Lifeboat Foundation: Safeguarding Humanity
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Category: biotech/medical – Page 9

Scientists at Northwestern University have developed a new approach that directly combats the progression of neurodegenerative diseases like Alzheimer’s disease and amyotrophic lateral sclerosis (ALS).

In these devastating illnesses, proteins misfold and clump together around brain cells, which ultimately leads to cell death. The innovative new treatment effectively traps the proteins before they can aggregate into the toxic structures capable of penetrating neurons. The trapped proteins then harmlessly degrade in the body.

The “clean-up” strategy significantly boosted the survival of lab-grown human neurons under stress from disease-causing proteins.

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New research by scientists at the University of Toronto and the Structural Genomics Consortium has deepened our understanding of how viruses like the flu, common cold, and COVID-19 get into cells in human airways.

Using the Canadian Light Source at the University of Saskatchewan, the researchers identified for the first time the crystal structures of a human protein (TMPRSS11D) that viruses use as a doorway into our body. The study is published in the journal Nature Communications.

Understanding how viruses use our proteins to gain entry into our cells will help researchers develop better ways to stop infections in their tracks.

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Current dental implants can work well, but they’re not perfect. They don’t attach to bones and gums in the same way that real teeth do. And around 20% of people who get implants end up developing an infection called peri-implantitis, which can lead to bone loss.

It is all down to the microbes that grow on them. There’s a complex community of microbes living in our mouths, and disruptions can lead to infection. But these organisms don’t just affect our mouths; they also seem to be linked to a growing number of disorders that can affect our bodies and brains. If you’re curious, read on.

The oral microbiome, as it is now called, was first discovered in 1670 by Antonie van Leeuwenhoek, a self-taught Dutch microbiologist. “I didn’t clean my teeth for three days and then took the material that had lodged in small amounts on the gums above my front teeth … I found a few living animalcules,” he wrote in a letter to the Royal Society at the time.

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Researchers at UC Santa Barbara, UCSF and the University of Pittsburgh have developed a new workflow for designing enzymes from scratch, paving the way toward more efficient, powerful and environmentally benign chemistry. The new method allows designers to combine a variety of desirable properties into new-to-nature catalysts for an array of applications, from drug development to materials design.

This research is published in the journal Science, and is the result of a collaborative effort among the DeGrado lab at UCSF, the Yang lab at UCSB and the Liu lab at the University of Pittsburgh.

“If people could design very efficient enzymes from scratch, you could solve many important problems,” said UCSB chemistry professor Yang Yang, a senior author on the paper.

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In Biology 101, we learn that RNA is a single, ribbon-like strand of base pairs that is copied from our DNA and then read like a recipe to build a protein. But there’s more to the story. Some RNA strands fold into complex shapes that allow them to drive cellular processes like gene regulation and protein synthesis, or catalyze biochemical reactions.

We know that these active molecules, called non-coding RNAs, are present in all life forms, yet we’re just starting to understand their many roles—and how they can be harnessed for applications in environmental science, agriculture, and medicine.

To study—and potentially modify—the functions of non-coding RNAs, we need to determine their structure. Scientists from Lawrence Berkeley National Laboratory (Berkeley Lab) and the Hebrew University of Jerusalem have developed a streamlined process that predicts the structure of an RNA molecule down to the atomic level.

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Most vaccines—and boosters—are injected directly into muscle tissue, usually in the upper arm, to kickstart the body’s immune system in the fight against disease. But for respiratory diseases like COVID-19, it can be important to have protection right where the virus enters: the respiratory tract.

In a new study, Yale researchers have found that nasal vaccine boosters can trigger strong immune defenses in the respiratory tract, even without the help of immune-boosting ingredients known as adjuvants. The findings, researchers suggest, may offer critical insights into developing safer, more effective nasal vaccines in the future.

“Our study shows how a simple viral protein antigen can boost respiratory tract immune responses against viruses,” said Akiko Iwasaki, Sterling Professor of Immunobiology at Yale School of Medicine (YSM) and senior author of the study. “These data imply that viral proteins in may be used as a safe way to promote antiviral immunity at the site of viral entry.”

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Cells have a trick called splicing. They can cut a gene’s message into pieces and decide which fragments to keep. By mixing and matching these fragments, a single gene can produce many different proteins, giving tissues and organs more options to thrive and evolve. Out of all tissues, splicing is most prevalent in the brain.

Researchers at the Center for Genomic Regulation (CRG) have discovered that one such fragment, a “microexon” just nine amino acids long, is inserted into the DAAM1 protein exclusively in neurons and nowhere else in the body. The inclusion of the microexon is critical for healthy neuronal development, with effects rippling all the way up to . The findings are published in Nature Communications.

DAAM1 makes a protein that helps cells maintain their shape and enables their movement. When the team deleted the nine-letter microexon in mice, the animals were healthy at birth, but their adult brain cells had half of the usual “learning spines,” protrusions known to be important for learning and retrieval of memories.

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The ability to detect imminent threats and execute behaviors aimed at protecting oneself, such as hiding, running away or defending oneself, is central to the survival of most animal species. A region of the mammalian brain known to play a key role in threat response is the hypothalamus, which also regulates the release of hormones and other vital bodily functions.

Researchers at California Institute of Technology (Caltech) and Howard Hughes Medical Institute recently carried out a study aimed at better understanding how a specific group of neurons in the dorsomedial subdivision (VMHdm), which are identified by the presence of the steroidogenic factor 1 (SF1) gene, contribute to the coding of predator imminence.

Their findings, published in Neuron, show that distinct subsets of VMHdmSF1 neurons encode multiple internal states that are evoked by the imminence of predators.

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