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	2011   Godoy, J.R., Oesteritz, S., Hanschmann, E.M., Ockenga, W., Ackermann, W., and Lillig, C.H. Segment-specific overexpression of redoxins after renal ischemia and reperfusion: protective roles of glutaredoxin 2, peroxiredoxin 3, and peroxiredoxin 6 Free Radic. Biol. Med. 51: 552-561 (2011)   Hoffmann, B., Uzarska, M.A., Berndt, C., Godoy, J.R., Haunhorst, P., Lill, R., Lillig, C.H., and Mühlenhoff, U. The Multi-domain Thioredoxin-Monothiol Glutaredoxins Represent a Distinct Functional Group Antioxid. Redox Signal. 15: 19-30 (2011) [medline] [journal/ARS ]   Godoy, J.R.*, Funke, M.*, Ackermann, W., Haunhorst, P., Oesteritz, S., Capani, F., Elsässer, H.P., Lillig, C.H. Redox atlas of the mouse: Immunohistochemical detection of glutaredoxin-, peroxiredoxin-, and thioredoxin-family proteins in various tissues of the laboratory mouse. Biochim. Biophys. Acta - Gen. Sub. 1810: 2-92 (2011) [medline] [journal/BBA] [project webpage]   Aon-Bertolino, M.L., Ignacio Romero, J., Galeano, P., Holubiec, M., Badorrey, M.S., Saraceno, G.E., Hanschmann, E.M., Lillig, C.H., and Capani, F. Thioredoxin and glutaredoxin system proteins - immunolocalization in the rat central nervous system Biochim. Biophys. Acta - Gen. Sub. 1810: 93-110 (2011) [pdf] [medline] [journal/BBA]   2010   Hanschmann, E.M., Lönn, M.E., Schütte, L.D., Funke, M., Godoy, J.R., Eitner, S., Hudemann, C., and Lillig, C.H. Both thioredoxin 2 and glutaredoxin 2 contribute to the reduction of the mitochondrial 2-CYS peroxiredoxin PRX3 J. Biol. Chem. 285: 40699-40705 (2010) [pdf] [medline] [journal/JBC]   Mühlenhoff, U., Molik, S., Godoy, J.R., Uzarska, M.A., Richter, N., Seubert, A., Zhang, Y., Stubbe, J., Pierrel, F., Herrero, E., Lillig, C.H., and Lill, R. Cytosolic monothiol glutaredoxins function in intracellular iron sensing and trafficking via their bound iron-sulfur cluster. Cell Metab. 12: 373-85 (2010) [pdf] [medline] [journal/CM]   Haunhorst, P., Berndt, C., Eitner, S., Godoy, J.R. and Lillig, C.H. Characterization of human monothiol glutaredoxin 3 (PICOT) as iron-sulfur protein. Biochem. Biophys. Res. Commun. 394: 372-376 (2010) [pdf] [medline] [journal/BBRC]   2009   Lillig, C.H. and Lill, R. Lights on iron sulfur clusters. Chem. Biol. 16: 1213 (2009)[pdf] [medline] [journal/CB]   Lillig, C.H., and Arner, E. Special issue on selenoprotein expression and function. Biochim. Biophys. Acta - Gen. Sub. 1790: 1387-1388 (2009) [pdf] [medline] [journal/BBA]   Lillig, C.H. and Berndt, C. Thioredoxins and Glutaredoxins. Functions and Metal Ion Interactions. in "Metallothioneins and Related Chelators" , Vol. 5 of 'Metal Ions in Life Sciences'; A. Sigel, H. Sigel, R. K. and O. Sigel, Eds.; The Royal Society of Chemistry, Cambridge, UK, ISBN: 978-1-84755-899-2 (2009) [publisher/RSC]   Hudemann, C.*, Lönn, M.E.*, Godoy, J.R., Zahedi Avval, F., Capani, F., Holmgren, A., and Lillig, C.H., Identification, expression pattern and characterization of mouse glutaredoxin 2 isoforms. Antioxid. Redox Signal. 11: 1-14 (2009) [pdf] [medline] [journal/ARS]   2008   Lillig, C.H., and Berndt, C. Preface to the special issue on redox control of cell function. Biochim. Biophys. Acta - Gen. Sub. 1780: 1169 (2008) [pdf] [journal/BBA] [the whole special issue /ScienceDirect]   Lillig, C.H., Berndt, C., and Holmgren, A. Glutaredoxin systems. Biochim. Biophys. Acta - Gen. Sub. 1780: 1304-1317 (2008) [pdf] [medline] [journal/BBA]   Izquierdo, A., Casas, C., Mühlenhoff, U., Lillig, C.H., and Herrero, E. Yeast Grx6 and Grx7 are monothiol glutaredoxins associated with the early secretory pathway. Eukaryot. Cell 7: 1415-1426 (2008) [pdf] [medline] [journal/EC]   Berndt, C., Lillig, C.H., and Holmgren, A.Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim. Biophys. Acta - Mol. Cell Res. 1783: 641-650 (2008) [pdf] [medline] [journal/BBA]   Hudemann, C., Berndt, C., and Lillig, C.H., Glutaredoxine und Eisen-Schwefel Zentren. Biospektrum 14: 32-35 (2008) [pdf in German]   Lönn, M.E.*, Hudemann, C.*, Berndt, C., Cherkasov, V., Capani, F., Holmgren, A., and Lillig, C.H., Expression pattern of human glutaredoxin 2 isoforms: Identification and characterization of two testis/cancer cell-specific isoforms. Antioxid. Redox Signal. 10: 547-558 (2008) [pdf] [medline] [journal/ARS]   2007   Hashemy, S.I., Johansson, C., Berndt, C., Lillig, C.H., and Holmgren, A., Oxidation and S-nitrosylation of cysteines in human cytosolic and mitochondrial glutaredoxins: Effects on structure and activity. J. Biol. Chem. 282:14428-14436 (2007) [pdf] [medline] [journal/JBC]   Porat, A. Lillig, C.H., Johansson, C., Fernandes, A.P., Nilsson, L., Holmgren, A., and Beckwith, J. The reducing activity of glutaredoxin 3 towards cytoplasmic substrate proteins is restricted by methionine 43. Biochemistry 46: 3366-3377 (2007) [pdf] [medline] [journal/Biochemistry]   Berndt, C., Lillig, C.H., and Holmgren, A. Thiol-based mechanisms of the thioredoxin and glutaredoxin systems: implications for diseases in the cardiovascular system. Am. J. Physiol. Heart Circ. Physiol. 292: H1227-1236 (2007) [pdf] [medline] [journal/AJPHCP]   Berndt, C., Hudemann, C., Hanschmann, E.M., Axelsson, R., Holmgren, A., and Lillig, C.H. How does iron-sulfur cluster coordination regulate the activity of human glutaredoxin 2? Antioxid. Redox Signal. 9: 151-157 (2007) [pdf] [medline] [journal/ARS]   Lillig, C.H., and Holmgren, A., Thioredoxin and related molecules - from biology to health and disease. Antioxid. Redox Signal. 9: 25-47 (2007) [pdf] [medline] [journal/ARS]   2005   Holmgren, A., Johansson, C., Berndt, C., Lönn, M.E., Hudemann, C., and Lillig, C.H., Thiol redox control via thioredoxin and glutaredoxin systems. Biochem. Soc. Trans. 33: 1375-1377 (2005) [pdf] [medline] [journal/BST]   Lillig, C.H., Berndt, C., Vergnolle, O., Lönn, M.E., Hudemann, C., Bill, E., and Holmgren, A., Characterization of human glutaredoxin 2 as new iron-sulfur protein: a possible role as redox sensor. Proc. Natl. Acad. Sci. U.S.A. 102: 8168-8173 (2005) [pdf] [medline] [journal/PNAS]   Fernandes, A.P., Fladvad, M., Berndt, C., Andresen, C., Lillig, C.H., Neubauer, P., Sunnerhagen, M., Holmgren, A., and Vlamis-Gardikas, A., A novel monothiol glutaredoxin (GRX4) from Escherichia coli can serve as a substrate for thioredoxin reductase. J. Biol. Chem. 280: 24544-24552 (2005) [pdf] [medline] [journal/JBC]   Wang, W., Oliva, C., Li, G., Holmgren, A., Lillig, C.H., and Kirk, K.L., Reversible silencing of CFTR chloride channels by glutathionylation. J. Gen. Physiol. 125: 127-141 (2005) [pdf] [medline] [journal/JGP]   Enoksson, M., Potamitou Fernandes, A., Prast, S., Lillig, C.H., Holmgren, A., and Orrenius, S., Overexpression of glutaredoxin 2 attenuates apoptosis by preventing cytochrome c release. Biochem. Biophys. Res. Comm. 327: 774-779 (2005) [pdf] [medline] [journal/BBRC]   2004   Lillig, C.H., Lönn, M.E., Enoksson, M., Potamitou Fernandes, A., and Holmgren, A., siRNA-mediated silencing of glutaredoxin 2 increases the sensitivity of HeLA cells towards doxorubicin and phenylarsine oxide. Proc. Natl. Acad. Sci. U.S.A. 101: 13227-13232 (2004) [pdf] [medline] [journal/PNAS]   Berndt, C., Lillig, C.H., Wollenberg, M., Bill, E., Mansilla, M.C., de Mendoza, D., Seidler, A., and, Schwenn, J.D, Characterization and reconstitution of a 4Fe4S adenylyl sulfate (APS) / phospho-adenylyl sulfate (PAPS) reductase from Bacillus subtilis. J. Biol. Chem. 279: 7850-7855 (2004) [pdf] [medline] [journal/JBC]   Johansson, C., Lillig, C.H., and Holmgren, A., Human mitochondrial glutaredoxin reduces S-glutathionylated proteins with high affinity accepting electrons from either glutathione or thioredoxin reductase. J. Biol. Chem. 279: 7537-7543 (2004) [pdf] [medline] [journal/JBC]   2003   Lillig, C.H., Potamitou, A., Schwenn, J.D., Vlamis-Gardikas, A., and Holmgren, A., Redox regulation of 3' phospoadenylylsulfate reductase from Escherichia coli by glutathione and glutaredoxins. J. Biol. Chem. 278: 22325-22330 (2003) [pdf] medline] [journal/JBC]   Rouhier, N., Vlamis-Gardikas, A., Lillig, C.H., Berndt, C., Schwenn, J.D., Holmgren, A., and Jacquot, J.-P., Further characterization of the redox properties of poplar glutaredoxin. Antioxid. Redox Signal. 5: 15-22 (2003) [pdf] [medline] [journal/ARS]   2001   Lillig, C.H., Schiffmann, S., Berndt, C., Berken, A., Tischka, R., and Schwenn, J.D., Molecular and catalytic properties of Arabidopsis thaliana adenylylsulfate-(APS)-kinase. Arch. Biochem. Biophys. 392: 303-310 (2001) [pdf] [medline] [journal/ABB]   1999   Prior, A., Uhrig, J.F., Heins, L., Wiesmann, A., Lillig, C.H., Stoltze, C., Soll, J., and Schwenn, J.D., Structural and kinetic properties of adenylyl sulfate reductase from Catharanthus roseus cell cultures. Biochim. Biophys. Acta - Prot. Struct. Mol. Enzymol. 1430: 25-38 (1999) [pdf] [medline] [journal/BBA]   Lillig, C.H., Prior, A., Schwenn, J.D., Aslund, F., Ritz, D., Vlamis-Gardikas, A., and Holmgren, A., New thioredoxins and glutaredoxins as electron donors of 3phosphoadenylylsulfate reductase. J. Biol. Chem. 274: 7695-7698 (1999) [pdf] [medline] [journal/JBC]
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