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FEBS Letters, ISSN 0014-5793, 2004, Volume 566, Issue 1, pp. 311 - 315
We have reported that human protein disulfide isomerase‐related protein (hPDIR) has isomerase and chaperone activities that are lower than those of the human... 
Protein disulfide isomerase | CXXC motif | Domain mutation | Protein disulfide isomerase-related protein | Chaperone activity | SDS–PAGE, sodium dodecyl sulfate–polyacrylamide gel electorophoresis | hPDI, human protein disulfide isomerase | hPDIR, human protein disulfide isomerase-related protein | GSH, glutathione (reduced form) | GSSG, glutathione (oxidized form) | ER, endoplasmic reticulum | SDS-PAGE, sodium dodecyl sulfate-polyacrylamide gel electorophoresis | SITE | chaperone activity | MUTAGENESIS | BIOPHYSICS | protein disulfide isomerase | BIOCHEMISTRY & MOLECULAR BIOLOGY | VIABILITY | CALCIUM-BINDING | domain mutation | protein disulfide isomerase-related protein | CELL BIOLOGY | Protein Structure, Tertiary | Recombinant Proteins - metabolism | Amino Acid Sequence | Molecular Chaperones - metabolism | Oxidation-Reduction | Protein Structure, Secondary | Protein Disulfide-Isomerases - metabolism | Humans | Molecular Chaperones - genetics | Molecular Sequence Data | Recombinant Proteins - chemistry | Spectrometry, Fluorescence | Recombinant Proteins - genetics | Molecular Chaperones - chemistry | Protein Folding | Amino Acid Motifs | Proteins - genetics | Protein Disulfide-Isomerases - genetics | Proteins - metabolism | Escherichia coli - genetics | Escherichia coli - metabolism | Protein Disulfide-Isomerases - chemistry | Mutation | Proteins - chemistry
Journal Article
Biochemical Journal, ISSN 0264-6021, 08/2004, Volume 382, Issue 1, pp. 169 - 176
Polyclonal antibodies that had been raised against particular PDI (protein disulphide-isomerase) family proteins did not cross-react with other PDI family... 
Protein disulphide-isomerase-related protein (PDIR) | Motif mutation | CXXC motif | Phage antibody library | Protein disulphide-isomerase | Single-chain antibody fragment | phage antibody library | single-chain antibody fragment | BIOCHEMISTRY & MOLECULAR BIOLOGY | SYNTHETIC REPERTOIRES | protein disulphide-isomerase | LYSOZYME | CLEAVAGE | motif mutation | CHAPERONE ACTIVITY | IN-VITRO | THIOREDOXIN | SEQUENCE | MOLECULAR-CLONING | HUMAN P5 | protein disulphide-isomerase-related protein (PDIR) | GENE SEGMENTS | Amino Acid Sequence | Antibody Specificity | Sequence Analysis, Protein - methods | Protein Disulfide-Isomerases - metabolism | Humans | Molecular Sequence Data | Peptide Library | Immunoglobulin Fragments | Cross Reactions | Protein Disulfide-Isomerases - immunology | Animals | Amino Acid Motifs - immunology | Cattle | Lysine - metabolism | Antibodies, Monoclonal - metabolism | Antibodies, Monoclonal - chemistry | CaBP1, calcium-binding protein 1 | scFv, single-chain antibody fragment of variable region | Trx domain, thioredoxin-like domain | RU, resonance unit | hPDIR, hPDI-related protein | hPDI, bPDI, yPDI, human, bovine and yeast PDI respectively | PDIR, PDI-related protein | pfu, plaque-forming units | hP5, human P5 | CDR, complementarity-determining regions | ER, endoplasmic reticulum | PDI, protein disulphide-isomerase
Journal Article
Journal of Virology, ISSN 0022-538X, 02/2009, Volume 83, Issue 3, pp. 1483 - 1491
Journal Article
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