Hsp70 and Hsp90--a relay team for protein folding.

By Harald Wegele, L. Müller, J. Buchner. Reviews of Physiology, Biochemistry and Pharmacology, 2004

619 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/02a1196c21cb9df9e2e7d71c793ecbf09c03c260

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

1. John R. Riordan

In Molecular Biology

1. John R. Yates III
2. John D. Venable
3. L. Whitesell
4. Susan Lindquist
5. Xiaodong Wang
6. John R. Riordan
7. J. Kelly
8. William E. Balch

Citations in the corpus

• HSP90 and the chaperoning of cancer (2005, background): “Their basal levels facilitate normal protein folding and guard the proteome from the dangers of misfolding and aggregatio”
• Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. (2006, background): “…transfection to control the level of protein expression of select Hsp90 cochaperones including p23 (Figure 3) and the immunophilin FKBP8 (Figure 4), which have been previously documented to regulate ATP-dependent folding steps in the cyclic Hsp90-client interaction pathway (Wegele et al., 2004).”