Publications by authors named "Bing-Sheng Yang"
Article Synopsis
- Osteoclast (OC) over-activation due to inflammation is linked to bone loss, and the study investigates the role of the CD163/TWEAK/Fn14 signaling pathway in this process.
- Researchers compared CD163-deficient mice to normal mice, analyzed the effects of CD163 and TWEAK levels in bone marrow, and studied the impacts of rCD163 supplementation and TWEAK/Fn14 blockade on bone mass.
- Results showed that CD163 deficiency led to reduced bone mass and increased OC presence; targeting the CD163/TWEAK/Fn14 axis may offer a new therapy for inflammatory bone loss by influencing osteoclast activity.
Article Synopsis
- * A primary focus for treatment is to counteract these growth-inhibitory factors or enhance the supportive factors that promote axonal growth.
- * Research has identified various post-translational modifications (such as tyrosination, acetylation, and phosphorylation) of proteins that are crucial for axonal growth and recovery after spinal cord injury, potentially leading to new therapeutic strategies.
Pheochromocytoma is a rare neuroendocrine tumor which derives from chromaffin cells of the adrenal gland or relevant to sympathetic nerves and ganglia. The clinical features of pheochromocytoma are various. Paroxysmal episodes of serious hypertension, headache, palpitation, and diaphoresis are the typical manifestations (Bravo, 2004).
View Article and Find Full Text PDFIdiopathic hypereosinophilic syndrome (HES) is a rare leukoproliferative systemic disorder characterized by sustained overproduction of eosinophils and poor prognosis. A case that a 67-year-old man with persistent symptoms of heart failure due to cardiac involvement in idiopathic HES is concentrated on. Echocardiography revealed the marked endocardial thickening of both ventricles with an apical obstruction of the right ventricle.
View Article and Find Full Text PDFThe binding of both factors (eRF1 and eRF3) is essential for fast kinetics of the termination of protein translation. The C-terminal domain of eRF1 is known to interact with the C domain of eRF3. Eo-eRF1b contains two highly conserved tryptophan residues (W-11 and W-373), W-11 located in the Eo-eRF1b N domain and W-373 located in the Eo-eRF1b C domain.
View Article and Find Full Text PDFThe C domain of eRF1 interacts with the C domain of eRF3, and the binding of both factors is essential for fast kinetics of the termination of protein translation. Analysis by computational simulation demonstrated that several peptides involved in Eo-eRF1/Eo-eRF3 interaction directly. Among these peptides, the two motifs GVEDT and GFGG were highly conserved, while the fragment aa338-346 of Eo-eRF1a/b was variable.
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