Protein-specific chaperones: The role of hsp47 begins to gel

Current Biology

Volumn 10, Issue 24, 2000, Pages

  Hendershot, Linda M ^a   Bulleid, Neil J ^b  

^a ST JUDE CHILDREN S RESEARCH HOSPITAL   (United States)

^b UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

EID: 0034649591     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0960-9822(00)00850-2     Document Type: Review

References (16)

1. BiP (GRP78), an essential hsp70 resident protein in the endoplasmic reticulum
2. Quality control in the secretory pathway
3. Procollagen folding and assembly: The role of endoplasmic reticulum enzymes and molecular chaperones
4. Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum
5. Hsp47: A collagen-specific molecular chaperone
6. Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis
7. Collagen fibril formation
8. Extracellular matrix 1: Fibril-forming collagens
9. Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP
10. BiP binds type I procollagen pro alpha chains with mutations in the carboxyl-terminal propeptide synthesized by cells from patients with osteogenesis imperfecta
11. Prolyl 4-hydroxylase and its role in collagen synthesis
12. Collagens and their abnormalities in a wide spectrum of diseases
13. Protein disulfide isomerase acts as a molecular chaperone during the assembly of procollagen
14. Hsp47: A molecular chaperone that interacts with and stabilizes correctly-folded procollagen
15. Procollagen traverses the Golgi stack without leaving the lumen of cisternae: Evidence for cisternal maturation
16. Setting the standards: Quality control in the secretory pathway