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L. E. Shaw

Researcher at University of Reading

Publications -  7
Citations -  722

L. E. Shaw is an academic researcher from University of Reading. The author has contributed to research in topics: Amyotrophic lateral sclerosis & Medicine. The author has an hindex of 4, co-authored 4 publications receiving 671 citations.

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Oestrogenic activity of parabens in MCF7 human breast cancer cells.

TL;DR: Molecular modelling has indicated the mode by which paraben molecules can bind into the ligand binding pocket of the crystal structure of the ligands binding domain (LBD) of the oestrogen receptor alpha (ERalpha) in place of 17beta-oestradiol, and has shown that two parabens molecules canbind simultaneously in a mode in which their phenolic hydroxyl groups bind similarly to those of the meso-hexoestrol molecule.
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Oestrogenic activity of isobutylparaben in vitro and in vivo.

TL;DR: Results here show that branching of the alkyl chain to isobutylparaben increases oestrogenic activity beyond that of the equivalent length linear alkyL chain in n‐butyl paraben.
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Oestrogenic activity of benzylparaben.

TL;DR: It is demonstrated that the oestrogenicity of methylparaben can be increased by the addition of an aryl group as well as by lengthening or branching the alkyl grouping.
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Changes in oestrogen receptor-alpha and -beta during progression to acquired resistance to tamoxifen and fulvestrant (Faslodex, ICI 182,780) in MCF7 human breast cancer cells.

TL;DR: It is shown that whilst ERα can be abrogated by fulvestrant and increased by tamoxifen in some circumstances, this does not always hold true and mechanisms other than alteration to ER must be involved in the development of antioestrogen resistant growth.
Posted ContentDOI

SOD1-ALS-Browser: a web-utility for investigating the clinical phenotype in SOD1 amyotrophic lateral sclerosis

TL;DR: SOD1-ALS Browser as mentioned in this paper is a web-based tool for comparative phenotype analysis in ALS, which contains a built-in dataset of clinical information from 1,383 people with ALS harboring a SOD1 variant resulting in one of 162 unique amino acid sequence alterations, and from a non-SOD 1 comparator ALS cohort of 13,469 individuals.