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.
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.”
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.”
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