scholarly journals 2P144 Four-domain arrangements of Thermophilic Fungal protein disulfide isomerase in redox state revealed by small-angle X-ray scattering(33. Redox enzyme,Poster Session,Abstract,Meeting Program of EABS & BSJ 2006)

2006 ◽  
Vol 46 (supplement2) ◽  
pp. S331
Author(s):  
Toshihiko Oka ◽  
Aya Maeno ◽  
Eiji Kurimoto ◽  
Osamu Asami ◽  
Tsutomu Kajino ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Redox State ◽  
Poster Session ◽  
Redox Enzyme ◽  
Disulfide Isomerase ◽  
Fungal Protein ◽  
X Ray ◽  
Meeting Program ◽  
X Ray Scattering ◽  
Protein Disulfide

[4] Thermophilic fungal protein disulfide isomerase

1998 ◽  
pp. 50-59 ◽  
Author(s):  
Tsutomu Kajino ◽  
Chie Miyazaki ◽  
Osamu Asami ◽  
Masana Hirai ◽  
Yukio Yamada ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Fungal Protein ◽  
Protein Disulfide

scholarly journals Protein disulfide isomerase A1 regulates breast cancer cell immunorecognition in a manner dependent on redox state

2020 ◽  
Vol 44 (6) ◽  
pp. 2406-2418 ◽  
Author(s):  
Rashed Alhammad ◽  
Sasiprapa Khunchai ◽  
Nopprarat Tongmuang ◽  
Thawornchai Limjindaporn ◽  
Pa‑Thai Yenchitsomanus ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Cancer Cell ◽  
Breast Cancer Cell ◽  
Protein Disulfide Isomerase ◽  
Redox State ◽  
Disulfide Isomerase ◽  
Protein Disulfide

scholarly journals Route Exploration and Synthesis of the Reported Pyridone-Based PDI Inhibitor STK076545

2020 ◽  
Author(s):  
Eric Greve ◽  
Sergey Lindeman ◽  
Chris Dockendorff
Keyword(s):  
Protein Disulfide Isomerase ◽  
Enzyme Protein ◽  
Allyl Ester ◽  
Disulfide Isomerase ◽  
X Ray ◽  
Surface Receptors ◽  
Promising Target ◽  
Biological Studies ◽  
Final Compound ◽  
Protein Disulfide

The enzyme protein disulfide isomerase (PDI) is essential for the correct folding of proteins and the activation of certain cell surface receptors, and is a promising target for the treatment of cancer and thrombotic conditions. A previous high-throughput screen identified the commercial compound STK076545 as a promising PDI inhibitor. To confirm its activity and support further biological studies, a resynthesis was pursued of the reported b-keto-amide with an N-alkylated pyridone at the a-position. Numerous conventional approaches were complicated by undesired fragmentations or rearrangements. However, a successful 5-step synthetic route was achieved using an aldol reaction with an a-pyridone allyl ester as a key step. An X-ray crystal structure of the final compound confirmed that the reported structure of STK076545 was achieved, however its lack of PDI activity and inconsistent spectral data suggest that the commercial structure was misassigned.

Disulfide bond formation in refolding of thermophilic fungal protein disulfide isomerase

2001 ◽  
Vol 91 (6) ◽  
pp. 596-598 ◽  
Author(s):  
Takushi Harada ◽  
Eiji Kurimoto ◽  
Kenrou Tokuhiro ◽  
Osamu Asami ◽  
Tomoya Sakai ◽  
...  
Keyword(s):  
Disulfide Bond ◽  
Protein Disulfide Isomerase ◽  
Bond Formation ◽  
Disulfide Bond Formation ◽  
Disulfide Isomerase ◽  
Fungal Protein ◽  
Protein Disulfide
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