M
Malcolm G. Parker
Researcher at Lincoln's Inn
Publications - 67
Citations - 8644
Malcolm G. Parker is an academic researcher from Lincoln's Inn. The author has contributed to research in topics: Receptor & Nuclear receptor. The author has an hindex of 36, co-authored 67 publications receiving 8504 citations. Previous affiliations of Malcolm G. Parker include University of Leicester.
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Journal ArticleDOI
Fatty Acids, Eicosanoids, and Hypolipidemic Agents Identified as Ligands of Peroxisome Proliferator-Activated Receptors by Coactivator-Dependent Receptor Ligand Assay
Grigorios Krey,Olivier Braissant,Fabienne L’Horset,Eric Kalkhoven,Mai Perroud,Malcolm G. Parker,Walter Wahli +6 more
TL;DR: The results suggest that PPARs, by their ability to interact with a number of structurally diverse compounds, have acquired unique ligand-binding properties among the superfamily of nuclear receptors that are compatible with their biological activity.
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A modified oestrogen receptor ligand-binding domain as an improved switch for the regulation of heterologous proteins
TL;DR: A transcriptionally inactive mutant of the murine oestrogen receptor is used which is unable to bind oestrogens yet retains normal affinity for the synthetic ligand, 4-hydroxytamoxifen.
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Identification of a conserved region required for hormone dependent transcriptional activation by steroid hormone receptors
TL;DR: It is proposed that the conserved region in the C‐terminus of the hormone binding domain between residues 538 and 552 in the mouse oestrogen receptor may be essential for ligand dependent transcriptional activation by other members of the nuclear receptor family.
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Estrogen receptors alpha and beta form heterodimers on DNA.
TL;DR: It is shown that ERα and ERβ, expressed both in vitro and in vivo, form heterodimers which bind to DNA with an affinity similar to that of ER α and greater than that ofERβ homodimer.
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Characterization and colocalization of steroid binding and dimerization activities in the mouse estrogen receptor
TL;DR: Analysis of sequences in this region revealed that a heptad repeat of hydrophobic residues was conserved in all members of the nuclear receptor superfamily, implying that the steroid binding and dimerization domains overlap.