scholarly journals Functional analysis of protein disulfide isomerase�P5 in glioblastoma cells as a novel anticancer target

2018 ◽  
Author(s):  
Tomohisa Horibe ◽  
Aya Torisawa ◽  
Yoshie Masuda ◽  
Koji Kawakami
Keyword(s):  
Functional Analysis ◽  
Protein Disulfide Isomerase ◽  
Glioblastoma Cells ◽  
Disulfide Isomerase ◽  
Anticancer Target ◽  
Protein Disulfide

Functional Analysis of Human P5, a Protein Disulfide Isomerase Homologue

2002 ◽  
Vol 132 (3) ◽  
pp. 451-455 ◽  
Author(s):  
M. Kikuchi ◽  
E. Doi ◽  
I. Tsujimoto ◽  
T. Horibe ◽  
Y. Tsujimoto
Keyword(s):  
Functional Analysis ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Protein Disulfide

scholarly journals Crystal Structure and Functional Analysis of Drosophila Wind, a Protein-disulfide Isomerase-related Protein

2003 ◽  
Vol 278 (45) ◽  
pp. 44600-44607 ◽  
Author(s):  
Qingjun Ma ◽  
Chaoshe Guo ◽  
Kathrin Barnewitz ◽  
George M. Sheldrick ◽  
Hans-Dieter Söling ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Functional Analysis ◽  
Protein Disulfide Isomerase ◽  
Related 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.

A Gallium(III) Complex that Engages Protein Disulfide Isomerase A3 (PDIA3) as an Anticancer Target

2020 ◽  
Vol 132 (45) ◽  
pp. 20322-20328
Author(s):  
Hao‐Yan Yin ◽  
Jiu‐Jiao Gao ◽  
Xuemin Chen ◽  
Bin Ma ◽  
Zi‐Shu Yang ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Anticancer Target ◽  
Protein Disulfide

Crystal Structure and Functional Analysis of the Protein Disulfide Isomerase-Related Protein ERp29

2009 ◽  
Vol 385 (5) ◽  
pp. 1630-1642 ◽  
Author(s):  
Naomi N. Barak ◽  
Piotr Neumann ◽  
Madhumati Sevvana ◽  
Mike Schutkowski ◽  
Kai Naumann ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Functional Analysis ◽  
Protein Disulfide Isomerase ◽  
Related Protein ◽  
Disulfide Isomerase ◽  
Protein Disulfide

A Gallium(III) Complex that Engages Protein Disulfide Isomerase A3 (PDIA3) as an Anticancer Target

2020 ◽  
Vol 59 (45) ◽  
pp. 20147-20153 ◽  
Author(s):  
Hao‐Yan Yin ◽  
Jiu‐Jiao Gao ◽  
Xuemin Chen ◽  
Bin Ma ◽  
Zi‐Shu Yang ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Anticancer Target ◽  
Protein Disulfide
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