Results 11 to 20 of about 11,635 (216)

Distinct Shift in Beta-Cell Glutaredoxin 5 Expression Is Mediated by Hypoxia and Lipotoxicity Both In Vivo and In Vitro

Frontiers in Endocrinology, 2018
Histomorphological and functional alterations in pancreatic islet composition directly correlate with hyperglycemia severity. Progressive deterioration of metabolic control in subjects suffering from type 2 diabetes is predominantly caused by impaired ...
Sebastian Friedrich Petry, Lia Mingzhe Sun, Anna Knapp, Sabrina Reinl, Thomas Linn   +4 more
doaj   +2 more sources

The structure of a reduced mutant T4 glutaredoxin [PDF]

FEBS Letters, 1995
The mutant T4 glutaredoxin where the active site residues Val15 and Tyr16 have been substituted by Gly and Pro, respectively, crystallizes in a form where the active site disulfide is accessible to reagents. Treatment of the crystals with dithiotreitol causes very subtle changes in the overall glutaredoxin structure.
Ingelman, Margareta, Nordlund, Pär, Eklund, Hans   +2 more
openaire   +3 more sources

Utility of Synechocystis sp. PCC glutaredoxin A as a platform to study high-resolution mutagenesis of proteins.

Frontiers in Plant Science, 2013
Glutaredoxin from the cyanobacterium Synechocystis sp. PCC 6803 is a small protein, containing only 88 amino acids, that participates in a large number of redox reactions, serving both as an electron donor for enzyme-catalyzed reductions and as a ...
David B Knaff, Roger Bryan Sutton
doaj   +2 more sources

Cloning, Overexpression, and Characterization of Glutaredoxin 2, An Atypical Glutaredoxin from Escherichia coli [PDF]

Journal of Biological Chemistry, 1997
Glutaredoxin 2 (Grx2) from Escherichia coli catalyzes GSH-disulfide oxidoreductions via two redox-active cysteine residues, but in contrast to glutaredoxin 1 (Grx1) and glutaredoxin 3 (Grx3), is not a hydrogen donor for ribonucleotide reductase. To characterize Grx2, a chromosomal fragment containing the E.
A, Vlamis-Gardikas, F, Aslund, G, Spyrou, T, Bergman, A, Holmgren   +4 more
openaire   +3 more sources

Prediction of thioredoxin and glutaredoxin target proteins by identifying reversibly oxidized cysteinyl residues

Journal of Integrative Bioinformatics, 2010
A significant part of cellular proteins undergo reversible thiol-dependent redox transitions which often control or switch protein functions. Thioredoxins and glutaredoxins constitute two key players in this redox regulatory protein network.
Lee Hang-mao, Dietz Karl Josef, Hofestädt Ralf   +2 more
doaj   +2 more sources

Deletion of glutaredoxin promotes oxidative tolerance and intracellular infection in Listeria monocytogenes [PDF]

Virulence, 2019
Thiol-disulfide glutaredoxin systems of bacterial cytoplasm favor reducing conditions for the correct disulfide bonding of functional proteins, and therefore were employed by bacteria to defend against oxidative stress.
Jing Sun, Yi Hang, Yue Han, Xian Zhang, Li Gan, Chang Cai, Zhongwei Chen, Yang Yang, Quanjiang Song, Chunyan Shao, Yongchun Yang, Yingshan Zhou, Xiaodu Wang, Changyong Cheng, Houhui Song   +14 more
doaj   +2 more sources

Redox signals and oxidative stress in the control of mitochondrial protein import. [PDF]

Protein Sci
Abstract Mitochondrial protein import is essential for organelle biogenesis and cellular homeostasis. It operates in an environment that is intrinsically shaped by redox chemistry. Mitochondria are major sources of reactive oxygen species (ROS), which arise as by‐products of oxidative phosphorylation. Cells therefore maintain sophisticated ROS‐handling
Hasberg L, Lauterbach VK, Ochsenreiter T, Riemer J.   +3 more
europepmc   +2 more sources

Glutaredoxins in fungi [PDF]

Photosynthesis Research, 2006
Glutaredoxins (GRXs) can be subdivided into two subfamilies: dithiol GRXs with the CPY/FC active site motif, and monothiol GRXs with the CGFS motif. Both subfamilies share a thioredoxin-fold structure. Some monothiol GRXs exist with a single-Grx domain while others have a thioredoxin-like domain (Trx) and one or more Grx domains in tandem.
Herrero Perpiñán, Enrique, Ros Salvador, Joaquim, Tamarit Sumalla, Jordi, Bellí i Martínez, Gemma   +3 more
openaire   +3 more sources

Nuclear Monothiol Glutaredoxins of Saccharomyces cerevisiae Can Function as Mitochondrial Glutaredoxins [PDF]

Journal of Biological Chemistry, 2004
Glutaredoxins are thiol oxidoreductases that regulate protein redox state. In Saccharomyces cerevisiae, Grx1 and Grx2 are cytosolic dithiol glutaredoxins, whereas Grx3, Grx4, and Grx5 are monothiol glutaredoxins. Grx5 locates at the mitochondrial matrix and is needed for iron/sulfur cluster biogenesis. Its absence causes phenotypes such as inactivation
Molina Navarro, Maria Micaela, Bellí i Martínez, Gemma, Torre Ruiz, M. A. de la, Rodríguez Manzanaque, Maria Teresa, Herrero Perpiñán, Enrique   +4 more
openaire   +3 more sources

Tyr76 is essential for the cold adaptation of a class II glutaredoxin 4 with a heat‐labile structure from the Arctic bacterium Sphingomonas sp.

FEBS Open Bio, 2023
Glutaredoxins (Grxs) are small proteins that share a well‐conserved thioredoxin (Trx)‐fold and participate in many biological processes. This study examined the cold adaptation mechanism of a Fe‐S cluster binding class II Grx4 (SpGrx4) from the ...
Trang Hoang, ChanSu Jeong, Sei‐Heon Jang, ChangWoo Lee   +3 more
doaj   +1 more source