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1996 1
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14 results

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Page 1
Vitamin D did not reduce multiple sclerosis disease activity after a clinically isolated syndrome.
Butzkueven H, Ponsonby AL, Stein MS, Lucas RM, Mason D, Broadley S, Kilpatrick T, Lechner-Scott J, Barnett M, Carroll W, Mitchell P, Hardy TA, Macdonell R, McCombe P, Lee A, Kalincik T, van der Walt A, Lynch C, Abernethy D, Willoughby E, Barkhof F, MacManus D, Clarke M, Andrew J, Morahan J, Zhu C, Dear K, Taylor BV; PREVANZ Investigators. Butzkueven H, et al. Brain. 2024 Apr 4;147(4):1206-1215. doi: 10.1093/brain/awad409. Brain. 2024. PMID: 38085047 Free PMC article. Clinical Trial.
Low serum levels of 25-hydroxyvitamin D [25(OH)D] and low sunlight exposure are known risk factors for the development of multiple sclerosis. Add-on vitamin D supplementation trials in established multiple sclerosis have been inconclusive. ...
Low serum levels of 25-hydroxyvitamin D [25(OH)D] and low sunlight exposure are known risk factors for the development of mult …
Surface expression of GluR-D AMPA receptor is dependent on an interaction between its C-terminal domain and a 4.1 protein.
Coleman SK, Cai C, Mottershead DG, Haapalahti JP, Keinänen K. Coleman SK, et al. J Neurosci. 2003 Feb 1;23(3):798-806. doi: 10.1523/JNEUROSCI.23-03-00798.2003. J Neurosci. 2003. PMID: 12574408 Free PMC article.
In contrast, little is known of the molecular interactions of the GluR-D subunit, or of the mechanisms regulating the traffic of GluR-D-containing AMPA receptors. ...Coimmunoprecipitation demonstrated that GluR-D associated with 4.1 protein(s) in both HEK293 …
In contrast, little is known of the molecular interactions of the GluR-D subunit, or of the mechanisms regulating the traffic of GluR …
Effect of cumulin and super-GDF9 in standard and biphasic mouse IVM.
Akin N, Richani D, Liao X, Zhao Y, Herta AC, Billooye K, Stocker WA, Mottershead DG, Harrison CA, Smitz J, Anckaert E, Gilchrist RB. Akin N, et al. J Assist Reprod Genet. 2022 Jan;39(1):127-140. doi: 10.1007/s10815-021-02382-z. Epub 2022 Jan 4. J Assist Reprod Genet. 2022. PMID: 34984599 Free PMC article.
High activity, soluble, bacterially expressed human vitamin D receptor and its ligand binding domain.
Mottershead DG, Polly P, Lyons RJ, Sutherland RL, Watts CK. Mottershead DG, et al. J Cell Biochem. 1996 Jun 1;61(3):325-37. doi: 10.1002/(SICI)1097-4644(19960601)61:3%3C325::AID-JCB1%3E3.0.CO;2-V. J Cell Biochem. 1996. PMID: 8761938
The effects of 1 alpha, 25(OH)2 vitamin D3 on cell growth and differentiation are primarily mediated by the nuclear vitamin D receptor (VDR). In order to study aspects of receptor function and ultimately the structural basis of the VDR-ligand interaction, it is necessary t …
The effects of 1 alpha, 25(OH)2 vitamin D3 on cell growth and differentiation are primarily mediated by the nuclear vitamin D recepto …
Determinants of antagonist binding at the alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor subunit, GluR-D. Role of the conserved arginine 507 and glutamate 727 residues.
Jouppila A, Pentikäinen OT, Settimo L, Nyrönen T, Haapalahti JP, Lampinen M, Mottershead DG, Johnson MS, Keinänen K. Jouppila A, et al. Eur J Biochem. 2002 Dec;269(24):6261-70. doi: 10.1046/j.1432-1033.2002.03345.x. Eur J Biochem. 2002. PMID: 12473122 Free article.
To examine the role of these residues (R507 and E727 in the GluR-D subunit) in the discrimination between agonists and antagonists, we analyzed the ligand-binding properties of homomeric GluR-D and its soluble ligand-binding domain with mutations at these positions. …
To examine the role of these residues (R507 and E727 in the GluR-D subunit) in the discrimination between agonists and antagonists, w …
Alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor channels lacking the N-terminal domain.
Pasternack A, Coleman SK, Jouppila A, Mottershead DG, Lindfors M, Pasternack M, Keinänen K. Pasternack A, et al. J Biol Chem. 2002 Dec 20;277(51):49662-7. doi: 10.1074/jbc.M208349200. Epub 2002 Oct 21. J Biol Chem. 2002. PMID: 12393905 Free article.
We have studied the properties of homomeric alpha-amino-3-hydroxy-5-methylisoxazolepropionate (AMPA)-selective GluR-D glutamate receptors carrying N-terminal deletions. Our analysis indicates that, surprisingly, transport to the cell surface, ligand binding properties, ago …
We have studied the properties of homomeric alpha-amino-3-hydroxy-5-methylisoxazolepropionate (AMPA)-selective GluR-D glutamate recep …
Discrimination between agonists and antagonists by the alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid-selective glutamate receptor. A mutation analysis of the ligand-binding domain of GluR-D subunit.
Lampinen M, Settimo L, Pentikainen OT, Jouppila A, Mottershead DG, Johnson MS, Keinanen K. Lampinen M, et al. J Biol Chem. 2002 Nov 1;277(44):41940-7. doi: 10.1074/jbc.M205242200. Epub 2002 Aug 7. J Biol Chem. 2002. PMID: 12167621 Free article.
Wild-type and mutated versions of the ligand-binding domain of GluR-D were expressed in insect cells as secreted soluble polypeptides and subjected to binding assays using [(3)H]AMPA, an agonist, and [(3)H]Ro 48-8587 (9-imidazol-1-yl-8-nitro-2,3,5,6-tetrahydro[1,2,4]triazo …
Wild-type and mutated versions of the ligand-binding domain of GluR-D were expressed in insect cells as secreted soluble polypeptides …
A biosensing system based on extracellular potential recording of ligand-gated ion channel function overexpressed in insect cells.
Haruyama T, Bongsebandhu-Phubhakdi S, Nakamura I, Mottershead D, Keinänen K, Kobatake E, Aizawa M. Haruyama T, et al. Anal Chem. 2003 Feb 15;75(4):918-21. doi: 10.1021/ac025670x. Anal Chem. 2003. PMID: 12622384
Application of glutamate, a natural agonist, induced a complex and robust potentiometric response in cells expressing homomeric GluR-D glutamate receptor, but not in nonexpressing control cells. The response consisted of an initial decrease in outer potential followed by a …
Application of glutamate, a natural agonist, induced a complex and robust potentiometric response in cells expressing homomeric GluR-D
14 results