Results 141 to 150 of about 3,189 (173)
Some of the next articles are maybe not open access.
Redox properties and evolution of human glutaredoxins
Proteins: Structure, Function, and Bioinformatics, 2007AbstractGlutaredoxins (Grxs) are glutathione‐dependent oxidoreductases that belong to the thioredoxin superfamily catalyzing thiol‐disulfide exchange reactions via active site cysteine residues. Focusing on the human dithiol glutaredoxins having a C‐X‐Y‐C active site sequence motif, the redox potentials of hGrx1 and hGrx2 were determined to be −232 and
Johan, Sagemark +5 more
openaire +2 more sources
Evolution and diversity of glutaredoxins in photosynthetic organisms
Cellular and Molecular Life Sciences, 2009The genome sequencing of prokaryotic and eukaryotic photosynthetic organisms enables a comparative genomic study of the glutaredoxin (Grx) family. The analysis of 58 genomes, using a specific motif composed of the active site sequence and of amino acids involved in glutathione binding, led to an updated classification of Grxs into six classes. Only two
Couturier, Jérémy +2 more
openaire +3 more sources
Immunolocalization of thioredoxin and glutaredoxin in mammalian hypophysis
Molecular and Cellular Endocrinology, 1992Thioredoxin (TRX) and glutaredoxin (GRX) are two small proteins catalyzing thiol-disulfide oxidoreductions. A role of both proteins in secretory processes has been suggested and recently it has been demonstrated that thioredoxin functions as a growth factor for lymphocytes in cell cultures.
C A, Padilla +4 more
openaire +2 more sources
A revised sequence of calf thymus glutaredoxin
Biochemical and Biophysical Research Communications, 1989The previously published structure of the glutaredoxin from calf thymus [Klintrot et al., (1984) Eur. J. Biochem. 144, 417-423] was reinvestigated by tandem mass spectrometry and found to have an N-terminal Ac-Ala-Gln-Ala-... sequence and an additional four amino acids inserted between positions 67 and 68.
I A, Papayannopoulos +3 more
openaire +2 more sources
Characterization of the Redox Properties of Poplar Glutaredoxin
Antioxidants & Redox Signaling, 2003The presence of glutaredoxins in plants is now well recognized, but their functions and natural substrates remain largely unknown. Recently, a poplar glutaredoxin has been biochemically characterized and several mutants have been engineered in order to explore its reactivity. This work focuses on some physiological functions of the enzyme. According to
Rouhier, Nicolas +6 more
openaire +4 more sources
Antioxidant Function of Thioredoxin and Glutaredoxin Systems
Antioxidants & Redox Signaling, 2000Selenium is an essential trace element with known antioxidant properties. Cytosolic thioredoxin reductase from mammalian cells is a dimeric flavin enzyme comprising a glutathione reductase-like equivalent elongated with 16 residues including the conserved carboxy-terminal sequence, Gly-Cys-SeCys-Gly, where SeCys is selenocysteine.
openaire +2 more sources
The Glutaredoxin Family in Oxygenic Photosynthetic Organisms
Photosynthesis Research, 2004Glutaredoxins (GRXs) are small redox proteins of the thioredoxin (TRX) superfamily. Compared to TRXs, much less information on the GRX family is available, especially in photosynthetic organisms since GRXs have been mainly studied in E. coli, yeast and mammal cells.
openaire +2 more sources
Glutaredoxins with iron-sulphur clusters in eukaryotes - Structure, function and impact on disease
Biochimica Et Biophysica Acta - Bioenergetics, 2021Carsten Berndt +2 more
exaly
Thioredoxin and Glutaredoxin Isoforms
2002Alexios, Vlamis-Gardikas, Arne, Holmgren
openaire +2 more sources