References
- Freedman R B. Protein disulphide isomerase: multiple roles in the modification of nascent secretory protein. Cell 1989; 57: 1069–72
- Pihlajaniemi T, Helaakoski T, Tasanen K, et al. Molecular cloning of the β subunit of human prolyl 4-hydroxylase. This subunit and protein disulphide isomerase are products of the same gene. EMBO J 1987; 6: 643–9
- Kivirikko K I., Myllylä R, Pihlajaniemi T. Protein hydroxylation: prolyl 4-hydroxylase, an enzyme with four cosubstrates and a multifunctional subunit. FASEB J 1989; 3: 1609–17
- Kivirikko K I., Helaakoski T, Tasanen K, et al. Molecular biology of prolyl 4-hydroxylase. Ann NY Acad Sci 1990; 580: 132–42
- Koivu J, Myllylä R, Helaakoski T, Pihlajaniemi T, Tasanen K, Kivirikko K l. A single polypeptide acts both as the β-subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase. J Biol Chem 1987; 262: 6447–9
- Myllylä R, Kaska D D., Kivirikko K l. The catalytic mechanism of the hydroxylation reaction of peplidyl proline and lysine does not require protein disulphide-isomerase activity. Biochem J 1989; 263: 609–11
- Pelham H RB. Control of protein exit from the endoplasmic reticulum. Annu Rev Cell Biol 1989; 5: 1–23
- Helaakoski T, Vuori K, Myllylä R, Kivirikko K I., Pihlajaniemi T. Molecular cloning of the α-subunit of human prolyl 4-hydroxylase: the complete cDNA-derived amino acid sequence and evidence for alternative splicing of RNA transcripts. Proc Natl Acad Sci USA 1989; 86: 4392–6
- Geetha-Habid M, Noiva R, Kaplan H A., Lennarz W J. Glycosylation site binding protein, a component of oligo-saccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ER. Cell 1988; 54: 1053–60
- Bulleid N J., Freedman R B. Cotranslational glycosylation of proteins in systems depleted of protein disulphide isomerase. EMBO J 1990; 9: 3527–32
- Wetterau J R., Combs K A., Spinner S N., Joiner B J. Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex. J Biol Chem 1990; 265: 9800–7
- Wells W W., Xu D P., Yang Y, Rocque P A. Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. J Biol Chem 1990; 265: 15361–4
- Edman J C., Ellis L, Blacher R W., Roth R A., Rutter W J. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin. Nature 1985; 317: 267–70
- Parkkonen T, Kivirikko K I., Pihlajaniemi T. Molecular cloning of a multifunctional chicken protein acting as the prolyl 4-hydroxylase β-subunit, protein disulphide-isomerase and a cellular thyroid-hormone-binding protein. Comparison of cDNA-deduced amino acid sequences with those in other species. Biochem J 1988; 256: 1005–11
- Bennett C F., Balcarek J M., Varrichio A, Crooke S T. Molecular cloning and complete amino-acid sequence of form-I phosphoinositide-specific phospholipase C. Nature 1988; 334: 268–70
- Hsu M MP, Muhich M L., Boothroyd J C. A developmentally regulated gene of trypanosomes encodes a homologue of rat protein-disulfide isomerase and phosphoinositol-phos-pholipase C. Biochemistry 1989; 28: 6440–6
- Mazzarella R A., Srinivasan M, Haugejorden S M., Green M. ERp72, an abudant luminal endoplasmic reticulum protein, contains three copies of the active site sequences of protein disulfide isomerase. J Biol Chem 1990; 265: 1094–101
- Huang S-H, Tomich J M., Wu H, Jong A, Holcenberg J. Human deoxycytidine kinase. Sequence of cDNA clones and analysis of expression in cell lines with and without enzyme activity. J Biol Chem 1989; 264: 14762–8
- Tasanen K, Parkkonen T, Chow L T., Kivirikko K I., Pihlajaniemi T. Characterization of the human gene for a polypeptide that acts both as the β subunit of prolyl 4-hydroxylase and as protein disulfide isomerase. J Biol Chem 1988; 263: 16218–24