Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1051/medsci/2024155 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
[New Split-GFP systems to follow organelle contact sites in yeast and human cells].
Med Sci (Paris)
November 2024
Université Paris-Saclay, CNRS, Institut de chimie physique, UMR8000, Orsay, France.
HIV-1 Gag Compact form Stabilized by Intramolecular Interactions is Crucial for Infectious Particle Production.
J Mol Biol
August 2024
UMR 7021, CNRS, Laboratoire de Bioimagerie et Pathologies - LBP, Université de Strasbourg, Faculté de Pharmacie, Illkirch, France. Electronic address:
HIV-1 Gag polyprotein plays a pivotal role in assembly and budding of new particles, by specifically packaging two copies of viral gRNA in the host cell cytoplasm and selecting the cell plasma membrane for budding. Both gRNA and membrane selections are thought to be mediated by the compact form of Gag. This compact form binds to gRNA through both its matrix (MA) and nucleocapsid (NC) domains in the cytoplasm.
View Article and Find Full Text PDFFAST, a method based on split-GFP for the detection in solution of proteins synthesized in cell-free expression systems.
Sci Rep
April 2024
Laboratory of Genetics of Microorganisms and Microbial Biotechnology, School of Biosciences and Veterinary Medicine, University of Camerino, 62032, Camerino, MC, Italy.
Article Synopsis
- Cell-free protein synthesis (CFPS) systems are gaining popularity, but traditional detection methods like radioactive labeling and fluorescent tagging are often impractical due to safety, cost, and complexity issues.
- We've developed FAST (Fluorescent Assembly of Split-GFP for Translation Tests), a new method using split GFP fragments that simplifies protein detection by fusing a small tag (GFP11) to proteins, resulting in a fluorescent signal when it interacts with another fragment (GFP1-10).
- This method allows for quick and sensitive detection of synthesized proteins in various CFPS systems and can also be used to investigate how antibiotics inhibit translation in a straightforward manner.
Mitochondria-ER contact sites expand during mitosis.
iScience
April 2024
Calcium Signaling Group, Research Department, Weill Cornell Medicine Qatar, Education City, Qatar Foundation, Doha, Qatar.
Mitochondria-ER contact sites (MERCS) are involved in energy homeostasis, redox and Ca signaling, and inflammation. MERCS are heavily studied; however, little is known about their regulation during mitosis. Here, we show that MERCS expand during mitosis in three cell types using various approaches, including transmission electron microscopy, serial EM coupled to 3D reconstruction, and a split GFP MERCS marker.
View Article and Find Full Text PDFTripeptidyl peptidase II coordinates the homeostasis of calcium and lipids in the central nervous system and its depletion causes presenile dementia in female mice through calcium/lipid dyshomeostasis-induced autophagic degradation of CYP19A1.
Theranostics
February 2024
The Second Affiliated Hospital of Xinxiang Medical University (Henan Mental Hospital), Xinxiang, 453000, PR China.
Tripeptidyl peptidase II (TPP2) has been proven to be related to human immune and neurological diseases. It is generally considered as a cytosolic protein which forms the largest known protease complex in eukaryotic cells to operate mostly downstream of proteasomes for degradation of longer peptides. However, this canonical function of TPP2 cannot explain its role in a wide variety of biological and pathogenic processes.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!