Getting newly synthesized proteins into shape

Article Abstract:

Research has been conducted on the polypeptide cellular synthesis. The function of the chaperones in the polypeptide folding during their release into the cytosol has been investigated.

Cytosol

---

Negative regulation of fibroblast motility by Ena/VASP proteins

Article Abstract:

Research has been conducted on the Ena/VASP proteins. Results indicate that these proteins negatively regulate fibroblast motility.

Sweden, Cells, Cell migration, Fibroblasts

---

Protein folding in vivo: unraveling complex pathways

Article Abstract:

Protein folding in a cell is a complex process. Molecular chaperones, a class of proteins that bind to unfolded or partially folded polypeptides, have been cited as facilitators of the acquisition of the active conformation of polypeptides. Results of previous studies indicate the existence of multiple chaperones within a complex which suggests a dynamic interaction. Furthermore, protein folding pathways need not be exclusively unidirectional.

Protein folding

Similar abstracts:

• Abstracts: Negative regulation of male development in Caenorhabditis elegans by a protein-protein interaction between TRA-2A and FEM-3
• Abstracts: Defective transcription-coupled repair in cockayne syndrome b mice is associated with skin cancer predisposition
• Abstracts: Tribbles coordinates mitosis and morphogenesis in Drosophila by regulating string/CDC25 proteolysis. Guidance of cell migration by the Drosophila PDGF/VEGF receptor
• Abstracts: An RNA-dependent RNA polymerase gene in Arabidopsis is required for posttranscriptional gene silencing mediated by a transgene but not by a virus
• Abstracts: FOG-2, a cofactor for GATA transcription factors, is essential for heart morphogenesis and development of coronary vessels from epicardium

This website is not affiliated with document authors or copyright owners. This page is provided for informational purposes only. Unintentional errors are possible.