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Shuttle service in cells

Researchers at Ruhr University Bochum discovered a new enzyme, Ubp15p, that collaborates with motor proteins to convert the protein transport machinery back into its initial condition. The enzyme detaches a specific signal sequence from a protein, allowing for recycling and reuse.

SourceRuhr-University Bochum·JournalJournal of Biological Chemistry·DateJul 25, 2011

Making blood-sucking deadly for mosquitoes

A team of biochemists at the University of Arizona discovered that disrupting a molecular process used by mosquitoes to direct proteins to their proper destinations causes more than 90 percent of affected mosquitoes to die within 48 hours of blood feeding. This approach could be used as an additional strategy in the worldwide effort to...

SourceUniversity of Arizona·JournalProceedings of the National Academy of Sciences·DateJul 15, 2011

Termites' digestive system could act as biofuel refinery

A Purdue University study discovered a combination of enzymes in termite guts and symbionts that can efficiently break down woody biomass for biofuel production. The researchers found that the enzymes work together synergistically to release sugars from plant material, which is essential for creating biofuels like ethanol.

SourcePurdue University·JournalPLOS ONE·DateJul 5, 2011

Positioning enzymes with ease

Researchers at Arizona State University have developed a superior method for immobilizing enzymes on surfaces, enabling precise control over their orientation. This technique uses high-affinity peptides to covalently bind enzymes, increasing efficiency and stability.

SourceArizona State University·JournalPLOS ONE·DateApr 9, 2011

New insight into how 'tidying up' enzymes work

Researchers have gained insight into how 'tidying up' enzymes, like cytochromes P450, break down drug molecules. The study reveals that the oxygen transfer process can be influenced by three factors: molecular docking, oxygen-accepting ability, and enzyme pocket shape.

SourceUniversity of Bristol·JournalProceedings of the National Academy of Sciences·DateMar 28, 2011

Novel method could improve the performance of proteins used therapeutically

Whitehead Institute scientists have developed a novel method using the enzyme sortase A to site-specifically modify proteins, increasing their potency, thermal stability, and metabolism. This technique can be applied to improve therapeutically important proteins such as interferon alpha 2 and granulocyte colony-stimulating factor 3.

SourceWhitehead Institute for Biomedical Research·JournalProceedings of the National Academy of Sciences·DateMar 9, 2011

Scientists find key mechanism of childhood respiratory disease

Researchers discovered a critical link between respiratory syncytial virus and oxidative stress, which causes lung inflammation and damage in children. The study found that the virus blocks the activity of Nrf2, a protein needed for antioxidant enzymes, leading to increased reactive oxygen species and cell killing.

SourceUniversity of Texas Medical Branch at Galveston·JournalAmerican Journal of Respiratory and Critical Care Medicine·DateMar 7, 2011

Enzyme cocktail could eliminate a step in biofuel process

Virginia Tech researchers have discovered an enzyme mixture that can work in the presence of toxic infused liquid biomass, eliminating the need for detoxification and reducing production costs. The enzyme cocktail increases biofuel yields by avoiding the production of by-products and synthesis of cell mass.

SourceVirginia Tech·JournalChemistry & Biology·DateFeb 24, 2011

1 group of enzymes could have a positive impact on health, from cholesterol to osteoporosis

Recent studies on PCSK enzymes have shed light on novel functions in diseases such as cardiovascular disorders, osteoporosis, and cancer. The research has revealed that these enzymes may play a crucial role in regulating cholesterol levels and bone formation, offering potential new treatments for dyslipidemia and osteoporosis.

SourceInstitut de recherches cliniques de Montreal·JournalJournal of Biological Chemistry·DateFeb 16, 2011

Unexpected new mechanism behind rheumatoid arthritis

A team of researchers at the University of Gothenburg has identified an enzyme called GGTase-I that, when blocked, can lead to chronic inflammation and joint destruction in mice. The study suggests that GGTase-I plays a crucial role in suppressing RAC1 activity, which is behind the development of inflammatory disorders.

SourceUniversity of Gothenburg·JournalJournal of Clinical Investigation·DateFeb 7, 2011

Fueling the body on fat

A new report reveals a key mechanism linking cellular energy state with whole-body energy state, optimizing fat absorption. Researchers found that the AMPK-SRC-2 pathway plays a crucial role in regulating fat uptake and storage.

SourceCell Press·JournalCell Metabolism·DateJan 4, 2011

New discovery prevents symptoms of rare genetic disorder

A new study by Iowa State University researchers demonstrates that replacing the enzyme for MPS I shortly after birth can prevent irreversible damage and clinical signs of brain, heart, and bone disease. The breakthrough opens the door to improved methods of enzyme delivery in human patients with similar genetic disorders.

SourceIowa State University·JournalScience Translational Medicine·DateDec 2, 2010

Plant-derived scavengers prowl the body for nerve toxins

Researchers at Arizona State University have successfully produced plant-derived human butyrylcholinesterase, a bioscavenger that can neutralize organophosphate toxins. This breakthrough holds promise for protecting the nervous system from pesticide and nerve agent poisoning, as well as treating related diseases such as Alzheimer's.

SourceArizona State University·JournalProceedings of the National Academy of Sciences·DateNov 23, 2010