Results 61 to 70 of about 97,846 (317)

Mitochondrial Thioredoxin System as a Modulator of Cyclophilin D Redox State [PDF]

, 2016
The mitochondrial thioredoxin system (NADPH, thioredoxin reductase, thioredoxin) is a major redox regulator. Here we have investigated the redox correlation between this system and the mitochondrial enzyme cyclophilin D.
Bindoli, Alberto, Cali', Tito, Citta, Anna, Folda, Alessandra, Rigobello, MARIA PIA, Scalcon, Valeria, Scutari, Guido, Zonta, Francesco   +7 more
core   +1 more source

A functionalized hydroxydopamine quinone links thiol modification to neuronal cell death

Redox Biology, 2020
Recent findings suggest that dopamine oxidation contributes to the development of Parkinson's disease (PD); however, the mechanistic details remain elusive.
Ali Farzam, Karan Chohan, Miroslava Strmiskova, Sarah J. Hewitt, David S. Park, John P. Pezacki, Dennis Özcelik   +6 more
doaj   +1 more source

Conjugate of Thiol and Guanidyl Units with Oligoethylene Glycol Linkage for Manipulation of Oxidative Protein Folding

Molecules, 2021
Oxidative protein folding is a biological process to obtain a native conformation of a protein through disulfide-bond formation between cysteine residues.
Shunsuke Okada, Motonori Matsusaki, Masaki Okumura, Takahiro Muraoka   +3 more
doaj   +1 more source

Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC-53 and ERp44. [PDF]

, 2008
Sulfatase modifying factor 1 (SUMF1) encodes for the formylglicine generating enzyme, which activates sulfatases by modifying a key cysteine residue within their catalytic domains. SUMF1 is mutated in patients affected by multiple sulfatase deficiency, a
Annunziata F., BALLABIO, ANDREA, Cosma M. P., Cozzolino M., FRALDI, ALESSANDRO, Lombardi A., MONTI, MARIA, PUCCI, PIETRO, Sitia R., Spampanato C., Zito E.   +10 more
core   +1 more source

Biosynthesis and enzymology of the Caenorhabditis elegans cuticle: identification and characterization of a novel serine protease inhibitor. [PDF]

, 2006
The nematode Caenorhabditis elegans represents an excellent model in which to examine nematode gene expression and function. A completed genome, straightforward transgenesis, available mutants and practical genome-wide RNAi approaches provide an ...
Andrew J. Birnie, Antony P. Page, Brenner, Brooks, Canty, Chu, Davis, Edens, Eschenlauer, Frand, Friedman, Gillian McCormack, Hawdon, Hill, Johnstone, Kamath, Kamath, Kramerova, Kramerova, Kress, Lustigman, Milstone, Myllyharju, Myllyharju, Novelli, Page, Page, Page, Page, Page, Pappano, Peters, Poole, Roberts, Sapio, Simmer, Singh, Sulston, Thacker, Thacker, Thein, Winter, Yang   +42 more
core   +1 more source

Lung epithelial protein disulfide isomerase A3 (PDIA3) plays an important role in influenza infection, inflammation, and airway mechanics

Redox Biology, 2019
Protein disulfide isomerases (PDI) are a family of redox chaperones that catalyze formation or isomerization of disulfide bonds in proteins. Previous studies have shown that one member, PDIA3, interacts with influenza A virus (IAV) hemagglutinin (HA ...
Nicolas Chamberlain, B. Korwin-Mihavics, E. Nakada, S. Bruno, D. Heppner, D. Chapman, S. Hoffman, A. van der Vliet, B. Suratt, O. Dienz, J. Alcorn, V. Anathy   +11 more
semanticscholar   +1 more source

Oxidative Protein-Folding Systems in Plant Cells

International Journal of Cell Biology, 2013
Plants are unique among eukaryotes in having evolved organelles: the protein storage vacuole, protein body, and chloroplast. Disulfide transfer pathways that function in the endoplasmic reticulum (ER) and chloroplasts of plants play critical roles in the
Yayoi Onda
doaj   +1 more source

The role and mechanism of TXNDC5 in diseases

European Journal of Medical Research, 2022
Thioredoxin domain-containing protein 5 (TXNDC5) is a member of the protein disulfide isomerase (PDI) family. It can promote the formation and rearrangement of disulfide bonds, ensuring proper protein folding. TXNDC5 has three Trx-like domains, which can
Xueling Wang, Haoran Li, Xiaotian Chang
doaj   +1 more source

The MIA pathway: a key regulator of mitochondrial oxidative protein folding and biogenesis [PDF]

, 2015
Mitochondria are fundamental intracellular organelles with key roles in important cellular processes like energy production, Fe/S cluster biogenesis, and homeostasis of lipids and inorganic ions.
Mordas, Amelia, Tokatlidis, Konstantinos
core   +2 more sources

The transmembrane protein disulfide isomerase TMX1 negatively regulates platelet responses.

Blood, 2019
Secreted platelet protein disulfide isomerases, PDI, ERp57, ERp5, and ERp72, have important roles as positive regulators of platelet function and thrombosis.
Zhenzhen Zhao, Yi Wu, Junsong Zhou, Fengwu Chen, Aizhen Yang, D. Essex   +5 more
semanticscholar   +1 more source