A method for expression and purification of soluble, active Hsp47, a collagen-specific molecular chaperone

Protein Expression and Purification

Volumn 23, Issue 1, 2001, Pages 8-13

  Thomson, Christy A ^a   Ananthanarayanan, Vettai S ^a  

^a MCMASTER UNIVERSITY   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL CELL; CHAPERONE; COLLAGEN; GEL ELECTROPHORESIS; GENE EXPRESSION SYSTEM; HEAT SHOCK PROTEIN 47; MERCAPTOETHANOL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; SPECIFICITY; SULFUR 35; TEMPERATURE;

EID: 0034804473     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1006/prep.2001.1470     Document Type: Article

References (16)

1. Protein folding in the cell
2. Hsp47: A collagen-specific molecular chaperone
3. Expression and function of heat shock protein 47: A collagen-specific molecular chaperone in the endoplasmic reticulum
4. Cloning of a human collagen-binding protein, and its homology with rat gp46, chick hsp47 and mouse J6 proteins
5. The human genome has only one functional hsp47 gene (CBP2) and a pseudogene (pshsp47)
6. Heat shock protein 47 is expressed in fibrous regions of human atheroma and is regulated by growth factors and oxidized low-density lipoprotein
7. The retention of abnormal type I procollagen and correlated expression of Hsp47 in fibroblasts from a patient with lethal Osteogenesis Imperfecta
8. pH-dependent function, purification, and intracellular location of a major collagen-binding glycoprotein
9. Interaction of procollagen I and other collagens with colligin
10. Structure-function studies on Hsp47: pH-dependent inhibition of collagen fibril formation in vitro
11. Insulin-responsive glucose transporters are concentrated in a cell surface-derived membrane fraction of 3T3-L1 adipocytes
12. Intein-mediated protein ligation: Harnessing nature's escape artists
13. Peptide-dependent stimulation of the ATPase activity of the molecular chaperone BiP is the result of conversion of oligomers to active monomers
14. Caenorhabditis elegans small heat-shock proteins Hsp12.2 and Hsp12.3 form tetramers and have no chaperone-like activity
15. Oligomerization properties of ERp29, an endoplasmic reticulum stress protein
16. Endoplasmic reticulum protein 47 binds specifically to the N-terminal globular domain of the amino-propeptide of the procollagen I α1(I)-chain