Journal article
Protein folding: Chaperones get Hip
Current biology, Vol.6(3), pp.272-275
03/1996
Handle:
https://hdl.handle.net/2376/108157
PMID: 8805243
Abstract
The discovery of a new co-chaperone, Hip, that interacts with Hsp70 underscores the complexity of the Hsp70 ‘chaperone machine’ that mediates early steps of protein folding in cells.
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Details
- Title
- Protein folding: Chaperones get Hip
- Creators
- Thomas Ziegelhoffer - Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USAJill L Johnson - Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USAElizabeth A Craig - Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA
- Publication Details
- Current biology, Vol.6(3), pp.272-275
- Academic Unit
- UNKNOWN
- Publisher
- Elsevier Inc
- Identifiers
- 99900547543301842
- Language
- English
- Resource Type
- Journal article