Results 161 to 170 of about 86,419 (320)

Folding of peptides and proteins: role of disulfide bonds, recent developments

Biomolecular Concepts, 2013
Disulfide-containing proteins are ideal models for studies of protein folding as the folding intermediates can be observed, trapped, and separated by HPLC during the folding reaction.
Hidaka Yuji, Shimamoto Shigeru
doaj   +1 more source

Differential activity of rice protein disulfide isomerase family members for disulfide bond formation and reduction

FEBS Open Bio, 2014
Protein disulfide isomerases (PDIs), a family of thiol-disulfide oxidoreductases that are ubiquitous in all eukaryotes, are the principal catalysts for disulfide bond formation. Here, we investigated three rice (Oryza sativa) PDI family members (PDIL1;1,
Yayoi Onda, Yohei Kobori
doaj   +1 more source

Proapoptotic Activities of Protein Disulfide Isomerase (PDI) and PDIA3 Protein, a Role of the Bcl-2 Protein Bak [PDF]

, 2015
Guoping Zhao, Huayi Lü, Chi Li
openalex   +1 more source

Proteomic Analysis of Regulated Dendritic Cell Endosomes Reveals Dynamic Adaptation to Antigen Uptake and Cross‐Presentation

European Journal of Immunology, Volume 56, Issue 2, February 2026.
Phagocytosis of yeast activates recruitment of proteases and trafficking factors from the secretory and endosomal pathways to the IRAP compartment and subsequently phagosomes, promoting cross‐presentation. In the absence of Sec22b, IRAP endosome and phagosome maturation to late endosomes is accelerated.
Alice Senni, Louise Grumbach, Sara Ceccacci, Mathieu Frechin, Nicolas Goudin, Ida Chiara Guerrera, Barbara Bertocci, Peter van Endert   +7 more
wiley   +1 more source

Thiol Isomerases: Enzymatic Mechanisms, Models of Oxidation, and Antagonism by Galloylated Polyphenols

Antioxidants
Thiol isomerases are a family of enzymes that participate in oxidative protein folding. They contain highly reactive vicinal thiols in a CXXC motif within their catalytic domains to mediate thiol-disulfide switching as part of their reductase, oxidase ...
Osamede C. Owegie, Quinn P. Kennedy, Pavel Davizon-Castillo, Moua Yang   +3 more
doaj   +1 more source

A Protein Disulfide Isomerase Plays a Role in Programmed Cell Death [PDF]

, 2008
Kathleen L. Farquharson
openalex   +1 more source

nDsbD: a redox interaction hub in the Escherichia coli periplasm [PDF]

, 2018
.: DsbD is a redox-active protein of the inner Escherichia coli membrane possessing an N-terminal (nDsbD) and a C-terminal (cDsbD) periplasmic domain. nDsbD interacts with four different redox proteins involved in the periplasmic disulfide isomerization ...
Capitani, G., Glockshuber, R., Grütter, M., Stirnimann, C.   +3 more
core  

Oxidative Stress: Molecular Mechanisms, Diseases, and Therapeutic Targets

MedComm, Volume 7, Issue 2, February 2026.
Oxidative stress occurs when the reactive oxygen species (ROS) production overwhelms the ROS scavenging, which lead to genomic instability, epigenetic regulation, proteostasis imbalance, and lipid peroxidation, subsequently causing the occurrence and development of numerous diseases. ABSTRACT Although the physiological level of reactive oxygen species (
Yi Qin, Chen Qian, Wenhao Li, Qihan Wang, Qifeng Sheng, Zheqing Chen, Wei Zhang, Wenming Li, Gaoran Ge, Zhanjun Yan, Dechun Geng   +10 more
wiley   +1 more source

Manipulation of the Unfolded Protein Response by Intracellular Bacterial Pathogens: Mechanisms of ER Hijacking and Therapeutic Implications

The FASEB Journal, Volume 40, Issue 2, 31 January 2026.
This review illustrates how intracellular bacterial pathogens—such as Brucella, Mycobacterium tuberculosis, and Legionella—secrete effector proteins that specifically target the IRE1α, PERK, and ATF6 branches of the unfolded protein response (UPR) to hijack ER stress signaling.
Enhui Dai, Dongjie Sun, Yanxiao Zhao, Mengtao Zhang, Yifan Wu, Jiabo Ding   +5 more
wiley   +1 more source

The Potato Sucrose Transporter StSUT1 Interacts with a DRM-Associated Protein Disulfide Isomerase [PDF]

, 2011
Undine Krügel, Hongxia He, Konstanze Gier, Jana Reins, Izabela Chincinska, Bernhard Grimm, Waltraud X. Schulze, Christina Kühn   +7 more
openalex   +1 more source