Changing stroke rehab and research worldwide now.Time is Brain! trillions and trillions of neurons that DIE each day because there are NO effective hyperacute therapies besides tPA(only 12% effective). I have 523 posts on hyperacute therapy, enough for researchers to spend decades proving them out. These are my personal ideas and blog on stroke rehabilitation and stroke research. Do not attempt any of these without checking with your medical provider. Unless you join me in agitating, when you need these therapies they won't be there.

What this blog is for:

My blog is not to help survivors recover, it is to have the 10 million yearly stroke survivors light fires underneath their doctors, stroke hospitals and stroke researchers to get stroke solved. 100% recovery. The stroke medical world is completely failing at that goal, they don't even have it as a goal. Shortly after getting out of the hospital and getting NO information on the process or protocols of stroke rehabilitation and recovery I started searching on the internet and found that no other survivor received useful information. This is an attempt to cover all stroke rehabilitation information that should be readily available to survivors so they can talk with informed knowledge to their medical staff. It lays out what needs to be done to get stroke survivors closer to 100% recovery. It's quite disgusting that this information is not available from every stroke association and doctors group.

Showing posts with label ribosomes. Show all posts
Showing posts with label ribosomes. Show all posts

Tuesday, February 24, 2026

Neurons Use RNA “Tentacles” to Survive Starvation

 Will your competent? doctor and hospital ensure further research occurs that identifies a way to use this to save neurons during and immediately post stroke?

Do you prefer your doctor, hospital and board of director's incompetence NOT KNOWING? OR NOT DOING? Your choice; let them be incompetent or demand action!

Neurons Use RNA “Tentacles” to Survive Starvation

ummary: Neurons are high-energy cells that must find ways to survive when nutrients are scarce. New research has discovered a fascinating survival mechanism: neurons pair up their protein factories (ribosomes) into inactive “disomes” to save energy.

Unlike bacteria, which use proteins to link ribosomes, animal cells use long, flexible RNA “tentacles” called expansion segments. These segments form a “kissing loop” that locks ribosomes together during stress, protecting these expensive molecular machines until favorable conditions return.

Key Facts

  • The Energy-Saving Disome: When stressed (by cold or lack of food), animal cells assemble inactive ribosomes into pairs called disomes to halt costly protein production.
  • RNA Tentacles: The connection is made by a specific ribosomal RNA segment called “31b,” an expansion segment that acts like a tentacle protruding from the ribosome.
  • The “Kissing Loop”: These RNA tentacles bind to each other through complementary sequences, forming a precise, reversible lock.
  • Cryo-ET Visualization: Researchers used cryogenic electron tomography to see these ribosome pairs directly inside intact, frozen cells for the first time.
  • Evolutionary Clue: Expansion segments have grown larger over the course of evolution; this study reveals they play a key role in how complex organisms manage cellular stress.

Source: Max Planck Society

Ribosomes are large molecular machines made of protein and RNA that build all proteins in the cell.

Because protein production is extremely energy-intensive, cells rapidly reduce protein synthesis when stressed. It has long been known that bacterial cells pair their inactive ribosomes into so-called “hibernating disomes” however, such structures had not previously been identified in animal cells.

This is an AI rendering of two ribosomes.
During periods of extreme stress, animal cells use ribosomal RNA expansion segments to form inactive pairs, protecting their protein-making machinery while conserving energy. Credit: Neuroscience

An unexpected role for ribosomal RNA during cellular stress

Using advanced imaging techniques, Erin Schuman and her team at the Department of Synaptic Plasticity at the Max Planck Institute for Brain Research in Frankfurt discovered that stressed animal cells – including neurons – assemble inactive ribosomes into tightly linked pairs, known as disomes. These ribosome pairs are not accidental collisions or artifacts, but a regulated and reversible response to stress.

The new study was published today in Science.

“Surprisingly, the two ribosomes are not held together by proteins, as is common in bacteria. Instead, the connection is made by a specific piece of ribosomal RNA called an expansion segment”, explains one of the lead authors, postdoctoral researcher, Andre Schwarz.

Expansion segments are long, flexible RNA “tentacles” that protrude from ribosomes and have grown larger over the course of evolution. Although they are a prominent feature of animal ribosomes, their functions only just started to emerge. This study now shows that one particular expansion segment, called “31b”, is both necessary and sufficient to link ribosomes together during stress

. At the molecular level, the expansion segment forms a precise RNA-RNA interaction – a so-called “kissing loop” – in which identical RNA loops bind each other through complementary sequences. Disrupting this interaction prevents disome formation, stunts cellular growth and makes cells more sensitive to stress.

Seeing ribosomes inside cells

A key strength of the study was the ability to visualize ribosomes directly inside intact cells using cryogenic electron tomography (Cryo-ET). Cryo-ET is a powerful 3D imaging technique that uses an electron microscope to see inside frozen biological samples (cells, organelles, molecules) with very high resolution. This approach allowed the team to visualize ribosomes in their native environment and resolve how they re-organize during stress.

The study combined an unusually broad range of techniques, including cell biology, biochemistry, yeast and mammalian cell genetic engineering, and high-resolution structural imaging.

“One major challenge was manipulating ribosomal RNA, which is encoded by hundreds to thousands of nearly identical gene copies in animal genomes. We overcame this hurdle by engineering hybrid ribosomes in yeast and by introducing small RNA molecules that specifically disrupted ribosome pairing in animal cells”, says Mara Mueller, graduate student in the Schuman Lab and co-first author of the study.

A new view of translation control

„Our findings uncover a previously unknown mechanism by which animal cells regulate protein synthesis during stress – one that relies on RNA structure. The study reveals a new function for ribosomal RNA expansion segments which have been rather mysterious”, says Erin Schuman.

By temporarily storing ribosomes in inactive pairs, cells protect these costly machines and enable rapid recovery once favorable conditions return. The discovery opens new avenues for understanding how cells adapt to stress and how ribosome organization contributes to health and disease.

Key Questions Answered:

Q: Why would a cell want to stop making proteins?

A: Making proteins is the most energy-intensive thing a cell does. In a crisis (like starvation), a cell has to cut its “spending.” By pairing up ribosomes and putting them in “hibernation,” the cell saves massive amounts of energy to stay alive.

Q: What happens if this pairing process is broken?

A: The study found that if the RNA “kissing loop” is disrupted, cells cannot properly enter hibernation mode. This stunts growth and makes the cells much more likely to die when conditions get tough.

Q: How did they see something this small?

A: They used Cryo-ET, which involves “plunge-freezing” cells so quickly that the water doesn’t form ice crystals. This preserves the cell in its natural state, allowing an electron microscope to take high-resolution 3D pictures of the molecules inside.

Editorial Notes:

  • This article was edited by a Neuroscience News editor.
  • Journal paper reviewed in full.
  • Additional context added by our staff.

About this genetics and neuroscience research news

Author: Irina Epstein
Source: Max Planck Institute
Contact: Irina Epstein – Max Planck Institute
Image: The image is credited to Neuroscience News

Original Research: Closed access.
rRNA expansion segments mediate the oligomerization of inactive animal ribosomes” by Andre Schwarz, Mara Mueller, Helene Will, Lea Dietrich, Stefano L. Giandomenico, Georgi Tushev, Ina Bartnik, Iskander Khusainov, Claudia M. Fusco, Erin M. Schuman. Science
DOI:10.1126/science.adr4287

Wednesday, April 10, 2024

Nobel-winning biologist on the most promising ways to stop ageing

 FYI.

Nobel-winning biologist on the most promising ways to stop ageing

Efforts to extend our lifespan continue and many look promising, but success will have unintended consequences, says Nobel prizewinner Venki Ramakrishnan


By Graham Lawton

18 March 2024New Scientist Default Image

Ula Šveikauskaitė

ANTI-AGEING is big business. From books encouraging diets such as intermittent fasting to cosmetic creams to combat wrinkles, a multibillion-dollar industry has been built on promises to make us live longer and look younger. But how close are we really to extending our lifespan in a way that gives us extra years of healthy life?

Nobel prizewinner Venki Ramakrishnan, a molecular biologist and former president of the UK’s Royal Society, is the latest to tackle this question. He has spent 25 years studying the ribosome, which is where our cells make proteins using the information encoded in our genes, at the MRC Laboratory of Molecular Biology in Cambridge, UK.

In his latest book, Why We Die: The new science of ageing and the quest for immortality, he goes on a journey around the cutting-edge biology of human ageing and asks whether it will be possible to extend our lifespan in the near future.

He talks to New Scientist about the recent breakthroughs in our knowledge of what causes ageing, how close we are to creating therapeutics to combat it, and the potential consequences if we succeed.

Graham Lawton: What inspired you to take a break from a hugely successful career researching how cells make proteins to write a book about ageing?

Venki Ramakrishnan: Two things. One is that the translation of genetic code into proteins affects almost every biological process, and it turns out to be central to many aspects of ageing.

The other reason is that we have worried about ageing and death ever since we…

To continue reading, subscribe today with our introductory offers

about the recent breakthroughs in our knowledge of what causes ageing, how close we are to creating therapeutics to combat it, and the potential consequences if we succeed.

Graham Lawton: What inspired you to take a break from a hugely successful career researching how cells make proteins to write a book about ageing?

Venki Ramakrishnan: Two things. One is that the translation of genetic code into proteins affects almost every biological process, and it turns out to be central to many aspects of ageing.

The other reason is that we have worried about ageing and death ever since we…

To continue reading, subscribe today with our introductory offers

Wednesday, May 17, 2017

Irish team unlock hidden triggers behind Alzheimer’s and Parkinson’s

You need this so demand prevention strategies from your doctor.
1. A documented 33% dementia chance post-stroke from an Australian study?   May 2012.
2. Then this study came out and seems to have a range from 17-66%. December 2013.
3. A 20% chance in this research.   July 2013.

Parkinson’s Disease May Have Link to Stroke


 
https://www.siliconrepublic.com/innovation/alzheimers-parkinsons-breakthrough


A team of researchers from Trinity College Dublin believes it has unlocked the hidden secrets of how Alzheimer’s and Parkinson’s form in the brain.
Due to their damaging effects on the human brain – and friends and family – research into how neurodegenerative diseases develop has been extensive.
Despite the science industry gaining a better understanding over the past few decades, very little remains understood.

However, a research team from Trinity College Dublin’s CRANN nanoscience institute believes it has uncovered some of these mysteries, in the hope of one day being able to create an effective treatment for diseases such as Alzheimer’s and Parkinson’s.
In a paper published online, the team led by Prof Martin Hegner revealed that, for the first time, it has observed how proteins fold while being produced in real time.
The breakthrough was made by analysing individual ribosomes – complex molecules that use genetic information to assemble proteins.
Within each of our cells, there are approximately 7m of these ribosomes, just 20 nanometres in diameter, only determined by science as recently as 2000.
What makes them so important in research into neurodegenerative diseases is that the assembly of proteins in cells is crucial, as they must fold into complex shapes to perform as expected.

‘Pushes the boundaries of what is technically possible’

This protein synthesis had remained a mystery until this latest research, but Hegner and his team found that during this process, chains of amino acids called polypeptides fold into their final 3D structures.
This breakthrough is vital in the development of future medicines for the treatment of these neurodegenerative diseases, among others, and CRANN’s research has already caught the eye of some pharmaceutical companies.
“The ribosome translation machinery is a highly complex system, involving many different factors such as energy input, messenger RNA decoding, amino acids, as well as their relative movements and interactions,” said Hegner on his team’s research.
“Investigating this system at the single-molecule level required a highly ambitious and multifaceted approach that pushes the boundaries of what is technically possible.”

Saturday, March 14, 2015

Ribosomes regulate stem cell fate

There is still so much unknown about stem cells that current research seems more like a shot in the dark that any logical way to proceed. This is one of the many reasons that the miracle of stem cells contributing instantly to Godie Howes' recovery is impossible to believe.
http://www.sciencemag.org/content/347/6227/1214.4.full?utm_campaign=email-sci-ec&utm_src=email
The use of stem cells in regenerative medicine holds enormous therapeutic potential. However, scientists still need to fully understand the molecular signals that control the ability of stem cells to self-renew and differentiate. To identify genes that many regulate this, Fortier et al. screened a library of mouse embryonic stem cells (ESCs) containing chromosomal deletions. They found that the loss of a single copy of several genes encoding protein subunits of the ribosome, a large protein complex that translates mRNA into proteins, resulted in impaired ESC differentiation but did not affect self-renewal.