Search Results - "Ljung, Johanna"

Cloning and Expression of a Novel Human Glutaredoxin (Grx2) with Mitochondrial and Nuclear Isoforms by Lundberg, Mathias, Johansson, Catrine, Chandra, Joya, Enoksson, Mari, Jacobsson, Gunilla, Ljung, Johanna, Johansson, Magnus, Holmgren, Arne

“…Glutaredoxin (Grx) is a glutathione-dependent hydrogen donor for ribonucleotide reductase. Today glutaredoxins are known as a multifunctional family of…”
Get full text

The Contributions of Protein Disulfide Isomerase and Its Homologues to Oxidative Protein Folding in the Yeast Endoplasmic Reticulum by Xiao, Ruoyu, Wilkinson, Bonney, Solovyov, Anton, Winther, Jakob R., Holmgren, Arne, Lundström-Ljung, Johanna, Gilbert, Hiram F.

“…In vitro, protein disulfide isomerase (Pdi1p) introduces disulfides into proteins (oxidase activity) and provides quality control by catalyzing the…”
Get full text

Catalysis of thiol/disulfide exchange. Glutaredoxin 1 and protein-disulfide isomerase use different mechanisms to enhance oxidase and reductase activities by Xiao, Ruoyu, Lundström-Ljung, Johanna, Holmgren, Arne, Gilbert, Hiram F

“…Glutaredoxin (Grx) and protein-disulfide isomerase (PDI) are members of the thioredoxin superfamily of thiol/disulfide exchange catalysts. Thermodynamically,…”
Get full text

Characterization of Sptrx, a Novel Member of the Thioredoxin Family Specifically Expressed in Human Spermatozoa by Miranda-Vizuete, A, Ljung, J, Damdimopoulos, A E, Gustafsson, J A, Oko, R, Pelto-Huikko, M, Spyrou, G

“…Thioredoxins (Trx) are small ubiquitous proteins that participate in different cellular processes via redox-mediated reactions. We report here the…”
Get full text

Rat and Calf Thioredoxin Reductase Are Homologous to Glutathione Reductase with a Carboxyl-terminal Elongation Containing a Conserved Catalytically Active Penultimate Selenocysteine Residue by Zhong, Liangwei, Arnér, Elias S.J., Ljung, Johanna, Åslund, Fredrik, Holmgren, Arne

“…We have determined the sequence of 23 peptides from bovine thioredoxin reductase covering 364 amino acid residues. The result was used to identify a rat cDNA…”
Get full text

Catalysis of Thiol/Disulfide Exchange by Xiao, Ruoyu, Lundström-Ljung, Johanna, Holmgren, Arne, Gilbert, Hiram F.

“…Glutaredoxin (Grx) and protein-disulfide isomerase (PDI) are members of the thioredoxin superfamily of thiol/disulfide exchange catalysts. Thermodynamically,…”
Get full text

Combinations of Protein-disulfide Isomerase Domains Show That There Is Little Correlation between Isomerase Activity and Wild-type Growth by Xiao, R, Solovyov, A, Gilbert, H F, Holmgren, A, Lundström-Ljung, J

“…Protein-disulfide isomerase (PDI) has five domains: a, b, b′, a′ and c, all of which except c have a thioredoxin fold. A single catalytic domain (a or…”
Get full text

Glutaredoxin Accelerates Glutathione-dependent Folding of Reduced Ribonuclease A Together with Protein Disulfide-isomerase (∗) by Lundström-Ljung, Johanna, Holmgren, Arne

“…Glutaredoxin (Grx) contains a redox-active disulfide and catalyzes thiol-disulfide interchange reactions with specificity for GSH. The dithiol form of Grx…”
Get full text

The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide by Koivunen, Peppi, Pirneskoski, Annamari, Karvonen, Päivi, Ljung, Johanna, Helaakoski, Tarja, Notbohm, Holger, Kivirikko, Kari I.

“…Protein disulfide isomerase (PDI) is a multifunctional polypeptide that acts as a subunit in the animal prolyl 4‐hydroxylases and the microsomal triglyceride…”
Get full text

Effect of Glutaredoxin and Protein Disulfide Isomerase on the Glutathione-Dependent Folding of Ribonuclease A by Ruoppolo, Margherita, Lundström-Ljung, Johanna, Talamo, Fabio, Pucci, Piero, Marino, Gennaro

“…Protein folding, associated with oxidation and isomerization of disulfide bonds, was studied using reduced and denatured RNase A (rd-RNase A) and mixed…”
Get full text

Human spermatid-specific thioredoxin-1 (Sptrx-1) is a two-domain protein with oxidizing activity by Jiménez, Alberto, Johansson, Catrine, Ljung, Johanna, Sagemark, Johan, Berndt, Kurt D, Ren, Bin, Tibbelin, Gudrun, Ladenstein, Rudolf, Kieselbach, Thomas, Holmgren, Arne, Gustafsson, Jan-Åke, Miranda-Vizuete, Antonio

“…Spermatid-specific thioredoxin-1 (Sptrx-1) is the first member of the thioredoxin family of proteins with a tissue-specific expression pattern, found…”
Get full text

Mutations in domain a′ of protein disulfide isomerase affect the folding pathway of bovine pancreatic ribonuclease A by Ruoppolo, Margherita, Orrù, Stefania, Talamo, Fabio, Ljung, Johanna, Pirneskoski, Annamari, Kivirikko, Kari I., Marino, Gennaro, Koivunen, Peppi

“…Protein disulfide isomerase (PDI, EC 5.3.4.1), an enzyme and chaperone, catalyses disulfide bond formation and rearrangements in protein folding. It is also a…”
Get full text

Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions by Hober, Sophia, Lundström Ljung, Johanna, Uhlén, Mathias, Nilsson, Björn

“…Insulin-like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM oxidized glutathione…”
Get full text

Reactivity of glutaredoxins 1, 2 and 3 from Escherichia coli and protein disulfide isomerase towards glutathionyl-mixed disulfides in ribonuclease A by Lundström-Ljung, Johanna, Vlamis-Gardikas, Alexios, Åslund, Fredrik, Holmgren, Arne

“…We have examined the activity of protein disulfide isomerase (PDI) and glutaredoxin (Grx) 1, 2 and 3 from Escherichia coli to catalyze the cleavage of…”
Get full text

Insulin‐like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions 1 by Hober, Sophia, Lundström Ljung, Johanna, Uhlén, Mathias, Nilsson, Björn

“…Insulin‐like growth factor (IGF) I does not quantitatively form its three native disulfide bonds in the presence of 10 mM reduced and 1 mM oxidized glutathione…”
Get full text

Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase by Lundström-Ljung, Johanna, Birnbach, Ulrike, Rupp, Katrin, Söling, Hans-Dieter, Holmgren, Arne

“…Protein disulfide-isomerase (PDI) is the best known representative of a growing family of enzymes with thioredoxin domains. Two such proteins with thioredoxin…”
Get full text