Molecular chaperones ten years on: Introduction

Seminars in Cell and Developmental Biology

Volumn 11, Issue 1, 2000, Pages 1-5

  Ellis, R John ^a  

^a UNIVERSITY OF WARWICK   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; CHAPERONIN; HEAT SHOCK PROTEIN 104; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; POLYPEPTIDE; PROTEIN DISULFIDE ISOMERASE;

CELL FUNCTION; EDITORIAL; MEDICAL RESEARCH; MOLECULAR BIOLOGY; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; ANIMAL; CHEMISTRY; CLASSIFICATION; FORECASTING; HUMAN; PHYSIOLOGY; PROTEIN RENATURATION; REVIEW;

ANIMALS; FORECASTING; HUMANS; MOLECULAR CHAPERONES; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION;

EID: 0034133858     PISSN: 10849521     EISSN: None     Source Type: Journal    
DOI: 10.1006/scdb.1999.0345     Document Type: Article

References (13)

1. Molecular chaperones
2. Do molecular chaperones have to be proteins?
3. Nucleosomes are assembled by an acidic protein which binds histones and transfers them to DNA
4. Proteins as molecular chaperones
5. Discovery of molecular chaperones
6. Molecular chaperones of the ER: Their role in protein folding and genetic disease
7. Molecular chaperones: Proteins essential for the biogenesis of some macromolecular structures
8. Homologous plant and bacterial proteins chaperone oligomeric protein assembly
9. Identification of in vivo substrates of the chaperonin GroEL
10. Macromolecular crowding: Biochemical, biophysical and physiological consequences
11. Effects of macromolecular crowding on protein folding and aggregation
12. Protein misfolding, evolution and disease