Comparative docking studies of rosmarinic acid and sinesitin to inhibit HSP70
The HSP70 family of heat shock proteins consists of molecular chaperones of approximately 70kDa in size that serve critical roles in protein homeostasis. These adenosine triphosphatases unfold misfolded or denatured proteins and can keep these proteins in an unfolded, folding-competent state. They a...
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Penerbit Universiti Malaysia Pahang
2019
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| Online Access: | http://umpir.ump.edu.my/id/eprint/26608/ http://umpir.ump.edu.my/id/eprint/26608/1/Comparative%20docking%20studies%20of%20rosmarinic.pdf |
| _version_ | 1848822575950462976 |
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| author | V., Mansoureh Nazari Mahmood, Syed Subashini, Raman |
| author_facet | V., Mansoureh Nazari Mahmood, Syed Subashini, Raman |
| author_sort | V., Mansoureh Nazari |
| building | UMP Institutional Repository |
| collection | Online Access |
| description | The HSP70 family of heat shock proteins consists of molecular chaperones of approximately 70kDa in size that serve critical roles in protein homeostasis. These adenosine triphosphatases unfold misfolded or denatured proteins and can keep these proteins in an unfolded, folding-competent state. They also protect nascently translating proteins, promote the cellular or organellar transport of proteins, reduce proteotoxic protein aggregates and serve general housekeeping roles in maintaining protein homeostasis. The HSP70 family is the most conserved in evolution, and all eukaryotes contain multiple members. the HSP70 family of proteins can be thought of as a potent buffering system for cellular stress either from extrinsic (physiological, viral and environmental) or intrinsic (replicative or oncogenic) stimuli. Not surprisingly, cancer cells rely heavily on this buffering system for survival. The overwhelming majority of human tumours overexpress HSP70 family members, and expression of these proteins is typically a marker for poor prognosis. |
| first_indexed | 2025-11-15T02:43:26Z |
| format | Article |
| id | ump-26608 |
| institution | Universiti Malaysia Pahang |
| institution_category | Local University |
| language | English |
| last_indexed | 2025-11-15T02:43:26Z |
| publishDate | 2019 |
| publisher | Penerbit Universiti Malaysia Pahang |
| recordtype | eprints |
| repository_type | Digital Repository |
| spelling | ump-266082021-02-05T03:35:19Z http://umpir.ump.edu.my/id/eprint/26608/ Comparative docking studies of rosmarinic acid and sinesitin to inhibit HSP70 V., Mansoureh Nazari Mahmood, Syed Subashini, Raman QD Chemistry The HSP70 family of heat shock proteins consists of molecular chaperones of approximately 70kDa in size that serve critical roles in protein homeostasis. These adenosine triphosphatases unfold misfolded or denatured proteins and can keep these proteins in an unfolded, folding-competent state. They also protect nascently translating proteins, promote the cellular or organellar transport of proteins, reduce proteotoxic protein aggregates and serve general housekeeping roles in maintaining protein homeostasis. The HSP70 family is the most conserved in evolution, and all eukaryotes contain multiple members. the HSP70 family of proteins can be thought of as a potent buffering system for cellular stress either from extrinsic (physiological, viral and environmental) or intrinsic (replicative or oncogenic) stimuli. Not surprisingly, cancer cells rely heavily on this buffering system for survival. The overwhelming majority of human tumours overexpress HSP70 family members, and expression of these proteins is typically a marker for poor prognosis. Penerbit Universiti Malaysia Pahang 2019 Article PeerReviewed pdf en http://umpir.ump.edu.my/id/eprint/26608/1/Comparative%20docking%20studies%20of%20rosmarinic.pdf V., Mansoureh Nazari and Mahmood, Syed and Subashini, Raman (2019) Comparative docking studies of rosmarinic acid and sinesitin to inhibit HSP70. International Journal of Engineering Technology And Sciences (IJETS), 6 (1). pp. 114-119. ISSN 2289-697X. (Published) http://journal.ump.edu.my/ijets/article/view/2242 http://dx.doi.org/10.15282/ijets.6.1.2019.1010 |
| spellingShingle | QD Chemistry V., Mansoureh Nazari Mahmood, Syed Subashini, Raman Comparative docking studies of rosmarinic acid and sinesitin to inhibit HSP70 |
| title | Comparative docking studies of rosmarinic acid and sinesitin to inhibit HSP70 |
| title_full | Comparative docking studies of rosmarinic acid and sinesitin to inhibit HSP70 |
| title_fullStr | Comparative docking studies of rosmarinic acid and sinesitin to inhibit HSP70 |
| title_full_unstemmed | Comparative docking studies of rosmarinic acid and sinesitin to inhibit HSP70 |
| title_short | Comparative docking studies of rosmarinic acid and sinesitin to inhibit HSP70 |
| title_sort | comparative docking studies of rosmarinic acid and sinesitin to inhibit hsp70 |
| topic | QD Chemistry |
| url | http://umpir.ump.edu.my/id/eprint/26608/ http://umpir.ump.edu.my/id/eprint/26608/ http://umpir.ump.edu.my/id/eprint/26608/ http://umpir.ump.edu.my/id/eprint/26608/1/Comparative%20docking%20studies%20of%20rosmarinic.pdf |