A CALM SEA AND BEAUTIFUL DAYS WITH YOU 《波うららかに、めおと日和》 (2025)
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A CALM SEA AND BEAUTIFUL DAYS WITH YOU 《波うららかに、めおと日和》 (2025)
My life partner's qualities
understand and practices religion
Patient
Loyal
Communicative (able to process and express emotions)
Gentle
Attentive (listens well)
Committed to go through the ups and downs of life together
Support each other to be better (seek new knowledge e.g. in parenting, health, religion, current issues, finance)
Awareness in proper management of finances. Conscious spending habit and loans.
Be each other's strength when feeling down
and most of all, enjoy with being in each other's company and be each other's best friend.
At the moment, these are the qualities that I hope and envision my life partner would have.
May Allah, The All Hearing of duas, The Mujeeb, grant my dua. Amiin.
Letter to Raab
Yaa Raab,
Hanya kepadaMu ku mengadu akan kesedihan ku. Dan Engkau wahai Raab ku, lebih mengetahui segala isi hati kami.
Wahai Tuhanku yang menciptakanku dengan penuh rahmat, cinta dan hikmah. Aku beriman dan redha pada apa yang telah Engkau tetapkan untuk ku, Yaa Raab. Dan aku akui segala ketetapanMu adalah yang terbaik untuk ku kerana Engkau Maha Pengasih lagi Maha Bijaksana dalam ilmuMu dan aturanMu. Dari itu Ya Allah, berilah ku keteguhan hati serta kesabaran dalam menjalani ketetapanMu ke atas diriku ini.
Wahai Raab Ku, aku adalah hambaMu yang lemah. Usiaku telah melanjut dan hatiku terasa sunyi. Bukanlah sunyi kerana alpakan Kasih dan RahmatMu. Namun sunyi yang terbit dari fitrahku sebagai manusia.
Wahai Raab ku, Engkau telah menjadikan kami berpasangan dan fitrah kehidupan sekalian makhlukMu adalah berpasangan. Berikanlah ku Ya Raab, pasangan hidup yang baik. Yang dapat memperbaiki urusan Dunia dan Akhirat ku dan menyayangiku seikhlasnya kerana RahmatMu. Kurniakanlah kami keturunan yang soleh dan jadikanlah kami dan keturunan kami dari kalangan orang-orang yang memelihara solat dan sentiasa mendapat RahmatMu di dunia dan akhirat. Limpahkanlah kami dengan rezekiMu yang halal dan tiada putus-putus sehingga kami tidak meminta-minta dari makhlukMu.
Wahai Raab ku yang Maha mendengar, perkenankanlah doaku.
Raabana Aatina Fiddunia Hassanah Wafil Aakhirati Hassanah Waqinna 'Azabannar.
You shaming your brother with his sins is a greater sin than his disobedience.
Ibn al-Qayyim, Madarij al-Salikin 1/195. (via ibn-al-qayyim)
Accept the apology | Ibn Qayyim
The science behind giving up Inside the brain, a group of cells known as nociceptin neurons get very active before a mouse’s breakpoint. They emit nociceptin, a complex molecule that suppresses dopamine, a chemical largely associated with motivation.
Moments of clarity in dementia patients at end of life: Glimmers of hope?
Paradoxical lucidity, the phenomenon where some with severe dementia suddenly regain their memory and exhibit normal behaviors immediately prior to death, may help shed new light on the mechanisms of Alzheimer’s disease.
Unraveling Alzheimer’s: New Study Documents How Brain Cells Go Bad
In the brains of people with Alzheimer’s disease, there are abnormal deposits of amyloid beta protein and tau protein, and swarms of activated immune cells. But scientists do not fully understand how these three major factors combine to drive the disease. Now, UNC School of Medicine and National Institutes of Health researchers have untangled the mystery in lab experiments to reveal why one Alzheimer’s drug currently in development shows promise and how other therapies might reverse the disease process.
(Image caption: Neurons treated with Alzheimer’s-associated proteins exhibit drastic calcium increases (blue, green, yellow, red to white), and the cells form tau-filled beaded structures (shown with arrows) identical to neurons seen in Alzheimer’s patients. Credit: Cohen Lab, UNC School of Medicine)
Led by Todd Cohen, PhD, assistant professor of neurology, UNC scientists used human cell cultures to show how amyloid beta can trigger a dramatic inflammatory response in immune cells and how that interaction damages neurons. Then they showed how that kind of neuron damage leads to the formation of bead-like structures filled with abnormal tau protein. Similar bead-like structures are known to form in the brain cells of people with Alzheimer’s disease.
The UNC researchers also identified two proteins – MMP-9 and HDAC6 – that help promote this harmful, amyloid-to-inflammation-to-tau cascade. These proteins and others associated with them could become drug targets to treat or prevent Alzheimer’s.
“It’s exciting that we were able to observe tau – the major Alzheimer’s protein – inside these beaded structures,” said Cohen, who is also a member of the UNC Neuroscience Center. “We think that preventing these structures from forming would leave people with healthier neurons that are more resistant to Alzheimer’s.”
The findings, published in the journal Cell Reports, were made possible through a collaboration of three UNC labs led by Rick Meeker, PhD, Xian Chen, PhD, and Cohen, as well as the NIH lab of Jau-Shyong Hong, PhD.
To begin the study, Cohen, Meeker, and colleagues exposed immune cells normally found in an activated, inflammatory state in Alzheimer’s brains to tiny clusters of amyloid beta – or oligomers, which are believed to be the most harmful forms of the protein.
“Our thinking was that the amyloid beta oligomers would activate an inflammatory response in these immune cells, as prior research from Meeker suggested, and we wanted to see if this would induce pathological forms of tau when given to neurons,” Cohen said.
The researchers then focused on the fluid in which the immune cells had been growing. This fluid, which was filled with inflammatory factors – or proteins – resembled the fluid in which these cells typically live inside human brains. Cohen’s team added this fluid to cultures of human cortical neurons. The neurons soon developed abnormal, bead-like swellings along their axons and dendrites that were well studied previously in Meeker’s laboratory.
This “neuritic beading” on axons and dendrites has been seen in Alzheimer’s patients and has been considered an early sign of neuronal damage, although it hasn’t been clear how beading was connected to abnormal tau or if the beading led to Alzheimer’s disease.
Cohen’s team then looked for tau in the beads and found a striking accumulation of it, though it was in an abnormal form and undetectable with the usual tools scientists use to detect the type of tau typically seen in Alzheimer’s patients. Instead, the beaded tau was modified in a different way than previously thought. This modification is what Cohen said causes tau to become aggregated.
Tau proteins normally provide structural support for long, railway-like structures called microtubules, which are used to transport key molecules along axons. For reasons that have never been clear, tau proteins in Alzheimer’s-affected neurons have a different pattern. They are detached from microtubules, bear abnormal chemical modifications, and clump into long, tangled, and thread-like aggregates. Whether these tau aggregates actively harm neurons isn’t clear, but prior studies suggested that the loss of tau from microtubules and resulting disruption of axonal transport might cause serious damage.
The finding of abnormal tau in the neuritic beads indicated that these beads could mark tau’s entry into the Alzheimer’s disease process. Within the beads, Cohen’s lab also found high calcium levels, which are known to harm neurons and are considered an important feature of neurons in people with Alzheimer’s.
“We think these neuroinflammatory factors trigger this cascade,” Cohen said. “They flood the neuron with calcium. And we think that once the calcium accumulates, it causes tau to become abnormally modified. This probably leads to a snowball effect: tau detaches from microtubules and is trafficked throughout the neuron, ending up in these beads. One possibility is that these tau-filled beads are the sites where the classic tangle-like aggregates of tau will eventually emerge, which is the hallmark of Alzheimer’s disease.”
A team led by collaborating researcher Xian Chen, PhD, associate professor of biochemistry and biophysics at UNC, used mass spectrometry to sort out the amyloid beta-induced neuroinflammatory molecules that had triggered the calcium influx and neuritic beading. They were able to show that one protein in particular, MMP-9, was responsible for some of this adverse effect.
“MMP-9 is an inflammatory protein shown to be elevated in the brains of Alzheimer’s patients,” Cohen said. “In our study, we show that MMP-9 alone can trigger a calcium influx that floods the neuron.”
The researchers also identified the protein HDAC6, which originates from within neurons and concentrates in the neuritic beads. Normally, HDAC6 is thought to detect unwanted protein aggregates within neurons and transport them away for disposal. However, blocking HDAC6 stopped nearly all beads from forming in Cohen’s lab experiments.
Both of these proteins have been found to be elevated in affected areas of Alzheimer’s brains. Drug companies are now developing and testing HDAC6 inhibitors, which have performed surprisingly well in early studies, although it has not been fully understood how these inhibitors work.
“Our work might explain why HDAC6 inhibitors have shown such early promise,” Cohen said. “And we think our work can help inform the development of other kinds of inhibitors that affect this cascade, particularly those that might impact cognitive processes.”
A therapeutic strategy to block HDAC6 – and/or MMP-9 – might have applications beyond Alzheimer’s. Neuritic beading is seen in several other neurodegenerative diseases as well as after head injury. Scientists have even observed beading to small extents in seemingly healthy elderly brains. Beading might be a general mechanism underlying cognitive decline, Cohen said.
In their study, Cohen and colleagues found some tau-filled neuritic beads in the brains of aged mice. And they discovered that chronic neuroinflammation could induce the beads to form in younger mice.
The researchers are now focused on creating a mouse model to confirm and further investigate the amyloid-to-inflammation-to tau process seen in this Cell Reports study.
“If we can demonstrate this cascade in a wild-type mouse, then we’ll be able to study Alzheimer’s and test therapies in ordinary lab mice without the need for artificial genetic engineering used in traditional Alzheimer’s mouse models,” Cohen said.
Picturesque stream in Brittany, France.
Blood test IDs key Alzheimer’s marker
Decades before people with Alzheimer’s disease develop memory loss and confusion, their brains become dotted with plaques made of a sticky protein – called amyloid beta – that is thought to contribute to the disease and its progression.
Currently, the only way to detect amyloid beta in the brain is via PET scanning, which is expensive and not widely available, or a spinal tap, which is invasive and requires a specialized medical procedure. But now, a study led by researchers at Washington University School of Medicine in St. Louis suggests that measures of amyloid beta in the blood have the potential to help identify people with altered levels of amyloid in their brains or cerebrospinal fluid.
Ideally, a blood-based screening test would identify people who have started down the path toward Alzheimer’s years before they could be diagnosed based on symptoms.
“Our results demonstrate that this amyloid beta blood test can detect if amyloid has begun accumulating in the brain,” said Randall J. Bateman, MD, the Charles F. and Joanne Knight Distinguished Professor of Neurology and the study’s senior author. “This is exciting because it could be the basis for a rapid and inexpensive blood screening test to identify people at high risk of developing Alzheimer’s disease.”
The findings were announced July 19 at the Alzheimer’s Association International Conference in London and published online in the journal Alzheimer’s and Dementia.
As the brain engages in daily tasks, it continually produces and clears away amyloid beta. Some is washed into the blood, and some floats in the cerebrospinal fluid, for example. If amyloid starts building up, though, it can collect into plaques that stick to neurons, triggering neurological damage.
A blood test would be cheaper and less invasive than PET scans or spinal taps, but previous studies have found that measures of total levels of amyloid beta in the blood don’t correlate with levels in the brain.
So Bateman and colleagues measured blood levels of three amyloid subtypes – amyloid beta 38, amyloid beta 40 and amyloid beta 42 — using highly precise measurement by mass spectrometry to see if any correlated with levels of amyloid in the brain.
The researchers studied 41 people ages 60 and older. Twenty-three were amyloid-positive, meaning they had signs of cognitive impairment. PET scans or spinal taps in these patients also had detected the presence of amyloid plaques in the brain or amyloid alterations in the cerebrospinal fluid. The researchers also measured amyloid subtypes in 18 people who had no buildup of amyloid in the brain.
To measure amyloid levels, production and clearance over time, the researchers drew 20 blood samples from each person over a 24-hour period. They found that levels of amyloid beta 42 relative to amyloid beta 40 were consistently 10 to 15 percent lower in the people with amyloid plaques.
“Amyloid plaques are composed primarily of amyloid beta 42, so this probably means that it is being deposited in the brain before moving into the bloodstream,” Bateman said.
“The differences are not big, but they are highly consistent,” he explained. “Our method is very sensitive, and particularly when you have many repeated samples as in this study — more than 500 samples overall — we can be highly confident that the difference is real. Even a single sample can distinguish who has amyloid plaques.”
By averaging the ratio of amyloid beta 42 to amyloid beta 40 over each individual’s 20 samples, the researchers could classify people accurately as amyloid-positive or -negative 89 percent of the time. On average, any single time point was also about 86 percent accurate.
Amyloid plaques are one of the two characteristic signs of Alzheimer’s disease; the other sign is the presence of tangles of a brain protein known as tau. David Holtzman, MD, the Andrew B. and Gretchen P. Jones Professor and head of the Department of Neurology at the School of Medicine, is developing a blood-based test for tau that could complement the amyloid test.
“If we had a blood test for tau as well, we could combine them to get an even better idea of who is most at risk of developing Alzheimer’s disease,” Bateman said. “That would be a huge step forward in our ability to predict, and maybe even prevent, Alzheimer’s disease.”
I’m the coolest kid in the unit tonight 😂
Need
How Toxoplasmosis Exploits Immune Cells to Reach the Brain
Scientists have previously shown that a parasite from cats can infect people’s brain and affect our behaviour. Now, researchers at Stockholm University have discovered how the parasite takes control of our cells.
The research is in PLOS Pathogens. (full open access)
Genetics Study Adds Further Evidence That Education Reduces Alzheimer’s Risk
The theory that education protects against Alzheimer’s disease has been given further weight by new research from the University of Cambridge, funded by the European Union.
The research is in The BMJ. (full open access)
Drug discovery: Alzheimer’s and Parkinson’s spurred by same enzyme
Alzheimer’s disease and Parkinson’s disease are not the same. They affect different regions of the brain and have distinct genetic and environmental risk factors.
But at the biochemical level, these two neurodegenerative diseases start to look similar. That’s how Emory scientists led by Keqiang Ye, PhD, landed on a potential drug target for Parkinson’s.
In both Alzheimer’s (AD) and Parkinson’s (PD), a sticky and potentially toxic protein forms clumps in brain cells. In AD, the troublemaker inside cells is called tau, making up neurofibrillary tangles. In PD, the sticky protein is alpha-synuclein, forming Lewy bodies. Here is a thorough review of alpha-synuclein’s role in Parkinson’s disease.
Ye and his colleagues had previously identified an enzyme (asparagine endopeptidase or AEP) that trims tau in a way that makes it both more sticky and more toxic. In addition, they have found that AEP similarly processes beta-amyloid, another significant bad actor in Alzheimer’s, and drugs that inhibit AEP have beneficial effects in Alzheimer’s animal models.
In a new Nature Structural and Molecular Biology paper, Emory researchers show that AEP acts in the same way toward alpha-synuclein as it does toward tau.
“In Parkinson’s, alpha-synuclein behaves much like Tau in Alzheimer’s,” Ye says. “We reasoned that if AEP cuts Tau, it’s very likely that it will cut alpha-synuclein too.”
A particular chunk of alpha-synuclein produced by AEP’s scissors can be found in samples of brain tissue from patients with PD, but not in control samples, Ye’s team found.
In control brain samples AEP was confined to lysosomes, parts of the cell with a garbage disposal function. But in PD samples, AEP was leaking out of the lysosomes to the rest of the cell.
The researchers also observed that the chunk of alpha-synuclein generated by AEP is more likely to aggregate into clumps than the full length protein, and is more toxic when introduced into cells or mouse brains. In addition, alpha-synuclein mutated so that AEP can’t cut it is less toxic.
Ye cautions that AEP is not the only enzyme that cuts alpha-synuclein into various toxic pieces, and the full-length alpha-synuclein protein is still able to aggregate and cause harm. Also, whether we’re talking about amyloid, tau or alpha-synuclein, protein aggregates are not necessarily toxic to brain cells; that role may be reserved for smaller bundles called oligomers. Nevertheless, Ye says his team is moving on to testing drugs that inhibit AEP in Parkinson’s animal models.
Phase III Immunotherapy Trial For Migraine Shows Promising Results
A new study of fremanezumab, an immunotherapy that counteracts one of the molecules released during migraine, was found successful in reducing the number of days that chronic migraine sufferers experienced headaches.
The research is in New England Journal of Medicine. (full access paywall)