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	1.	Glutaredoxin accelerates glutathione-dependent folding of reduced ribonuclease A together with protein disulfide-isomerase. [electronic resource] by Lundström-Ljung, J Holmgren, A Producer: 19950515 In: The Journal of biological chemistry vol. 270 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	2.	Insulin-like growth factors I and II are unable to form and maintain their native disulfides under in vivo redox conditions. [electronic resource] by Hober, S Lundström Ljung, J Uhlén, M Nilsson, B Producer: 19990311 In: FEBS letters vol. 443 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	3.	Reactivity of glutaredoxins 1, 2 and 3 from Escherichia coli and protein disulfide isomerase towards glutathionyl-mixed disulfides in ribonuclease A. [electronic resource] by Lundström-Ljung, J Vlamis-Gardikas, A Aslund, F Holmgren, A Producer: 19990302 In: FEBS letters vol. 443 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	4.	Effect of glutaredoxin and protein disulfide isomerase on the glutathione-dependent folding of ribonuclease A. [electronic resource] by Ruoppolo, M Lundström-Ljung, J Talamo, F Pucci, P Marino, G Producer: 19971023 In: Biochemistry vol. 36 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	5.	Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue. [electronic resource] by Zhong, L Arnér, E S Ljung, J Aslund, F Holmgren, A Producer: 19980514 In: The Journal of biological chemistry vol. 273 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	6.	Combinations of protein-disulfide isomerase domains show that there is little correlation between isomerase activity and wild-type growth. [electronic resource] by Xiao, R Solovyov, A Gilbert, H F Holmgren, A Lundström-Ljung, J Producer: 20010823 In: The Journal of biological chemistry vol. 276 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	7.	Two resident ER-proteins, CaBP1 and CaBP2, with thioredoxin domains, are substrates for thioredoxin reductase: comparison with protein disulfide isomerase. [electronic resource] by Lundström-Ljung, J Birnbach, U Rupp, K Söling, H D Holmgren, A Producer: 19950224 In: FEBS letters vol. 357 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	8.	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. [electronic resource] by Koivunen, P Pirneskoski, A Karvonen, P Ljung, J Helaakoski, T Notbohm, H Kivirikko, K I Producer: 19990218 In: The EMBO journal vol. 18 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	9.	Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms. [electronic resource] by Lundberg, M Johansson, C Chandra, J Enoksson, M Jacobsson, G Ljung, J Johansson, M Holmgren, A Producer: 20010816 In: The Journal of biological chemistry vol. 276 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)
	10.	Characterization of Sptrx, a novel member of the thioredoxin family specifically expressed in human spermatozoa. [electronic resource] by Miranda-Vizuete, A Ljung, J Damdimopoulos, A E Gustafsson, J A Oko, R Pelto-Huikko, M Spyrou, G Producer: 20010920 In: The Journal of biological chemistry vol. 276 Online resources: Available from publisher's website Availability: No items available. Save to lists Add to cart (remove)