scholarly journals Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (PDILT) provide insight into its chaperone activity

2017 ◽  
Vol 293 (4) ◽  
pp. 1192-1202 ◽  
Author(s):  
Huanhuan Li ◽  
Kai Yang ◽  
Wenjia Wang ◽  
Yingbo Niu ◽  
Jun Li ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Chaperone Activity ◽  
Human Protein ◽  
Disulfide Isomerase ◽  
Solution Structures ◽  
Protein Disulfide ◽  
Insight Into

scholarly journals Structural insight into the dimerization of human protein disulfide isomerase

2014 ◽  
Vol 23 (5) ◽  
pp. 618-626 ◽  
Author(s):  
Sara Bastos-Aristizabal ◽  
Guennadi Kozlov ◽  
Kalle Gehring
Keyword(s):  
Protein Disulfide Isomerase ◽  
Human Protein ◽  
Disulfide Isomerase ◽  
Structural Insight ◽  
Protein Disulfide ◽  
Insight Into

scholarly journals The Reduction Potential of the Active Site Disulfides of Human Protein Disulfide Isomerase Limits Oxidation of the Enzyme by Ero1α

2010 ◽  
Vol 285 (38) ◽  
pp. 29200-29207 ◽  
Author(s):  
Joseph E. Chambers ◽  
Timothy J. Tavender ◽  
Ojore B. V. Oka ◽  
Stacey Warwood ◽  
David Knight ◽  
...  
Keyword(s):  
Active Site ◽  
Protein Disulfide Isomerase ◽  
Reduction Potential ◽  
Human Protein ◽  
Disulfide Isomerase ◽  
Protein Disulfide

scholarly journals Red/ox states of human protein disulfide isomerase regulate binding affinity of 17 beta-estradiol

2017 ◽  
Vol 619 ◽  
pp. 35-44 ◽  
Author(s):  
Razieh Karamzadeh ◽  
Mohammad Hossein Karimi-Jafari ◽  
Ali Akbar Saboury ◽  
Ghasem Hosseini Salekdeh ◽  
Ali Akbar Moosavi-Movahedi
Keyword(s):  
Binding Affinity ◽  
Protein Disulfide Isomerase ◽  
Human Protein ◽  
Disulfide Isomerase ◽  
Protein Disulfide

Functional analysis of tunicamycin-inducible gene A polypeptide from Aspergillus niger

2005 ◽  
Vol 83 (5) ◽  
pp. 654-658 ◽  
Author(s):  
Yurong Liang ◽  
Wei Li ◽  
Qing Ma ◽  
Yuying Zhang
Keyword(s):  
Functional Analysis ◽  
Aspergillus Niger ◽  
Substrate Specificity ◽  
Protein Disulfide Isomerase ◽  
Ribonuclease A ◽  
Chaperone Activity ◽  
Disulfide Isomerase ◽  
Chaperone Protein ◽  
Protein Disulfide ◽  
Inducible Gene

Tunicamycin-inducible gene A polypeptide (TIGA) is a member of the protein disulfide isomerase (PDI) family and is suggested to facilitate the folding of nascent polypeptides. The functional properties of TIGA were investigated here. TIGA acted as an isomerase, catalyzing the refolding of denatured and reduced ribonuclease A. TIGA also exhibited chaperone activity in the refolding of denatured prochymosin but not in the refolding of glyceraldehyde 3-phosphate dehydrogenase (GAPDH), indicating that it had substrate specificity with respect to chaperone activity. Detailed study with a series of thioredoxin-motif (trx-motif) mutants revealed that the 2 trx-motifs of TIGA were not equal in activity. The N-terminal trx-motif was more active than the C-terminal trx-motif, and the first cysteine in each trx-motif was necessary for isomerase activity.Key words: tunicamycin-inducible gene A polypeptide (TIGA), protein disulfide isomerase, chaperone, protein refolding.

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