Hsp90 as a capacitor for morphological evolution
Article Abstract:
The heat-shock protein Hsp90 is not always required for protein folding but it is linked to proteins that control cell growth during development. A new study surveys the properties of Drosophila with impaired Hsp90 function. It is shown that almost any resultant body structure can be altered. It is thought that Hsp90 impairment may be sequestered in times of stress by the abundance of unfolded proteins which could cause accelerated morphological evolutionary change.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
User Contributions:
Comment about this article or add new information about this topic:
A high-affinity confrontation of Hsp90 confers tumour selectivity on Hsp90 inhibitors
Article Abstract:
Heat shock protein 90 (Hsp 90) derived from tumour cells has 100-fold higher affinity for 17-allylaminogeldanamycin (17-AAG) than Hsp90 from normal cells is experimentally demonstrated. Results suggest that tumor cells contain Hsp90 complexes in an activated, high-affinity conformation that facilitates malignant progression, and that may represent a unique target for cancer therapeutics.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 2003
User Contributions:
Comment about this article or add new information about this topic:
- Abstracts: Quantum chaos for real. Electrical generation and absorption of phonons in carbon nanotubes
- Abstracts: Economically destructive fires and biodiversity conservation: an Australian perspective. Primate hotspots on Borneo: predictive value for general biodiversity and the effects of taxonomy
- Abstracts: Probing the calcium-induce conformational transition of troponin C with site-directed mutants. The genome sequence of the plant pathogen Xylella fastidiosa
- Abstracts: Impaired migration but not differentiation of haematopoietic stem cells in the absence of beta1 integrins. PTEN maintains haematopoietic stem cells and acts in lineage choice and leukaemia prevention
- Abstracts: A protein kinase homologue controls phosphorylation of ganciclovir in human cytomegalovirus-infected cells. Protein kinase C-alpha activates Raf-1 by direct phosphorylation