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Comment by Dr. Krishna Kumari Challa on October 9, 2024 at 6:29am

Nobel Prize in physics awarded to 2 scientists for discoveries that enabled machine learning

Two pioneers of artificial intelligence—John Hopfield and Geoffrey Hinton—won the Nobel Prize in physics Tuesday for helping create the building blocks of machine learning that is revolutionizing the way we work and live.

 These two gentlemen were really the pioneers. The artificial neural networks—interconnected computer nodes inspired by neurons in the human brain—the researchers pioneered are used throughout science and medicine and "have also become part of our daily lives.

There are enormous benefits, its rapid development has also raised concerns about our future. Collectively, humans carry the responsibility for using this new technology in a safe and ethical way for the greatest benefit of humankind, the Nobel committee says.

 www.nobelprize.org/prizes/phys … dvanced-information/

Comment by Dr. Krishna Kumari Challa on October 8, 2024 at 12:55pm

Researchers found fuel-producing microbes that eat carbon monoxide—a highly toxic, flammable gas that is generated, among other things, during steel production. Currently, the steel industry produces approximately 2 billion tons of steel per year, and carbon monoxide comprises between 20% and 30% of their waste gases. That waste carbon monoxide is currently burned to produce carbon dioxide. It is less toxic, but still quite harmful. However, carbon monoxide-consuming microbes could turn these vast quantities of waste gas into green fuel.
Some carbon monoxide-consuming microbes can produce ethanol, a biofuel that has already been blended into normal fuels for several decades to make them a bit greener.

https://theconversation.com/meet-the-microbes-that-transform-toxic-...

Part 2

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Comment by Dr. Krishna Kumari Challa on October 8, 2024 at 12:52pm

The microbes that transform toxic carbon monoxide into valuable biofuel

Microbes live everywhere, in enormous numbers. We might not see them with the naked eye, but they are in soils, lakes, oceans, hydrothermal vents, our homes, and even in and on our own bodies. And they don't just hang out there. They are always eating. Altogether, they eat so much that they influence the elemental cycles of the entire planet. 

Many of the microbes living on our planet do their utmost to keep these elemental cycles running in perfect balance. The fact of the matter is, though, that human interventions have significantly shifted the balance of more than one of them.
That sounds rather grim—and in part it is. It is time for a change. The key to change might lie in the simple trait that we share with every living organism on Earth. Everything needs food, from the microscopically small to the biggest blue whales. For microbes, food can include pretty much anything. Some microbes feed on apples; others prefer milk sugars (lactose) and help us make yogurt and cheese; and many, many microbes like the taste of waste.

This is extremely handy when it comes to cleaning our sewage water, for example. Billions of microbes in wastewater treatment plants happily gobble up all the nutrients in the water that's flushed down our drains. This reduces our risk of getting sick and helps improve surface water quality. Pretty amazing, right?

Some microbes on our planet can turn their food into our fuels. They, too, feed on waste.

Part 1

Comment by Dr. Krishna Kumari Challa on October 8, 2024 at 12:45pm

MicroRNAs are particularly promising for fighting cancer because some of these switches act as a tumor suppressor, so they put a brake on cells dividing inappropriately.
Because many viruses use microRNAs, several antiviral drugs are at varying stages of development, including for hepatitis C.

One complicating factor has been that microRNAs can be unstable.

But scientists also hope they can be used as a test called a "biomarker", which could reveal what type of cancer a patient could be suffering from, for example.
It also appears probable that microRNAs could be involved in the evolution of our species.
Part 2

Comment by Dr. Krishna Kumari Challa on October 8, 2024 at 12:44pm

What is microRNA? 

The Nobel Prize in Medicine was awarded on Monday to two US scientists for discovering microRNA, a previously unknown type of genetic switch which is hoped can pave the way for new medical breakthroughs.

But while several treatments and tests are under development using microRNAs against cancer, heart disease, viruses and other illnesses, none have actually yet reached patients.

And the world paid little attention when the new Nobel laureates Victor Ambros and Gary Ruvkun revealed their discovery decades ago, thinking it was just "something weird about worms".

How exactly these tiny genetic switches work inside our bodies?

Each cell in the human body has the same set of instructions, called DNA. Some turn into brain cells, while others become muscles.

So how do the cells know what to become? The relevant part of the DNA's instructions is pointed to via a process called gene regulation.

Ribonucleic acid (RNA) normally serves as a messenger. It delivers the instructions from the DNA to proteins, which are the building blocks of life that turn cells into brains—or muscles.

A good example  is the messenger RNA vaccines rolled out against COVID-19 during the pandemic, which insert a message with new instructions to build proteins that block viruses.

But the two new Nobel winners Ambros and Ruvkun discovered a whole new type of gene regulator that had previously been overlooked by science.

Rather than being the messenger which relays information, microRNA instead acts as a switch to turn other genes off and on.

This was a whole new level of control that we had totally missed.

The discovery of microRNAs brought an additional level of complexity by revealing that regions that were thought to be non-coding play a role in gene regulation.

Part 1

Comment by Dr. Krishna Kumari Challa on October 8, 2024 at 12:35pm

More detailed observations showed that the fused comb jellies had spontaneous movements for the first hour. After that, the timing of contractions on each lobe started to synch up more. After just two hours, 95% of the fused animal's muscle contractions were completely synchronous, they report.

They also looked closely at the digestive tract to find that it also had fused. When one of the mouths ingested fluorescently labeled brine shrimp, the food particles worked their way through the fused canal. Eventually, the comb jelly expelled waste products from both anuses, although not at the same time.
The allorecognition mechanisms are related to the immune system, and the fusion of nervous systems is closely linked to research on regeneration.

Rapid Physiological Integration of Fused Ctenophores, Current Biology (2024). DOI: 10.1016/j.cub.2024.07.084. www.cell.com/current-biology/f … 0960-9822(24)01023-6

Part 2

Comment by Dr. Krishna Kumari Challa on October 8, 2024 at 12:34pm

After injury,  comb jellies can fuse to become one!

Researchers reporting in the journal Current Biology on October 7 have made the surprising discovery that one species of comb jelly (Mnemiopsis leidyi) can fuse, such that two individuals readily turn into one following an injury. Afterwards, they rapidly synchronize their muscle contractions and merge digestive tracts to share food.

These  findings suggest that ctenophores may lack a system for allorecognition, which is the ability to distinguish between self and others.

Additionally, the data imply that two separate individuals can rapidly merge their nervous systems and share action potentials.

Researchers made the observation after keeping a population of the comb jellies in a seawater tank in the lab. They noticed an unusually large individual that seemed to have two backends and two sensory structures known as apical organs instead of one. They wondered if this unusual individual arose from the fusion of two injured jellies.

To find out, they removed partial lobes from other individuals and placed them close together in pairs. It turned out that, nine out of 10 times, it worked. The injured individuals became one, surviving for at least three weeks.

Further study showed that after a single night, the two original individuals seamlessly became one with no apparent separation between them. When the researchers poked at one lobe, the whole fused body reacted with a prominent startle response, suggesting that their nervous systems were also fully fused.

Mechanical stimulation applied to one side of the fused ctenophore resulted in a synchronized muscle contraction on the other side

Part 1

Comment by Dr. Krishna Kumari Challa on October 8, 2024 at 12:25pm

They found that the δ1 tail interacts more extensively with the main part of the protein, leading to greater self-inhibition compared to δ2. This means that δ1 is more tightly regulated by its tail than δ2. When these sites are mutated or removed, δ1 becomes more active, which leads to changes in circadian rhythms. In contrast, δ2 does not have the same regulatory effect from its tail region.
This discovery highlights how a small part of CK1δ can greatly influence its overall activity. This self-regulation is vital for keeping CK1δ activity balanced, which, in turn, helps regulate our circadian rhythms.

The study also addressed the wider implications of these findings. CK1δ plays a role in several important processes beyond circadian rhythms, including cell division, cancer development, and certain neurodegenerative diseases. By better understanding how CK1δ's activity is regulated, scientists could open new avenues for treating not just circadian rhythm disorders but also a range of conditions.

Rachel L. Harold et al, Isoform-specific C-terminal phosphorylation drives autoinhibition of Casein kinase 1, Proceedings of the National Academy of Sciences (2024). DOI: 10.1073/pnas.2415567121

Part 2

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Comment by Dr. Krishna Kumari Challa on October 8, 2024 at 12:24pm

End of Jetlag: Scientists discover secret to regulating our body clock

Scientists have discovered a revolutionary way to put an end to jet lag by uncovering the secret at the tail end of Casein Kinase 1 delta (CK1δ), a protein that regulates our body clock. This breakthrough, achieved by researchers  offers a new approach to adjusting our circadian rhythms, the natural 24-hour cycles that influence sleep-wake patterns and overall daily functions.

Published in the journal Proceedings of the National Academy of Sciences (PNAS), their findings could pave the way for new approaches to treating disorders related to the body clock.

CK1δ regulates circadian rhythms by tagging other proteins involved in our biological clock to fine-tune the timing of these rhythms. In addition to modifying other proteins, CK1δ itself can be tagged, thereby altering its own ability to regulate the proteins involved in running the body's internal clock.

Previous research identified two distinct versions of CK1δ, known as isoforms δ1 and δ2, which vary by just 16 building blocks or amino acids right at the end of the protein in a part called the C-terminal tail. Yet these small differences significantly impact CK1δ's function. While it was known that when these proteins are tagged, their ability to regulate the body clock decreases, no one knew exactly how this happened.

Using advanced spectroscopy and spectrometry techniques to zoom in on the tails, the researchers found that how the proteins are tagged is determined by their distinct tail sequences.

The findings pinpoint to three specific sites on CK1δ's tail where phosphate groups can attach, and these sites are crucial for controlling the protein's activity. When these spots get tagged with a phosphate group, CK1δ becomes less active, which means it doesn't influence our circadian rhythms as effectively. Using high-resolution analysis, we were able to pinpoint the exact sites involved .

Part 1

Comment by Dr. Krishna Kumari Challa on October 8, 2024 at 12:17pm

Such editing, the team notes, is particularly challenging due to issues with delocalization—prior attempts have involved applying high temperatures or radiation. Neither approach has been found to be suitable.

In this new approach, the team used light as a photocatalyst for activating a furan ring. The technique can be used to carry out single electron oxidation on a furan, resulting in radicalization.

The approach, they note, allows for a facile reaction that is susceptible to the addition of an amine. That leads to a cascade of electron and proton transfer between the product and the photocatalyst, resulting in the creation of a ring aldehyde intermediate.

Donghyeon Kim et al, Photocatalytic furan-to-pyrrole conversion, Science (2024). DOI: 10.1126/science.adq6245

Ellie F. Plachinski et al, Single-atom editing with light, Science (2024). DOI: 10.1126/science.ads2595

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