Article ; Online: Role of HSP90 in Cancer.
International journal of molecular sciences
2021 Volume 22, Issue 19
Abstract: HSP90 is a vital chaperone protein conserved across all organisms. As a chaperone protein, it correctly folds client proteins. Structurally, this protein is a dimer with monomer subunits that consist of three main conserved domains known as the N- ... ...
| Abstract | HSP90 is a vital chaperone protein conserved across all organisms. As a chaperone protein, it correctly folds client proteins. Structurally, this protein is a dimer with monomer subunits that consist of three main conserved domains known as the N-terminal domain, middle domain, and the C-terminal domain. Multiple isoforms of HSP90 exist, and these isoforms share high homology. These isoforms are present both within the cell and outside the cell. Isoforms HSP90 |
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| MeSH term(s) | Animals ; Carcinogenesis/metabolism ; Carcinogenesis/pathology ; HSP90 Heat-Shock Proteins/metabolism ; Humans ; Molecular Chaperones/metabolism ; Neoplasms/metabolism ; Neoplasms/pathology ; Protein Isoforms/metabolism |
| Chemical Substances | HSP90 Heat-Shock Proteins ; Molecular Chaperones ; Protein Isoforms |
| Language | English |
| Publishing date | 2021-09-25 |
| Publishing country | Switzerland |
| Document type | Journal Article ; Review |
| ZDB-ID | 2019364-6 |
| ISSN | 1422-0067 ; 1422-0067 ; 1661-6596 |
| ISSN (online) | 1422-0067 |
| ISSN | 1422-0067 ; 1661-6596 |
| DOI | 10.3390/ijms221910317 |
| Database | MEDical Literature Analysis and Retrieval System OnLINE |
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