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7 in total

Review 1. Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases.

Authors: K I Kivirikko; T Pihlajaniemi
Journal: Adv Enzymol Relat Areas Mol Biol Date: 1998

2. Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.

Authors: J Kemmink; N J Darby; K Dijkstra; M Nilges; T E Creighton
Journal: Biochemistry Date: 1996-06-18 Impact factor: 3.162

3. The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency.

Authors: N J Darby; E Penka; R Vincentelli
Journal: J Mol Biol Date: 1998-02-13 Impact factor: 5.469

4. The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules.

Authors: J Kemmink; N J Darby; K Dijkstra; M Nilges; T E Creighton
Journal: Curr Biol Date: 1997-04-01 Impact factor: 10.834

5. Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase.

Authors: N J Darby; T E Creighton
Journal: Biochemistry Date: 1995-09-19 Impact factor: 3.162

6. The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide.

Authors: P Koivunen; A Pirneskoski; P Karvonen; J Ljung; T Helaakoski; H Notbohm; K I Kivirikko
Journal: EMBO J Date: 1999-01-04 Impact factor: 11.598

7. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin.

Authors: J C Edman; L Ellis; R W Blacher; R A Roth; W J Rutter
Journal: Nature Date: 1985 Sep 19-25 Impact factor: 49.962

7 in total

5 in total

Assignment of 1H, 13C and 15N resonances of the a' domain of protein disulfide isomerase.

Review 1. Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases.

2. Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy.

3. The multi-domain structure of protein disulfide isomerase is essential for high catalytic efficiency.

4. The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules.

5. Functional properties of the individual thioredoxin-like domains of protein disulfide isomerase.

6. The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide.

7. Sequence of protein disulphide isomerase and implications of its relationship to thioredoxin.

Review 1. Protein disulfide isomerases exploit synergy between catalytic and specific binding domains.

2. Assignment of 1H, 13C and 15N resonances of the a' domain of ERp57.

3. Mechanistic insights on the reduction of glutathione disulfide by protein disulfide isomerase.

4. Mutations in domain a' of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A.

5. Close correlation between thiolate basicity and certain NMR parameters in cysteine and cystine microspecies.