Zobrazeno 1 - 10
of 11
pro vyhledávání: '"Yvonne E. Lindsay"'
Autor:
Arnaud Deladeriere, Hervé Guillou, Sabine Suire, Oliver Rausch, G. John Ferguson, Simon Andrews, Simon Walker, Tamara Chessa, Till Bretschneider, Cheng-Jin Du, Laura J. Norton, Anne Segonds-Pichon, Len R. Stephens, Takehiko Sasaki, Peter Finan, Yvonne E. Lindsay, Phillip T. Hawkins, John M. Lucocq
Publikováno v:
Advances in Biological Regulation
Advances in Biological Regulation, 2016, 60, pp.36-45. ⟨10.1016/j.jbior.2015.10.005⟩
Advances in Biological Regulation (60), 36-45. (2016)
Advances in Biological Regulation, 2016, 60, pp.36-45. ⟨10.1016/j.jbior.2015.10.005⟩
Advances in Biological Regulation (60), 36-45. (2016)
Class I phosphoinositide 3-kinases (PI3Ks) are important regulators of neutrophil migration in response to a range of chemoattractants. Their primary lipid products PtdIns(3,4,5)P3 and PtdIns(3,4)P2 preferentially accumulate near to the leading edge
Publikováno v:
Advances in Biological Regulation. 57:102-111
Small molecule inhibitors of many classes of enzymes, including phosphatases, have widespread use as experimental tools and as therapeutics. Efforts to develop inhibitors against the lipid phosphatase and tumour suppressor, PTEN, was for some time li
Autor:
Ana M. Schor, Go Ohe, Seth L. Schor, Yvonne E. Lindsay, Nicolas R. Leslie, Sarah J. Jones, Ian R. Ellis
Publikováno v:
Cellular Signalling. 22:1655-1659
The protein kinase AKT is activated strongly by many motogenic growth factors, yet has recently been shown capable of inhibiting migration in several cell types. Here we report that treatment with Migration Stimulating Factor (MSF), a truncated form
Autor:
Jenni Harvey, Sandra D. Santos, Andrew J. Irving, Ana Luísa Carvalho, Christopher N. Connolly, Yvonne E. Lindsay, Peter R. Moult, Nick R. Leslie, Alasdair Cross
Publikováno v:
The Journal of Neuroscience. 30:4088-4101
The hormone leptin can cross the blood–brain barrier and influences numerous brain functions (Harvey, 2007). Indeed, recent studies have demonstrated that leptin regulates activity-dependent synaptic plasticity in the CA1 region of the hippocampus
Autor:
Stephen T. Safrany, Michael J. Clague, Nick R. Leslie, Óscar Lorenzo, C. Peter Downes, Rachel Toth, Sarah H. Ross, Yvonne E. Lindsay, Fabrizio Villa
Publikováno v:
Cellular Signalling. 19:1521-1530
The Protein Tyrosine Phosphatase (PTP) family comprises a large and diverse group of enzymes, regulating a range of biological processes through de-phosphorylation of many proteins and lipids. These enzymes share a catalytic mechanism that requires a
Autor:
C. Peter Downes, Yvonne E. Lindsay, Alison Fairservice, Lindsay Davidson, Nick R. Leslie, John M. Lucocq, David McCoull, Alexander Gray
Publikováno v:
Journal of Cell Science. 119:5160-5168
Phosphatidylinositol (3,4,5) trisphosphate [PtdIns(3,4,5)P3] is a lipid second messenger, produced by Type I phosphoinositide 3-kinases (PI 3-kinases), which mediates intracellular responses to many growth factors. Although PI 3-kinases are implicate
Publikováno v:
FEMS Microbiology Letters. 140:203-207
Increasing NaCl concentrations in the growth medium inhibited the growth of Desulfovibrio halophilus due to both an increase in the lag phase of growth and a reduction in the specific growth rate. Addition of 1 mM glycine betaine to the growth medium
Publikováno v:
Biochemical Society Transactions. 32:1018-1020
Although reactive oxygen species play important roles in cellular physiology as signalling molecules, their molecular targets are largely unknown. A probable group of targets for mediating many of the effects of reactive oxygen species on cell signal
Publikováno v:
Biology of Reproduction. 51:358-365
During pregnancy, zinc (Zn) levels in the rat fetal liver increase markedly. Why they do so or how the increase is regulated is unknown. We firstly investigated whether the increase occurs as a result of increased Zn transfer across the placenta and
Publikováno v:
Biochemical Society transactions. 32(Pt 2)
PTEN (phosphatase and tensin homologue deleted on chromosome 10) is a member of the protein tyrosine phosphatase family that is structurally adapted to facilitate the metabolism of 3-phosphoinositide lipid second messengers, especially PtdIns(3,4,5)