![Loading...](https://link.springer.com/static/c4a417b97a76cc2980e3c25e2271af3129e08bbe/images/pdf-preview/spacer.gif)
-
Article
Evidence for interaction between Hsp90 and the ER membrane complex
Numerous putative heat shock protein 90 (Hsp90)-interacting proteins, which could represent novel folding clients or co-chaperones, have been identified in recent years. Two separate high-throughput screens in...
-
Article
Protein quality control: chaperones culling corrupt conformations
Achieving the correct balance between folding and degradation of misfolded proteins is critical for cell viability. The importance of defining the mechanisms and factors that mediate cytoplasmic quality contro...
-
Article
Molecular chaperones and the art of recognizing a lost cause
Molecular chaperones have long been heralded as machines for folding and salvaging proteins. However, not every attempt to fold or refold a protein can be successful. Chaperones are known to participate in the...