On the brotherhood of the mitochondrial chaperons mortalin and heat stock protein 60
The heat shock chaperones mortalin/mitochondrial heat shock protein 70 (mtHsp70) and Hsp60 are found in multiple subcellular sites and function in the folding and intracellular trafficking of many proteins. The chaperoning activity of these 2 proteins involves different structural and functional mec...
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oai:animorepository.dlsu.edu.ph:faculty_research-62042022-04-08T07:26:57Z On the brotherhood of the mitochondrial chaperons mortalin and heat stock protein 60 Deocaris, Custer C. Kaul, Sunil C. Wadhwa, Renu The heat shock chaperones mortalin/mitochondrial heat shock protein 70 (mtHsp70) and Hsp60 are found in multiple subcellular sites and function in the folding and intracellular trafficking of many proteins. The chaperoning activity of these 2 proteins involves different structural and functional mechanisms. In spite of providing an excellent model for an evolutionarily conserved molecular "brotherhood", their individual functions, although overlapping, are nonredundant. As they travel to various locations, both chaperones acquire different binding partners and exert a more divergent involvement in tumorigenesis, cellular senescence, and immunology. An understanding of their functional biology may lead to novel designing and development of therapeutic strategies for cancer and aging. 2006-01-01T08:00:00Z text https://animorepository.dlsu.edu.ph/faculty_research/5297 Faculty Research Work Animo Repository Molecular chaperones Heat shock proteins Biology Cell Biology |
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Molecular chaperones Heat shock proteins Biology Cell Biology |
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Molecular chaperones Heat shock proteins Biology Cell Biology Deocaris, Custer C. Kaul, Sunil C. Wadhwa, Renu On the brotherhood of the mitochondrial chaperons mortalin and heat stock protein 60 |
| description |
The heat shock chaperones mortalin/mitochondrial heat shock protein 70 (mtHsp70) and Hsp60 are found in multiple subcellular sites and function in the folding and intracellular trafficking of many proteins. The chaperoning activity of these 2 proteins involves different structural and functional mechanisms. In spite of providing an excellent model for an evolutionarily conserved molecular "brotherhood", their individual functions, although overlapping, are nonredundant. As they travel to various locations, both chaperones acquire different binding partners and exert a more divergent involvement in tumorigenesis, cellular senescence, and immunology. An understanding of their functional biology may lead to novel designing and development of therapeutic strategies for cancer and aging. |
| format |
text |
| author |
Deocaris, Custer C. Kaul, Sunil C. Wadhwa, Renu |
| author_facet |
Deocaris, Custer C. Kaul, Sunil C. Wadhwa, Renu |
| author_sort |
Deocaris, Custer C. |
| title |
On the brotherhood of the mitochondrial chaperons mortalin and heat stock protein 60 |
| title_short |
On the brotherhood of the mitochondrial chaperons mortalin and heat stock protein 60 |
| title_full |
On the brotherhood of the mitochondrial chaperons mortalin and heat stock protein 60 |
| title_fullStr |
On the brotherhood of the mitochondrial chaperons mortalin and heat stock protein 60 |
| title_full_unstemmed |
On the brotherhood of the mitochondrial chaperons mortalin and heat stock protein 60 |
| title_sort |
on the brotherhood of the mitochondrial chaperons mortalin and heat stock protein 60 |
| publisher |
Animo Repository |
| publishDate |
2006 |
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https://animorepository.dlsu.edu.ph/faculty_research/5297 |
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1767196302483914752 |