cannot bind free estrogens. Moreover, despite the fact that AFP was first discovered more than 50 years ago and is presently recognized as a "golden standard" among onco-biomarkers, its three-dimensional (3D) structure has not been experimentally solved yet. In this work using MODELLER program, we generated 3D mode

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Ellmann, Stephan, Heinrich Sticht, Falk Thiel, Matthias W. Beckmann, Reiner Strick, and Pamela L. Strissel. "Estrogen and progesterone receptors: from molecular structures to clinical targets." Cellular and Molecular Life Sciences 66, no. 15 (2009): 2405–26. http://dx.doi.org/10.1007/s00018-009-0017-3.

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Kerdivel, Gwenneg, Denis Habauzit, and Farzad Pakdel. "Assessment and Molecular Actions of Endocrine-Disrupting Chemicals That Interfere with Estrogen Receptor Pathways." International Journal of Endocrinology 2013 (2013): 1–14. http://dx.doi.org/10.1155/2013/501851.

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In all vertebrate species, estrogens play a crucial role in the development, growth, and function of reproductive and nonreproductive tissues. A large number of natural or synthetic chemicals present in the environment and diet can interfere with estrogen signaling; these chemicals are called endocrine disrupting chemicals (EDCs) or xenoestrogens. Some of these compounds have been shown to induce adverse effects on human and animal health, and some compounds are suspected to contribute to diverse disease development. Because xenoestrogens have varying sources and structures and could act in ad

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Charitidi, Konstantina, Inna Meltser, and Barbara Canlon. "Estradiol Treatment and Hormonal Fluctuations During the Estrous Cycle Modulate the Expression of Estrogen Receptors in the Auditory System and the Prepulse Inhibition of Acoustic Startle Response." Endocrinology 153, no. 9 (2012): 4412–21. http://dx.doi.org/10.1210/en.2012-1416.

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Estrogens' effects on hearing are documented across species, but the responsible molecular mechanisms remain unknown. The presence of estrogen receptors (ER) throughout the auditory system offers a potential pathway of direct estrogenic effects on auditory function, but little is known about how each ER's expression is regulated by the overall hormonal status of the body. In the present study, we determined the effects of ovariectomy and chronic 17β-estradiol treatment on mRNA and protein expression of ERα and ERβ in peripheral (cochlea) and central (inferior colliculus) auditory structures of

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Makar, Subhajit, Abhrajyoti Ghosh, Ashok Kumar, and Sushil K. Singh. "Recent Studies on Aromatase and Sulfatase Involved in Breast Cancer and their Inhibitors." Current Enzyme Inhibition 16, no. 1 (2020): 20–44. http://dx.doi.org/10.2174/1573408016666200325120248.

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Enzyme aromatase uses several androgen substrates for the biosynthesis of estrogen, i.e. conversion of androstenedione to estrone and testosterone to biologically potent estradiol. Aromatase inhibitors (AIs) such as anastrozole, letrozole and exemestane have been established in standard endocrine therapy of breast cancer, by interfering with estrogen signaling cascade. Steroid sulphatase (STS) regulates the level of active oestrogens and androgens in human target organs and steroidogenic tissues, which have a key role in hormone dependent breast cancers (HDBC). Sulfatase is still under the exp

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Tamura, Fumiya, Shintaro Sugimoto, Mana Sugimoto, et al. "The Effect of a Synthetic Estrogen, Ethinylestradiol, on the hERG Block by E-4031." Biomolecules 11, no. 9 (2021): 1385. http://dx.doi.org/10.3390/biom11091385.

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Inhibition of K+-conductance through the human ether-a-go-go related gene (hERG) channel leads to QT prolongation and is associated with cardiac arrhythmias. We previously reported that physiological concentrations of some estrogens partially suppress the hERG channel currents by interacting with the S6 residue F656 and increase the sensitivity of hERG blockade by E-4031. Although these studies suggested that clinically used synthetic estrogens with similar structures have the marked potential to alter hERG functions, the hERG interactions with synthetic estrogens have not been assessed. We th

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Lephart, Edwin D. "Modulation of Aromatase by Phytoestrogens." Enzyme Research 2015 (December 21, 2015): 1–11. http://dx.doi.org/10.1155/2015/594656.

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The aromatase enzyme catalyzes the conversion of androgens to estrogens in many human tissues. Estrogens are known to stimulate cellular proliferation associated with certain cancers and protect against adverse symptoms during the peri- and postmenopausal intervals. Phytoestrogens are a group of plant derived naturally occurring compounds that have chemical structures similar to estrogen. Since phytoestrogens are known to be constituents of animal/human food sources, these compounds have received increased research attention. Phytoestrogens may contribute to decreased cancer risk by the inhibi

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9

Amr, Abd, Elsayed Elsayed, Mohamed Al-Omar, Hanan Badr Eldin, Eman Nossier, and Mohamed Abdallah. "Design, Synthesis, Anticancer Evaluation and Molecular Modeling of Novel Estrogen Derivatives." Molecules 24, no. 3 (2019): 416. http://dx.doi.org/10.3390/molecules24030416.

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A series of estrone derivatives 3–8 was designed and synthesized using estrone arylmethylenes 2a,b as starting materials and their structures were confirmed by different spectral data and elemental analyses. All the newly synthesized compounds exhibited potent in vitro and in vivo cytotoxic activities against breast cancer cell lines. In addition, all compounds were subjected to in vitro and in vivo inhibition assays for EGFR and VEGFR-2 kinases as well as p53 ubiquitination activity to obtain more details about their mechanism of action. Based on the promising results, a molecular docking stu

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Padron, Adrian, Li Li, Eric M. Kofoed та Fred Schaufele. "Ligand-Selective Interdomain Conformations of Estrogen Receptor-α". Molecular Endocrinology 21, № 1 (2007): 49–61. http://dx.doi.org/10.1210/me.2006-0075.

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Abstract Selective estrogen receptor modulators (SERMs) inhibit estrogen activation of the estrogen receptor (ER) in some tissues but activate ER in other tissues. These tissue-selective actions suggest that SERMs may be identified with tissue specificities that would improve the safety of breast cancer and hormone replacement therapies. The identification of an improved SERM would be aided by understanding the effects of each SERM on the structure and interactions of ER. To date, the inability to obtain structures of the full-length ER has limited our structural characterization of SERM actio

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Dissertations / Theses on the topic "Estrogen Molecular structures"

1

Heldring, Nina. "Molecular basis of estrogen receptor antagonism /." Stockholm, 2006. http://diss.kib.ki.se/2006/91-7140-634-4/.

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Joshi, Sachindra Raj. "Influence of HMGB₁ on estrogen responsive gene expression and nucleosome structure." Bowling Green, Ohio : Bowling Green State University, 2009. http://rave.ohiolink.edu/etdc/view?acc%5Fnum=bgsu1257186343.

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Joshi, Sachindra Raj. "Influence of Hmgb1 on Estrogen Responsive Gene Expression and Nucleosome Structure." Bowling Green State University / OhioLINK, 2009. http://rave.ohiolink.edu/etdc/view?acc_num=bgsu1257186343.

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4

Alexopoulos, Eftichia. "Crystallographic and modeling studies of intermolecular interactions of biological interest." Doctoral thesis, [S.l.] : [s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972659137.

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Book chapters on the topic "Estrogen Molecular structures"

1

Greene, G. L., A. K. Shiau, and K. W. Nettles. "A Structural Explanation for ERα/ERβ SERM Discrimination." In New Molecular Mechanisms of Estrogen Action and Their Impact on Future Perspectives in Estrogen Therapy. Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-662-05386-7_3.

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Hillisch, A., O. Peters, D. Kosemund, et al. "Protein Structure-Based Design, Synthesis Strategy and In Vitro Pharmacological Characterization of Estrogen Receptor α and β Selective Compounds." In New Molecular Mechanisms of Estrogen Action and Their Impact on Future Perspectives in Estrogen Therapy. Springer Berlin Heidelberg, 2004. http://dx.doi.org/10.1007/978-3-662-05386-7_4.

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Kato, Asami, Gen Murakami, Yasushi Hojo, Sigeo Horie, and Suguru Kawato. "Rapid Effects of Estradiol on Dendritic Spines and Synaptic Plasticity in the Male and Female Hippocampus." In Estrogens and Memory. Oxford University Press, 2020. http://dx.doi.org/10.1093/oso/9780190645908.003.0004.

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Although the potent estrogen, 17β‎-estradiol (E2), has long been known to regulate the hippocampal dendritic spine density and synaptic plasticity, the molecular mechanisms through which it does so are less well understood. This chapter discusses the rapid modulation of hippocampal dendritic spine density and synaptic plasticity in male and female rats, with particular attention to studies in hippocampal slices from male rats. Among the mechanisms described are the roles of specific cell-signaling kinases and estrogen receptors in mediating the effects of E2 and progesterone on hippocampal neurons. In addition, dynamic changes of spine structures over time and sex differences in spine regulation are also considered. Finally, the chapter ends by discussing the importance of local hippocampal synthesis of E2 and androgens to hippocampal spine morphology and plasticity.

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4

Korach, Kenneth S. "Stilbestrol Estrogens: Molecular/ Structural Probes for Understanding Estrogen Action." In Molecular Structure and Biological Activity of Steroids. CRC Press, 2018. http://dx.doi.org/10.1201/9781351074803-5.

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Tonn Eisinger, Katherine R., Paul G. Mermelstein, and John Meitzen. "Estrogen Receptors at the Membrane." In Estrogens and Memory. Oxford University Press, 2020. http://dx.doi.org/10.1093/oso/9780190645908.003.0003.

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Recent research has established that modified versions of classical estrogen receptors (ERs) act at the membrane to influence neuronal function. Specifically, palmitoylated ERα‎ and ERβ‎ stimulate signal transduction pathways from the membrane through transactivation of metabotropic glutamate receptors (mGluRs). Caveolin (Cav) proteins assemble mGluR and ER into functional signaling microdomains, with the pairing of specific mGluR and ER varying by brain region and Cav isoform. Palmitoylation regulates the trafficking, localization, and interaction of these proteins by allowing association with membrane lipid rafts. This chapter outlines the discovery that the same ERs responsible for nuclear signaling act at the plasma membrane to exert a wide array of effects. Membrane-associated ER signaling affects molecular, structural, and physiological states, leading to system-level changes in circuit dynamics and, ultimately, behavior.

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Tsakovska, Ivanka, Ilza Pajeva, Petko Alov, and Andrew Worth. "Recent Advances in the Molecular Modeling of Estrogen Receptor-Mediated Toxicity." In Computational chemistry methods in structural biology. Elsevier, 2011. http://dx.doi.org/10.1016/b978-0-12-386485-7.00006-5.

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7

Jha, Tarun, Nilanajn Adhikari, Amit Kumar Halder, and Achintya Saha. "Ligand- and Structure-Based Drug Design of Non-Steroidal Aromatase Inhibitors (NSAIs) in Breast Cancer." In Quantitative Structure-Activity Relationships in Drug Design, Predictive Toxicology, and Risk Assessment. IGI Global, 2015. http://dx.doi.org/10.4018/978-1-4666-8136-1.ch011.

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Aromatase is a multienzyme complex overexpressed in breast cancer and responsible for estrogen production. It is the potential target for designing anti-breast cancer drugs. Ligand and Structure-Based Drug Designing approaches (LBDD and SBDD) are involved in development of active and more specific Nonsteroidal Aromatase Inhibitors (NSAIs). Different LBDD and SBDD approaches are presented here to understand their utility in designing novel NSAIs. It is observed that molecules should possess a five or six membered heterocyclic nitrogen containing ring to coordinate with heme portion of aromatase for inhibition. Moreover, one or two hydrogen bond acceptor features, hydrophobicity, and steric factors may play crucial roles for anti-aromatase activity. Electrostatic, van der Waals, and p-p interactions are other important factors that determine binding affinity of inhibitors. HQSAR, LDA-QSAR, GQSAR, CoMFA, and CoMSIA approaches, pharmacophore mapping followed by virtual screening, docking, and dynamic simulation may be effective approaches for designing new potent anti-aromatase molecules.

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Jha, Tarun, Nilanajn Adhikari, Amit Kumar Halder, and Achintya Saha. "Ligand- and Structure-Based Drug Design of Non-Steroidal Aromatase Inhibitors (NSAIs) in Breast Cancer." In Oncology. IGI Global, 2017. http://dx.doi.org/10.4018/978-1-5225-0549-5.ch004.

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Aromatase is a multienzyme complex overexpressed in breast cancer and responsible for estrogen production. It is the potential target for designing anti-breast cancer drugs. Ligand and Structure-Based Drug Designing approaches (LBDD and SBDD) are involved in development of active and more specific Nonsteroidal Aromatase Inhibitors (NSAIs). Different LBDD and SBDD approaches are presented here to understand their utility in designing novel NSAIs. It is observed that molecules should possess a five or six membered heterocyclic nitrogen containing ring to coordinate with heme portion of aromatase for inhibition. Moreover, one or two hydrogen bond acceptor features, hydrophobicity, and steric factors may play crucial roles for anti-aromatase activity. Electrostatic, van der Waals, and p-p interactions are other important factors that determine binding affinity of inhibitors. HQSAR, LDA-QSAR, GQSAR, CoMFA, and CoMSIA approaches, pharmacophore mapping followed by virtual screening, docking, and dynamic simulation may be effective approaches for designing new potent anti-aromatase molecules.

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9

Zänker, Kurt S., Uwe Schmitz, and Angelika Schwarte. "Computer-Assisted Molecular Design as a Guide for Determination of Structure-Activity Relationships for Estrogen Receptor Substrates by Means of a Model Receptor (hα1-Antitrypsin)." In Novel Approaches in Anticancer Drug Design. S. Karger AG, 1995. http://dx.doi.org/10.1159/000424065.

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