The BRIC research team has discovered a family of enzymes that prevents cancer cells to age like normal cells. The good news is, that the researchers have developed small molecules that can impede the enzyme activity.
It is researchers Paul Cloos, Jesper Christensen, Karl Agger, and Professor and Director of BRIC, Kristian Helin that have proved how the enzymes, which belongs to a family of enzymes called Jumonji-enzymes, play a role in the development of cancer. They have also established that the enzymes are more frequent in cancer cells than in normal cells.
As cells are ageing, their DNA structures change and become denser. That causes the genes to be less active, which in turn will stop the cell division. The BRIC team has found three Jumonji-enzymes that are capable of loosening the DNA structure. If the cells have too many of the Jumonji-enzymes, the enzymes will make it possible for the genes to cause uncontrolled growth. That can lead to cancer.
The research team are currently working on determining how the Jumonji-enzymes control normal cell growth, and how the increased amount of these enzymes can lead to cancer.
Climate Impact Research in Hannover: Small Plants against Large Waves
17.08.2018 | Leibniz Universität Hannover
First transcription atlas of all wheat genes expands prospects for research and cultivation
17.08.2018 | Leibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung
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Scientists at the University of California, Los Angeles present new research on a curious cosmic phenomenon known as "whistlers" -- very low frequency packets...
Scientists develop first tool to use machine learning methods to compute flow around interactively designable 3D objects. Tool will be presented at this year’s prestigious SIGGRAPH conference.
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Researchers from TU Graz and their industry partners have unveiled a world first: the prototype of a robot-controlled, high-speed combined charging system (CCS) for electric vehicles that enables series charging of cars in various parking positions.
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Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.
Actin is the most abundant protein in highly developed cells and has diverse functions in processes like cell stabilization, cell division and muscle...
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