How to nap like a pro

 How to nap during midday: you either know it and love it well, find yourself physically incapable of falling asleep unless it’s nighttime, or like the actor Jon Bernthal, completely reject the entire premise. But whether you’re a devoted daytime dozer who plans a nap into their afternoon schedule, or someone who can’t remember their last siesta, the practice of briefly checking out while the sun is still up is quite divisive.

“Napping is a controversial issue in the sleep community because it may be good for some people and it may be bad for other people,” says Dr Matthew Ebben, an associate professor of psychology and clinical neurology at Weill Cornell Medicine. Dr Ebben is also the associate director of the Center for Sleep Medicine, a multidisciplinary treatment center on New York City’s Upper East Side. A bulk of his job is making recommendations to his patients about how to improve their sleep and daytime alertness. Unfortunately, because napping is such an inexact science, feeling energised is not as simple as taking a short power nap or a two-hour deep snooze.

“If you look at the research, it really depends on what population you’re looking at,” Ebben says. “It’s often recommended that people nap about 90 minutes for optimal athletic performance. To reduce the risk of sleep inertia, the 20-minute recommendation is often given.”

The 20-minute nap has also gained popularity amongst people who don’t conduct sleep research for a living. Office workers, exhausted parents, and sleepyheads everywhere laud the 20-minute repose for being the most efficient, least day-ruining way to fight lethargy. In addition to Dr. Ebben, there’s plenty of other reputable sources who vouch for it as well, including Harvard University, the Mayo Clinic, and the National Institute of Health. But beware of sleep inertia, a term defined by the CDC as “temporary disorientation and decline in performance and/or mood after awakening from sleep.” In other words, that endlessly frustrating (and seemingly unfair) feeling of being even more groggy after taking a nap.

But for the thousands of nappers out there happily indulging in the 20-minute reset, a pertinent question remains: what is the best time to conk out? “When someone’s sleeping during normal nighttime hours, it’s usually recommended that they nap between 1 and 4 o’clock [in the afternoon],” according to Ebben. The key to all sleep-related issues, though, is the big nightly sleep. Many times, the necessity of a mid-afternoon nap stems from not getting deep enough rest during the night. To avoid needing a sunlit nap at all, Ebben says, make sure to be getting quality moonlit sleep. But on the flip side, a strong nap always carries the risk of creating weak sleep. Napping reduces adenosine (the natural reserve of sleep drive that happens in our brains during the day), which needs time to build up again to properly fall asleep at night.

“Every person has a certain 24-hour sleep need,” Ebben begins. “If they dissipate that sleep need at night, they feel alert and refreshed during the day. Now, if you nap during the day, even though you’re getting sufficient sleep at night, it could result in poor-quality sleep at night. But if you’re getting insufficient sleep at night, for whatever reason—you’re working late, you’re going out with friends, whatever—you can break your sleep up. You can nap during the day and sleep a little bit less at night.” (However, sticking to a regular nightly bedtime and sleep schedule is among the most advisable ways to feel your best during the day.)

Another thing Ebben wants to clarify is that, even if you are a strict no-phone-in-bed person—a practice that typically comes from the idea that bed should be a place strictly for going to sleep at night, and should not host any other activities—it is perfectly fine to nap in bed. I tell Ebben that I’ve seen online, and heard from real-life friends, that they nap solely on the couch, as a way to differentiate napping and full-on sleeping to their brain. Ebben calls this a “strange recommendation.”

“When we have folks that have insomnia, one of the treatment elements that we think about is what’s called stimulus control,” Ebben says. “When you pair sleep with your bedroom environment, you’re going to condition yourself to sleep in that environment over time. I mean, a nap is sleep. So if you just go into your bed and you nap and you set your alarm, maybe you want it to be a 20-minute nap, you are theoretically strengthening that conditioning. You’re applying that stimulus control to that situation. Now, if you plan on going on your phone, eating, doing other things in bed, that would not be good for that stimulus control.”

There you have it. Upon a chair, lying bare, on your bed, in a shed…napping can take many different forms. But if you want to take your napping advice from an expert, remember that 90 minutes is best if you want to get in tip-top athletic shape, and 20 minutes is ideal for feeling alert while not accidentally staying up all night. Pinpointing the hours of 1 to 4 P.M. will perfect your routine. And if you aren’t somebody who experiences the magnetic pull of a cat nap, well, Dr. Ebben has a message for that, too.

“Listen to your body. Don’t do it. You’re alert enough!”

 

 

 

This is only for your information, kindly take the advice of your doctor for medicines, exercises and so on.   

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“Harmless” Peptide May Actually Be Linked to Alzheimer’s Disease

 Research from UC Santa Cruz indicates that the P3 peptide—an alternative cleavage product of the amyloid precursor protein—may play a role in Alzheimer’s disease.

For many years, pharmaceutical companies have focused their Alzheimer’s drug development efforts on amyloid beta, a peptide known for forming sticky deposits in the brain. Billions of dollars and decades of research have gone into targeting these accumulations.

However, a biochemist at the University of California, Santa Cruz, says amyloid beta may not be the only peptide involved. A smaller and largely overlooked related peptide may also negatively affect brain cells.

In a new commentary published in the journal ChemBioChem, UC Santa Cruz professor Jevgenij Raskatov highlights peer-reviewed studies conducted by his research group and others showing that a shorter peptide can also gather into microscopic clusters and fibrous structures. This peptide, called P3, may also interact with amyloid β (Aβ) in ways that influence how it builds up and how toxic it becomes, suggesting it could contribute to neurodegeneration as well.

“The P3 peptide is, most likely, not the innocent bystander it was commonly thought to be. There’s still more research to be done. But this could turn Alzheimer’s research on its head,” said Raskatov, whose lab researches amyloid peptides to discover new ways to block toxicity and inform better therapeutics for Alzheimer’s patients. “P3 is a distinct aggregating peptide that is itself potentially neurotoxic and may be contributing to Alzheimer’s disease.”

Alzheimer’s Disease Burden and Limits of Amyloid-Beta Therapies

Alzheimer’s disease is the most common neurodegenerative disorder worldwide. Around 35 million people currently live with the condition, and its global economic impact exceeds $800 billion each year. Researchers expect the number of patients to double by 2050. Despite the intense focus on amyloid beta, most of the more than 400 clinical trials aimed at treating Alzheimer’s by targeting Aβ have failed. Some that showed limited benefit were also associated with serious side effects such as hemorrhages and strokes.

The Aβ peptide forms when a larger protein embedded in brain cell membranes, called the Amyloid Precursor Protein (APP), is cut by two enzymes in sequence. First β-secretase cleaves the protein, followed by γ-secretase. This process produces peptides of different lengths. Among them, those containing 40 or 42 amino acids have received the most attention. These are known as Aβ40 and Aβ42, with Aβ42 being especially prone to forming aggregates and causing toxicity. Because of this, it has been the primary focus of Alzheimer’s drug development for many years.

Existing medications include cholinesterase inhibitors and N-methyl-D-aspartate (NMDA) receptor antagonists. These drugs can temporarily ease symptoms but do not stop the disease from worsening. More recently, antibody-based treatments that target Aβ, such as lecanemab and donanemab, have been approved with the goal of clearing the peptide from the brain.

P3 Peptide Formation and the Overlooked “Amyloid α”

According to Raskatov, however, these approaches have delivered only limited progress. “Progress has been extremely slow, and the current state of the art in Alzheimer’s therapy leaves much to be desired,” he said. “We need fundamentally new approaches to the problem.”

The P3 peptide represents another major fragment generated from the same amyloid precursor protein. In this pathway, the protein is cleaved by α-secretase, followed by γ-secretase. Raskatov refers to this version as “Amyloid α,” or Aα, to help distinguish it from Amyloid beta and clarify its properties. Earlier research had assumed, without directly testing the idea, that P3 could not form amyloid structures, was harmless to cells, and would dissolve easily in water, eventually disappearing from the brain.

Because of those assumptions, the peptide received little scientific attention and was widely dismissed as irrelevant to Alzheimer’s disease. Raskatov, a peptide chemist, and members of his lab chose to challenge that long-standing belief. Over the past five years, they have published three major studies demonstrating clearly that P3 can form amyloid deposits just as readily as Aβ and can even generate them more quickly.

New Research Shows P3 Can Form Amyloid Deposits

Their research also suggests that P3 may damage neurons, although its toxicity appears to be lower than that of Aβ. Raskatov noted that an independent research group in the United Kingdom confirmed and expanded on these findings. At the same time, additional laboratories are beginning to explore how Aβ and Aα may influence one another.

David Teplow, an emeritus professor of neurology at UCLA and a prominent Alzheimer’s researcher, explained that amyloid beta has long been considered the primary cause of the disease. After reviewing Raskatov’s work independently, Teplow believes the field may be starting to reconsider that assumption.

“This re-evaluation has far-reaching consequences for both basic science and clinical research into the causes and treatment of Alzheimer’s disease,” said Teplow, a founding editorial board member of the Journal of Molecular Neuroscience, the American Journal of Neurodegenerative Disease, and editor-in-chief of Progress in Molecular Biology and Translational Science.

Ongoing Confusion and the Need for Further Study

While examining recent studies from other researchers, Raskatov said he was surprised by how his group’s findings have sometimes been interpreted. He identified at least four papers published in respected peer-reviewed journals that cited his work as proof that P3 is harmless and does not form amyloid.

“This is exactly the opposite of what we have actually shown,” Raskatov said. “We remain in the dark on how this sort of grand confusion may have come about. Clearly, there is more work ahead of us.”

 

This is only for your information, kindly take the advice of your doctor for medicines, exercises and so on.   

https://gscrochetdesigns.blogspot.com. one can see my crochet creations  

https://gseasyrecipes.blogspot.com. feel free to view for easy, simple and healthy recipes    

https://kneereplacement-stickclub.blogspot.com. for info on knee replacement

https://GSiyers home remedies.blogspot.com   is the latest addition to my blogs