Results 11 to 20 of about 83,411 (273)

Dual roles for a tick protein disulfide isomerase during the life cycle of the Lyme disease agent [PDF]

mBio
The protein disulfide isomerase (PDI) family is a group of enzymes that have thiol-disulfide oxidoreductase, disulfide isomerase, and redox-dependent chaperone activities.
Xiaotian Tang, Yingjun Cui, Ushuu Namarra, Xiuqi Tian, Freddie Rivas-Giorgi, Erol Fikrig   +5 more
doaj   +2 more sources

Selective Inhibition of Protein Disulfide Isomerase by Estrogens

Journal of Biological Chemistry, 1989
Protein disulfide isomerase (PDI) is a multifunctional microsomal enzyme that participates in the formation of protein disulfide bonds. PDI catalyzes the reduction of protein disulfide bonds in the presence of excess reduced glutathione and has been implicated in the reductive degradation of insulin; E.
John C.M. Tsibris, Lois T. Hunt, Gustavo Ballejo, Winona C. Barker, L J Toney, William N. Spellacy   +5 more
openalex   +4 more sources

Protein disulfide isomerase A3 as novel biomarker for endometrial cancer [PDF]

Frontiers in Oncology, 2023
ObjectiveThis study aims to investigate the potential of PDIA3 as a novel prognostic biomarker and therapeutic target for Endometrial Cancer (EC) with the ultimate goal of improving survival rates in EC patients.MethodsThis study employed a combination ...
Fanrong Yu, Xin Liu, Min Li, Xiufen Liu, Xintai Wang, Xintai Wang, Meixiang Guo   +6 more
doaj   +2 more sources

Protein disulfide isomerase is essential for spermatogenesis in mice. [PDF]

JCI Insight
Spermatogenesis requires precise posttranslational control in the endoplasmic reticulum (ER), but the mechanism remains largely unknown. The protein disulfide isomerase (PDI) family is a group of thiol oxidoreductases responsible for catalyzing the disulfide bond formation of nascent proteins.
Zhang Y, Yang A, Zhao Z, Chen F, Yan X, Han Y, Wu D, Wu Y.   +7 more
europepmc   +3 more sources

Protein disulfide isomerase is essential for osteoblast differentiation in mice [PDF]

Communications Biology
Protein disulfide isomerase (PDI) is an oxidoreductase responsible for the formation, reduction and isomerization of disulfide bonds of nascent proteins in endoplasmic reticulum (ER).
Yue Lu, Aizhen Yang, Zhenzhen Zhao, Yue Han, Depei Wu, Yi Wu   +5 more
doaj   +2 more sources

Identification and Functional Analysis of a Protein Disulfide Isomerase (AtPDI1) in Arabidopsis thaliana

Frontiers in Plant Science, 2018
Protein disulfide isomerase (PDI) catalyzes the conversion of thiol-disulfide and plays an important role in various physiological events in animals. A PDI (OaPDI) from a tropical plant was detailed studied and it was found to be involved in response of ...
Zhengrong Zhang, Xin Liu, Rong Li, Li Yuan, Yaqing Dai, Xiaoyun Wang   +5 more
doaj   +2 more sources

Disturbed flow regulates protein disulfide isomerase A1 expression via microRNA-204 [PDF]

Frontiers in Physiology
Redox processes can modulate vascular pathophysiology. The endoplasmic reticulum redox chaperone protein disulfide isomerase A1 (PDIA1) is overexpressed during vascular proliferative diseases, regulating thrombus formation, endoplasmic reticulum stress ...
Leonardo Y. Tanaka, Sandeep Kumar, Lucas F. Gutierre, Celso Magnun, Daniela Kajihara, Dong-Won Kang, Francisco R. M. Laurindo, Hanjoong Jo   +7 more
doaj   +2 more sources

Discrimination between Native and Non-native Disulfides by Protein-disulfide Isomerase [PDF]

Journal of Biological Chemistry, 2001
The folding assistant and chaperone protein-disulfide isomerase (PDI) catalyzes disulfide formation, reduction, and isomerization of misfolded proteins. PDI substrates are not restricted to misfolded proteins; PDI catalyzes the dithiothreitol (DTT)-dependent reduction of native ribonuclease A, microbial ribonuclease, and pancreatic trypsin inhibitor ...
Ji Zheng, Hiram Gilbert
openalex   +5 more sources

Identification of protein disulfide isomerase 1 as a key isomerase for disulfide bond formation in apolipoprotein B100 [PDF]

Molecular Biology of the Cell, 2015
Apolipoprotein (apo) B is an obligatory component of very low density lipoprotein (VLDL), and its cotranslational and posttranslational modifications are important in VLDL synthesis, secretion, and hepatic lipid homeostasis. ApoB100 contains 25 cysteine residues and eight disulfide bonds. Although these disulfide bonds were suggested to be important in
Wang, Shiyu, Park, Shuin, Kodali, Vamsi K, Han, Jaeseok, Yip, Theresa, Chen, Zhouji, Davidson, Nicholas O, Kaufman, Randal J   +7 more
openaire   +6 more sources

Novel anti-thrombotic agent for modulation of protein disulfide isomerase family member ERp57 for prophylactic therapy [PDF]

Scientific Reports, 2015
Protein disulfide isomerase (PDI) family members including PDI and ERp57 emerge as novel targets for anti-thrombotic treatments, but chemical agents with selectivity remain to be explored.
G. Cui, L. Shan, Lin Guo, Ivan Keung Chu, Guohui Li, Q. Quan, Yun Zhao, Cheong-Meng Chong, Zaijun Zhang, Pei Yu, M. Hoi, Yewei Sun, Yuqiang Wang, S. M. Lee   +13 more
semanticscholar   +3 more sources