Protein aggregation,misfolding and consequential human neurodegenerative diseases |
| |
Authors: | Neha Sami Safikur Rahman Vijay Kumar Sobia Zaidi Asimul Islam Sher Ali |
| |
Affiliation: | 1. Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, New Delhi, India;2. Department of Medical Biotechnology, Yeungnam University, Gyeongsan, South Korea |
| |
Abstract: | Proteins are major components of the biological functions in a cell. Biology demands that a protein must fold into its stable three-dimensional structure to become functional. In an unfavorable cellular environment, protein may get misfolded resulting in its aggregation. These conformational disorders are directly related to the tissue damage resulting in cellular dysfunction giving rise to different diseases. This way, several neurodegenerative diseases such as Alzheimer, Parkinson Huntington diseases and amyotrophic lateral sclerosis are caused. Misfolding of the protein is prevented by innate molecular chaperones of different classes. It is envisaged that work on this line is likely to translate the knowledge into the development of possible strategies for early diagnosis and efficient management of such related human diseases. The present review deals with the human neurodegenerative diseases caused due to the protein misfolding highlighting pathomechanisms and therapeutic intervention. |
| |
Keywords: | Protein misfolding aggregation amyloids pathomechanisms amyotrophic lateral sclerosis stem cell |
|
|