Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 3 de 3
Filter
Add more filters










Database
Publication year range
1.
Science ; 355(6321): 166-169, 2017 01 13.
Article in English | MEDLINE | ID: mdl-28082587

ABSTRACT

The localization of hydrogen atoms is an essential part of crystal structure analysis, but it is difficult because of their small scattering power. We report the direct localization of hydrogen atoms in nanocrystalline materials, achieved using the recently developed approach of dynamical refinement of precession electron diffraction tomography data. We used this method to locate hydrogen atoms in both an organic (paracetamol) and an inorganic (framework cobalt aluminophosphate) material. The results demonstrate that the technique can reliably reveal fine structural details, including the positions of hydrogen atoms in single crystals with micro- to nanosized dimensions.

2.
Cell Death Differ ; 18(5): 783-92, 2011 May.
Article in English | MEDLINE | ID: mdl-21072052

ABSTRACT

Glucocorticoid-induced apoptosis of thymocytes is one of the first recognized forms of programmed cell death. It was shown to require gene activation induced by the glucocorticoid receptor (GR) translocated into the nucleus following ligand binding. In addition, the necessity of the glucocorticoid-induced, but transcription-independent phosphorylation of phosphatidylinositol-specific phospholipase C (PI-PLC) has also been shown. Here we report that retinoic acids, physiological ligands for the nuclear retinoid receptors, enhance glucocorticoid-induced death of mouse thymocytes both in vitro and in vivo. The effect is mediated by retinoic acid receptor (RAR) alpha/retinoid X receptor (RXR) heterodimers, and occurs when both RARα and RXR are ligated by retinoic acids. We show that the ligated RARα/RXR interacts with the ligated GR, resulting in an enhanced transcriptional activity of the GR. The mechanism through which this interaction promotes GR-mediated transcription does not require DNA binding of the retinoid receptors and does not alter the phosphorylation status of Ser232, known to regulate the transcriptional activity of GR. Phosphorylation of PI-PLC was not affected. Besides thymocytes, retinoids also promoted glucocorticoid-induced apoptosis of various T-cell lines, suggesting that they could be used in the therapy of glucocorticoid-sensitive T-cell malignancies.


Subject(s)
Apoptosis/drug effects , Glucocorticoids/pharmacology , Receptors, Glucocorticoid/metabolism , Retinoids/pharmacology , T-Lymphocytes/drug effects , Alitretinoin , Animals , Cells, Cultured , DNA Fragmentation , Dexamethasone/adverse effects , Gene Deletion , Humans , Immunoprecipitation , Male , Mice , Mice, Inbred BALB C , Mice, Knockout , Organic Chemicals/pharmacology , Phosphoinositide Phospholipase C/metabolism , Phosphorylation , Protein Multimerization/drug effects , Receptors, Retinoic Acid/genetics , Receptors, Retinoic Acid/metabolism , Retinoic Acid Receptor alpha , Retinoid X Receptors/agonists , Retinoid X Receptors/metabolism , T-Lymphocytes/physiology , Transcription Factors/metabolism , Transcription, Genetic , Transcriptional Activation , Tretinoin/pharmacology , Two-Hybrid System Techniques
SELECTION OF CITATIONS
SEARCH DETAIL