Synthesis and Crystal Structure of a Phosphorylated Estrogen Receptor Ligand Binding Domain

The Structural Basis of Estrogen Receptor/Coactivator Recognition and the Antagonism of This Interaction by Tamoxifen

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Structure of the ligand‐binding domain of oestrogen receptor beta in the presence of a partial agonist and a full antagonist

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Steroid‐induced androgen receptor–oestradiol receptor β–Src complex triggers prostate cancer cell proliferation

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Normal and cancer-related functions of the p160 steroid receptor co-activator (SRC) family

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Nuclear receptor ligand-binding domains: three-dimensional structures, molecular interactions and pharmacological implications

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Mechanism of the nuclear receptor molecular switch

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Protein ligation: an enabling technology for the biophysical analysis of proteins

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Crystal Structure of a Phosphorylated Smad2

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Nuclear receptors: integration of multiple signalling pathways through phosphorylation

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Design of selective nuclear receptor modulators: RAR and RXR as a case study

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Constitutively active human estrogen receptors containing amino acid substitutions for tyrosine 537 in the receptor protein

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Post-translational modifications of steroid receptors

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Phosphorylation of the human estrogen receptor on tyrosine 537 in vivo and by src family tyrosine kinases in vitro

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Structure-Based Design of Estrogen Receptor-β Selective Ligands

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Characterization of the Interactions of Estrogen Receptor and MNAR in the Activation of cSrc

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NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses

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Ligand‐independent activation of the oestrogen receptor by mutation of a conserved tyrosine

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Inhibition of Estradiol Receptor/Src Association and Cell Growth by an Estradiol Receptor α Tyrosine-Phosphorylated Peptide

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Protein semisynthesis and expressed protein ligation: chasing a protein's tail

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Ligand-independent activation of the estrogen receptors alpha and beta by mutations of a conserved tyrosine can be abolished by antiestrogens.

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Function of Estrogen Receptor Tyrosine 537 in Hormone Binding, DNA Binding, and Transactivation

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Cooperativity and Dimerization of Recombinant Human Estrogen Receptor Hormone-binding Domain

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An Integrated-Molecule-Format Multicolor Probe for Monitoring Multiple Activities of a Bioactive Small Molecule

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Sex-steroid hormones and EGF signalling in breast and prostate cancer cells: Targeting the association of Src with steroid receptors

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Mutations of Tyrosine 537 in the Human Estrogen Receptor-α Selectively Alter the Receptor's Affinity for Estradiol and the Kinetics of the Interaction

Zhong, L., & Skafar, D. F. (2002) · Biochemistry · doi:10.1021/bi0121095 · Cited by 32 · see citing works

Panning for SNuRMs: using cofactor profiling for the rational discovery of selective nuclear receptor modulators

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Ecdysteroids: A novel class of anabolic agents?

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Phosphorylation of the retinoic acid receptor alpha induces a mechanical allosteric regulation and changes in internal dynamics

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Phytoecdysteroids and Anabolic Effect of Atriplex dimorphostegia: UPLC-PDA-MS/MS Profiling, In Silico and In Vivo Models

Zaghloul, E., Handousa, H., Singab, A. N. B., Elmazar, M. M., Ayoub, I. M., & Swilam, N. (2023) · Plants · doi:10.3390/plants12010206 · Cited by 11 · see citing works

The Effect of O-GlcNAcylation on Phosphorylation of tau

Qian, W. (2003) · PROGRESS IN BIOCHEMISTRY AND BIOPHYSICS

Tropomyosin Phosphorylation in Healthy and Diseased Hearts

Sheikh, H. N., & Wieczorek, D. F. (2010) · The FASEB Journal · doi:10.1096/fasebj.24.1_supplement.904.6

Systems analysis of phosphorylation‐regulated Bcl‐2 interactions establishes a model to reconcile the controversy over the significance of Bcl‐2 phosphorylation

Song, T., Wang, P., Yu, X., Wang, A., Chai, G., Fan, Y., & Zhang, Z. (2018) · British Journal of Pharmacology · doi:10.1111/bph.14555 · Cited by 11 · see citing works

Two phosphorylation sites on eIF‐2α

Kramer, G. (1990) · FEBS Letters · doi:10.1016/0014-5793(90)80919-a · Cited by 12 · see citing works

Connexin 43-serine 282 modulates serine 279 phosphorylation in cardiomyocytes

Sun, Z., Yang, Y., Wu, L., Talabieke, S., You, H., Zheng, Y., & Luo, D. (2019) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2019.04.032 · Cited by 13 · see citing works