The heat shock response: life on the verge of death.
- K. Richter, M. Haslbeck, J. Buchner
- BiologyMolecules and Cells
- 22 October 2010
The HSP90 chaperone machinery
- Florian H. Schopf, Maximilian M. Biebl, J. Buchner
- BiologyNature reviews. Molecular cell biology
- 21 April 2017
Owing to the importance of HSP90 in the regulation of many cellular proteins, it has become a promising drug target for the treatment of several diseases, which include cancer and diseases associated with protein misfolding.
Some like it hot: the structure and function of small heat-shock proteins
- M. Haslbeck, Titus M. Franzmann, D. Weinfurtner, J. Buchner
- BiologyNature Structural &Molecular Biology
- 1 October 2005
Small heat-shock proteins are a widespread and diverse class of molecular chaperones that maintain protein homeostasis by binding proteins in non-native conformations, thereby preventing substrate aggregation.
Small heat shock proteins are molecular chaperones.
- U. Jakob, M. Gaestel, K. Engel, J. Buchner
- BiologyJournal of Biological Chemistry
- 25 January 1993
Binding of non‐native protein to Hsp25 during heat shock creates a reservoir of folding intermediates for reactivation
- Monika Ehrnsperger, S. Graeber, M. Gaestel, J. Buchner
- BiologyEMBO Journal
- 15 January 1997
The task of sHsps in this context is to efficiently trap a large number of unfolding proteins in a folding‐competent state and thus create a reservoir of non‐native proteins for an extended period of time, allowing refolding after restoration of physiological conditions in cooperation with other chaperones.
Regulation of Hsp27 Oligomerization, Chaperone Function, and Protective Activity against Oxidative Stress/Tumor Necrosis Factor α by Phosphorylation*
- T. Rogalla, Monika Ehrnsperger, M. Gaestel
- BiologyJournal of Biological Chemistry
- 2 July 1999
It is demonstrated that large oligomers of sHsps are necessary for chaperone action and resistance against oxidative stress whereas phosphorylation down-regulates these activities by dissociation of s Hsps complexes to tetramers.
Hsp70 and Hsp90--a relay team for protein folding.
- H. Wegele, L. Müller, J. Buchner
- BiologyReviews of Physiology, Biochemistry and…
- 2004
This review summarizes the current knowledge in the field, including the ATP-dependent regulation of the Hsp70/Hsp90 multichaperone cycle and elucidates the complex interplay and their synergistic interaction.
The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones.
- Jing Li, Joanna Soroka, J. Buchner
- BiologyBiochimica et Biophysica Acta
- 1 March 2012
Hsp26: a temperature‐regulated chaperone
- M. Haslbeck, S. Walke, J. Buchner
- BiologyEMBO Journal
- 1 December 1999
The temperature‐dependent dissociation of the large storage form of Hsp26 into a smaller, active species and the subsequent re‐association to a defined large chaperone–substrate complex represents a novel mechanism for the functional activation of a molecular chaperones.
The architecture of functional modules in the Hsp90 co‐chaperone Sti1/Hop
- Andreas B Schmid, Stephan Lagleder, J. Buchner
- Biology, ChemistryEMBO Journal
- 21 March 2012
Sti1/Hop is a modular protein required for the transfer of client proteins from the Hsp70 to the HSp90 chaperone system in eukaryotes and it is shown that TPR2A is the high affinity Hsp90‐binding site and TPR1 and T PR2B bind HSP70 with moderate affinity.
...
...