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| MOLECULAR CHAPERONES IN CELLULAR PROTEIN-FOLDING |
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| Author(s): HARTL FU, MARTIN J |
| Source: CURRENT OPINION IN STRUCTURAL BIOLOGY Volume: 5 Issue: 1 Pages: 92-102 Published: FEB 1995 |
| Times Cited: 107 References: 91 |
| Abstract: Protein folding in the cell requires molecular chaperones. The chaperone proteins of the hsp70 and hsp60 (chaperonin) classes stabilize unfolded or partially folded polypeptides, thereby preventing aggregation, and mediate folding to the native state in ATP-dependent reactions. Recent advances include a more detailed understanding of the mechanistic principles of hsp70 and hsp60 action, the solution of the crystal structure of the chaperonin GroEL, acid the definition of pathways of chaperone-mediated protein folding. |
| Document Type: Article |
| Language: English |
| Reprint Address: HARTL, FU (reprint author), MEM SLOAN KETTERING CANC CTR, HOWARD HUGHES MED INST, 1275 YORK AVE, NEW YORK, NY 10021 USA |
Addresses:
1. MEM SLOAN KETTERING CANC CTR, CELLULAR BIOCHEM & BIOPHYS PROGRAM, NEW YORK, NY 10021 USA |
| Publisher: CURRENT BIOLOGY LTD, 34-42 CLEVELAND STREET, LONDON, ENGLAND W1P 6LB |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: QL448 |
| ISSN: 0959-440X |
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| | | | | | | | | Record from Web of Science® | | | | | | | | | |