A new study shows that the TLK1 and TLK2 enzymes are critical for ensuring the copying of DNA. The research is based on previous studies that pointed to TLK1/2 as potential candidate targets in cancer therapy, and it provides new molecular details on their key functions in cancer cell proliferation. The study was published in Science Advances.
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Researchers have uncovered a destructive mechanism at the molecular level that causes a well-known phenomenon associated with obesity: leptin resistance. They found that mice fed a high-fat diet produce an enzyme named MMP-2 that clips receptors for the hormone leptin from the surface of neuronal cells in the hypothalamus. This blocks leptin from binding to its receptors. This, in turn, keeps the neurons from signaling that your stomach is full and you should stop eating.
Scientists have invented a new method that allows for the flexible engineering of essential and non-essential enzymes without additional engineering. They describe a method based on CRISPR/Cas9, which enables flexible engineering of essential and non-essential enzymes without additional engineering.
This could be of great importance for various aspects including the development of bio-based production of pharmaceuticals, food additives, fuels, and cosmetics. The study published in the journal Metabolic Engineering.
Classic hydrogenation catalyst installs multiple stereocentres one by one to create small amino acid rings as single enantiomers. A rhodium catalyst that can walk around a macrocyclic ring and create multiple stereocentres in a row could change the way chemists make cyclic peptides. The unusual mechanism was discovered in a hydrogenation catalyst that has been studied for half a century.
Scientists have identified the function of a protein that has been confounding metabolism researchers for more than two decades. And it may have implications both for treating obesity and for understanding weight gain during pregnancy and menopause.
The protein, called the melanocortin 3 receptor (MC3R) maintains what Roger Cone, director of the U-M Life Sciences Institute, has termed "energy rheostasis," a poorly understood phenomenon in the field of metabolism research.
A lack of MC3R has almost no effect on mice under normal conditions. But when their metabolism is challenged, mice without this protein lose more weight when fasting and gain more weight when eating a high-fat diet, compared with normal mice.
Scientists at Scripps Research have solved the structure of a key protein that senses when our cells swell. This protein, called SWELL1 (or LRRC8A), works as an "ion channel" on the cell membrane to relieve pressure inside cells.
Researchers have discovered a direct link between the protein aggregation in nerve cells that is typical for neurodegenerative diseases, and the regulation of gene expression in Huntington's disease.
The results pave the way for the development of new treatment strategies for diseases that involve impairment of the basic mechanism by which the body's cells can break down and recycle their own component parts. This process, called autophagy, is disrupted in, for example, Huntington's and other neurodegenerative diseases.
The research, which is based on studies using cell culture and mouse models as well as human tissue from deceased individuals with Huntington's disease. The study was published in Cell Reports.
Enzymes perform very specific functions and require only little energy which is why the biocatalysts are also of interest to the chemical industry. Biologists have now provided a summary on what is known about the mechanisms of enzymes in nature. Moreover, the authors outline a future vision: artificial biocatalysts that are not protein-based, as they usually are in nature, but which are rather made from DNA.
Enzymes perform very specific functions and require only little energy which is why the biocatalysts are also of interest to the chemical industry. The study was published in the journal Nature Reviews Chemistry. Moreover, the authors outline a future vision: artificial biocatalysts that are not protein-based, as they usually are in nature, but which are rather made from DNA.
A biochemistry instructor curious about an enzyme discovered in the damaged neurons of people with multiple sclerosis made a leap toward a potential cure for countless neurodegenerative ills.
The research team based in Japan has designed new proteins that can self-assemble into the complex structures underlying biological organisms, laying the groundwork for leading-edge applications in biotechnology.
The researchers created and developed the proteins with a specific function and their method reveals a possibility that certain protein functions can be created on demand. The study was published in Synthetic Biology, a peer-reviewed journal published by the American Chemical Society (ACS).
The coupling of an enzyme with a light-activated catalyst offers great potential for organic synthesis. Catalysts working in pairs can promote more-effective reactions than can the same catalysts used sequentially. The study was published in the journal Nature.
The development of catalytic reactions is a dominant theme in chemistry, especially in industry, where major efforts are underway to develop large-scale chemical processes that are sustainable and avoid producing unnecessary waste. Chemical reactions can be accelerated using many types of catalyst, including metals (or their salts or complexes), small organic molecules, enzymes and light-activated catalysts.
Researchers have identified a key role for the TLK1 and TLK2 enzymes in DNA replication. During cell growth, cells copy their DNA through a process called DNA replication. For this process to be accurate, the genetic and epigenetic information must be copied flawlessly. The study was published in Science Advances.