Thanks to economic liberalism in 1990s, Indian families now live more individual nuclear life than ever. Avg neighborhood of city has population like avg village pollution, yet they never socialize like villages. Recently, even villages don’t socialize often (Earlier they used to do it under Dharma-pretext i.e. Satsang, Bhajan, Katha etc). On top of it, for last 24 months, we are under extreme isolation and panic. This directly affect our sleep and lead to malformation and functioning of proteins, results into cellular stress. Cellular stress = Viral infection.
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Being Social – Sleep – Health
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One of the reasons we are more sick now is because we are now living extremely individual life in our isolated urban home in nuclear family setup.
I have observed over the period of time that there is now less or limited social exchange on daily basis.
And those social functions now start with selfie and ends with selfie! 
😀
Not only this, being social is now limited to having drinks together or dinner in restaurant! That is not being social! 😀
सत्संग – time spent with pious is important!
This paper talks about how your social quotient shapes proteins folds. (lol I pity those who take protein supplements for shaping body! Its not protein alone but how the protein is folded! Artificial protein is havoc for body! Avoid! )
In reality, we really don’t need fruit fly experiments to understand this common sense!
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“A lot of elderly people live alone, and so we suspect that stresses from the combination of aging and social isolation creates a double-whammy at the cellular and molecular level,” said senior author Nirinjini Naidoo, PhD, a research associate professor of Sleep Medicine. “If you have an age-related disruption of the UPR response, compounded by sleep disturbances, and then you add social isolation, that may be a very unhealthy cocktail.”
This line of research stemmed from a surprise finding by the new study’s first author, Marishka K. Brown, PhD, who was then a postdoctoral researcher at Penn. She is now Program Director of the National Center on Sleep Disorders Research at the National Heart, Lung, and Blood Institute (NHLBI). While evaluating the effects of aging on the UPR in fruit flies, she noticed that molecular markers of UPR activation were at higher levels in flies kept singly in vials, compared to same-aged flies kept in groups.
“Ultimately, she realized that keeping animals isolated induces a cellular stress response and a higher level of UPR activation,” Naidoo said.
Markers of UPR activation include the protein BiP, a molecular “chaperone” that helps ensure proper protein folding within cells. Proteins, after being synthesized as simple chains of amino acids, are meant to fold into functional shapes, which are often highly complex. This delicate process is easily disturbed when cells are under stress and can lead to the harmful, runaway clumping of unfolded or misfolded proteins.
As its name suggests, the UPR is supposed to protect against this cellular catastrophe. But when it fails to work efficiently to restore proper protein-folding conditions, and stays activated, it can trigger harmful inflammation, suppress normal, healthy cellular activity, and ultimately force the death of the cell. Scientists have found evidence that this inefficient, chronic response becomes more likely with aging. “When animals get older, you start to see a more maladaptive UPR,” Naidoo said.
