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Number of items: 9.

E

Erskine, Peter T., Senior, Natalie, Maignan, S., Cooper, J., Lambert, Richard, Lewis, Gareth, Spencer, Paul, Awan, Sarah, Warren, Martin J., Tickle, Ian J., and others. (1997) Crystallization of 5-aminolaevulinic acid dehydratase from Escherichia coli and Saccharomyces cerevisiae and preliminary X-ray characterization of the crystals. Protein Science, 6 (8). pp. 1774-6. ISSN 0961-8368. (doi:10.1002/pro.5560060820) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:11092)

J

James, David C., Goldman, Merlin H., Hoare, Michael, Jenkins, Nigel, Oliver, Ronald W. A., Green, Brian N., Freedman, Robert B. (1996) Posttranslational processing of recombinant human interferon-gamma in animal expression systems. Protein Science, 5 (2). pp. 331-340. ISSN 0961-8368. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:19260)

L

Lamb, Heather K., Ren, Jingshan, Park, Alison, Johnson, Christopher, Leslie, Kris, Cocklin, Simon, Thompson, Paul, Mee, Christopher, Cooper, Alan, Stammers, David K., and others. (2004) Modulation of the ligand binding properties of the transcription repressor NmrA by GATA‐containing DNA and site‐directed mutagenesis. Protein Science, 13 (12). pp. 3127-3138. ISSN 0961-8368. (doi:10.1110/ps.04958904) (KAR id:115041)

R

Ruddock, Lloyd W., Freedman, Robert B., Klappa, Peter (2000) Specificity in substrate binding by protein folding catalysts: Tyrosine and tryptophan residues are the recognition motifs for the binding of peptides to the pancreas-specific protein disulfide isomerase PDIp. Protein Science, 9 (4). pp. 758-764. ISSN 0961-8368. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:16590)

Reader, JS, van Nuland, NAJ, Thompson, GS, Ferguson, SJ, Dobson, CM, Radford, SE (2001) A partially folded intermediate species of the beta-sheet protein apo-pseudoazurin is trapped during proline-limited folding. Protein Science, 10 . pp. 1216-1224. ISSN 0961-8368. (doi:10.1110/ps.52801) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:71825)

T

Thompson, GS, Radford, SE, Leung, Y-C, Redfield, C, Ferguson, SJ (2000) The structure and dynamics in solution of Cu(I) pseudoazurin from Paracoccus pantotrophus. Protein Science, 9 . pp. 846-858. ISSN 0961-8368. (doi:10.1110/ps.9.5.846) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:71828)

V

Vinci, Floriana, Ruoppolo, Margherita, Pucci, Piero, Freedman, Robert B., Marino, Gennaro (2000) Early intermediates in the PDI-assisted folding of ribonuclease A. Protein Science, 9 (3). pp. 525-535. ISSN 0961-8368. (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:16708)

W

Winter, Jeannette, Gleiter, Stefan, Klappa, Peter, Lilie, Hauke (2011) Protein disulfide isomerase isomerizes non-native disulfide bonds in human proinsulin independent of its peptide-binding activity. Protein Science, 20 (3). pp. 588-596. ISSN 0961-8368. (doi:10.1002/pro.592) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:31384)

Wallis, Anne Katrine, Sidhu, Ateesh, Byrne, Lee J., Howard, Mark J., Ruddock, Lloyd W., Williamson, Richard A., Freedman, Robert B. (2009) The ligand-binding b' domain of human protein disulphide-isomerase mediates homodimerization. Protein Science, 18 (12). pp. 2569-2577. ISSN 0961-8368. (doi:10.1002/pro.270) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:28017)

This list was generated on Thu Jun 4 00:01:22 2026 BST.