J. Koivu

A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase.

K. Tasanen, K. Kivirikko, T. Pihlajaniemi, 1987, The Journal of biological chemistry.

Identification of disulfide bonds in carboxy‐terminal propeptides of human type I procollagen

J. Koivu, 1987, FEBS letters.

Protein disulphide-isomerase activity in various cells synthesizing collagen.

T. Pihlajaniemi, R. Myllylä, K. Kivirikko, 1983, European journal of biochemistry.

Molecular cloning of the beta‐subunit of human prolyl 4‐hydroxylase. This subunit and protein disulphide isomerase are products of the same gene.

K. Tasanen, K. Kivirikko, T. Pihlajaniemi, 1987, The EMBO journal.

Interchain disulfide bond formation in types I and II procollagen. Evidence for a protein disulfide isomerase catalyzing bond formation.

R. Myllylä, J. Koivu, 1987, The Journal of biological chemistry.

Protein disulfide-isomerase retains procollagen prolyl 4-hydroxylase structure in its native conformation.

R. Myllylä, J. Koivu, 1986, Biochemistry.

Disulfide bonding as a determinant of the molecular composition of types I, II and III procollagen

J. Koivu, 1987, FEBS letters.