Estrogen receptor phosphorylation
Steroids, ISSN: 0039-128X, Vol: 68, Issue: 1, Page: 1-9
2003
- 403Citations
- 213Captures
- 2Mentions
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations403
- Citation Indexes402
- 402
- CrossRef318
- Patent Family Citations1
- 1
- Captures213
- Readers213
- 213
- Mentions2
- References2
- 2
Review Description
Estrogen receptor α (ERα) is phosphorylated on multiple amino acid residues. For example, in response to estradiol binding, human ERα is predominately phosphorylated on Ser-118 and to a lesser extent on Ser-104 and Ser-106. In response to activation of the mitogen-activated protein kinase pathway, phosphorylation occurs on Ser-118 and Ser-167. These serine residues are all located within the activation function 1 region of the N-terminal domain of ERα. In contrast, activation of protein kinase A increases the phosphorylation of Ser-236, which is located in the DNA-binding domain. The in vivo phosphorylation status of Tyr-537, located in the ligand-binding domain, remains controversial. In this review, I present evidence that these phosphorylations occur, and identify the kinases thought to be responsible. Additionally, the functional importance of ERα phosphorylation is discussed.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0039128X02001101; http://dx.doi.org/10.1016/s0039-128x(02)00110-1; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037211754&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/12475718; https://linkinghub.elsevier.com/retrieve/pii/S0039128X02001101; http://linkinghub.elsevier.com/retrieve/pii/S0039128X02001101; http://api.elsevier.com/content/article/PII:S0039128X02001101?httpAccept=text/xml; http://api.elsevier.com/content/article/PII:S0039128X02001101?httpAccept=text/plain; http://dx.doi.org/10.1016/s0039-128x%2802%2900110-1; https://dx.doi.org/10.1016/s0039-128x%2802%2900110-1
Elsevier BV
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