Chaperone (protein) - Wikipedia, the free encyclopedia
Hsp104, the Hsp100 of Saccharomyces cerevisiae, is essential for the propagation of many yeast prions. Deletion of the HSP104 gene results in cells that are unable to propagate ...
Heat shock protein - Wikipedia, the free encyclopedia
The HspC group of Hsp including Hsp90, Grp94: Maintenance of steroid receptors and transcription factors: 100 kDa: ClpB, ClpA, ClpX: Hsp104, Hsp110: Tolerance of extreme temperature
Molecular Cell - Motor Mechanism for Protein Threading through Hsp104
Atypical AAA+ Subunit Packing Creates an Expanded Cavity for Disaggregation by the Protein-Remodeling Factor Hsp104 Cell, Volume 131, Issue 7, 28 December 2007, Pages 1366-1377 ...
Hsp 104, Hsp70, and Hsp40: A Novel Chaperone System that Rescues ...
Hsp104-deficient lysate was derived from YPH499 carrying an the cell, premature exposure of heat-damaged proteins hsp104 :: LEU2 disruption (A1721 made by Y. Kimura).
PLoS Biology: Hsp104-Dependent Remodeling of Prion Complexes Mediates ...
PLoS Biology is an open-access, peer-reviewed journal that features works of exceptional significance in all areas of biological science, from molecules to ecosystems, including ...
PLoS Biology - Hsp104-Dependent Remodeling of Prion Complexes Mediates ...
PLoS Biology is an open-access, peer-reviewed journal that features works of exceptional significance in all areas of biological science, from molecules to ecosystems, including ...
Hsp104 Interacts with Hsp90 Cochaperones in Respiring Yeast -- Abbas ...
The highly abundant molecular chaperone Hsp90 functions with assistance from auxiliary factors, collectively referred to as Hsp90 cochaperones, and the Hsp70 system.
N-Terminal Domain of Yeast Hsp104 Chaperone Is Dispensable for ...
Hsp104 is a hexameric protein chaperone that resolubilizes stress-damaged proteins from aggregates. Hsp104 promotes [PSI +] prion propagation by breaking prion aggregates, which ...
The Cytoplasmic Chaperone Hsp104 Is Required for Conformational Repair ...
Vol. 10, Issue 11, 3623-3632, November 1999 The Cytoplasmic Chaperone Hsp104 Is Required for Conformational Repair of Heat-denatured Proteins in the Yeast Endoplasmic Reticulum
The role of pre-existing aggregates in Hsp104-dependent polyglutamine ...
©Blackwell Publishing Limited Genes to Cells (2004) 9 , 685-696 685 DOI: 10.1111/j.1365-2443.2004.00759.x The role of pre-existing aggregates in Hsp104-dependent polyglutamine ...
