English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Steroidal estrogens are lipid-soluble compounds that are able to pass through the plasma membrane of cells by diffusion. According to the current knowledge, the three main naturally occurring estrogens are estrone (E1), estradiol (E2), and estriol. E2 is the most active estrogen and the predominant female sex steroid during the reproductive years. In addition to these classical estrogens, there are various other steroidal and non-steroidal compounds that are able to interact with estrogen receptors (ERs), and thus at least partially act as estrogens. These include novel endogenous ligands (Saijo et al. 2011), pharmacological (McDonnell & Wardell 2010) and dietary compounds (Müller et al. 2004), as well as synthetic agents, such as pesticides and plasticizers (Craig et al. 2011). Two nuclear ER subtypes have been well characterized, namely ESR1 (ERa) and ESR2 (ERb). The nuclear ERs act as transcription factors, activated by ligand binding, and resulting in the recruitment of various receptor-interacting proteins and transcription factors of the general transcription machinery (Bulynko & O’Malley 2011, Hedengran Faulds et al. 2012). Several splice variants of both ERs have been found in normal and cancerous tissue, but their specific biological functions are still partially unclear. Despite the similarities between the two ERs, many studies have clearly demonstrated that there are subtype-specific actions, and, accordingly, the responses elicited by certain ligands differ depending on the receptor subtype. Furthermore, ERa and ERb display partially overlapping tissue distribution, but they also possess receptor-specific expression patterns, and when expressed in the same tissue, the receptors often localize to different cell types. Several studies indicate that rapid estrogen signaling is not mediated via the nuclear ERs, but through the G-protein-coupled ER1 (GPER, also known as GPR30). GPER activates epidermal growth factor receptor (EGFR) by inducing a release of heparin-binding EGF, which activates EGFR leading to ERK1/2 activation (Prossnitz & Barton 2011). Moreover, E2-mediated activation of GPER induces cAMP production, intracellular calcium mobilization, and PI3K activation (for review, see Prossnitz & Barton (2011)). The distinct properties of ERa, ERb and GPER have gained a lot of interest from the pharmaceutical industry, and there

Understanding the diversity of sex steroid action