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Schmidt, A., Rödder, K., Hasse, S., Masur, K., Toups, L., Lillig, C.H., von Woedtke, T., Wende, K., and Bekeschus, S. Redox regulation of activator protein 1 family members in blood cancer cell lines exposed to cold physical plasma treated medium.Plasma Processes and Polymers. 13:1179-1188 (2016)
Valek, L., Kanngiesser, M., Häussler, A., Agarwal, N., Lillig, C.H., and Tegeder. I., Redoxins in peripheral neurons after sciatic nerve injury. Free Radic. Biol. Med. 89:581-92 (2015) [medline]
Berndt, C., Schwenn, J.D., and Lillig, C.H., The specificity and efficiency of thioredoxins and glutaredoxins is determined by electrostatic and geometric complementarity. Chem. Sci. 6:7049-7058 (2015) [journal]
Weiss, M., Gümbel, D., Hanschmann, E.M., Mandelkow, R., Gelbrich, N., Zimmermann, U., Walther, R., Ekkernkamp, A., Sckell, A., Kramer, A., Burchardt, M., Lillig, C.H., and Stope, M.B., Cold atmospheric plasma treatment induces anti-proliferative effects in prostate cancer cells by redox and apoptotic signaling pathways. Plos One 10: e0130350 (2015) [medline]
Checconi, P., Salzano, S., Bowler, L., Mullen, L., Mengozzi, M., Hanschmann, E.M., Lillig, C.H., Sgarbanti, R., Panella, S., Nencioni, L., Palamara, A.T., and Ghezzi, P., Redox proteomics of the inflammatory secretome identifies a common set of redoxins and other glutathionylated proteins released in inflammation, influenza virus infection and oxidative stress. PLoS One 10: e0127086 (2015) [medline]
Capani, F., Barreto, G., Blanco Calvo, E., and Lillig, C.H. Antioxidants in Neurodegeneration. in Antioxidants in Health and Disease, Zampelas, A , Micha, R. Eds.; pages 199-213; CRC Press, Boca Raton, USA, (2015) [publisher]
Romero, J.I., Hanschmann, E.M., Gellert, M., Eitner, S., Holubiec, M.I., Blanco-Calvo, E., Lillig, C.H., and Capani, F., Thioredoxin 1 and glutaredoxin 2 contribute to maintain the phenotype and integrity of neurons following perinatal asphyxia. Biochim. Biophys. Acta - Gen. Sub. 1850: 1274-85 (2015) [medline]
Mullen, L., Hanschmann, E.M., Lillig, C.H., Herzenberg, L., Ghezzi, P., Cysteine Oxidation Targets Peroxiredoxins 1 and 2 for Exosomal Release through a Novel Mechanism of Redox-Dependent Secretion. Mol. Med. 21: 98-108 (2015) [medline]
Otero-Losada, M., Cao, G., Gonzalez, J., Muller, A., Ottaviano, G., Lillig, C.H., Capani, F., Ambrosio, G., Milei, J., Functional and morphological changes in endocrine pancreas following cola drink consumption in rats. PLOS One 10: e0118700 (2015) [medline]
Deponte, M., and Lillig, C.H., Enzymatic control of cysteinyl thiol switches in proteins. Biol. Chem. 396: 401-13 (2015) [medline]
Gellert, M., Hanschmann, E.M., Lepka, K., Berndt, C., and Lillig, C.H. Redox regulation of cytoskeletal dynamics during differentiation and de-differentiation. Biochim. Biophys. Acta - Gen. Sub. 1850: 1575-158 (2015) [medline]
Lillig, C.H., and Berndt C. Redox regulation of differentiation and de-differentiation. Biochim. Biophys. Acta - Gen. Sub. 1850: 1467-8 (2015) [medline]
Salzano, S., Checconi, P., Hanschmann, E.M., Lillig, C.H., Bowler, L.D., Chan, P., Vaudry, D., Mengozzi, M., Coppo, L., Sacre, S., Atkuri, K.R., Sahaf, B., Herzenberg, L.A., Herzenberg, L.A., Mullen, L., Ghezzi, P. Linkage of inflammation and oxidative stress via release of glutathionylated peroxiredoxin-2, which acts as a danger signal. Proc. Natl. Acad. Sci. USA. 111: 12157-62 (2014) [medline]
Berndt, C., Lillig, C.H., Flohe , L. Redox regulation by glutathione needs enzymes. Front. Pharmacol. 5: 168 (2014) [medline]
Romero, J., Muniz, J., Tornatore, T.L., Holubiec, M., Gonzalez, J., Barreto, G.E., Guelman, L., Lillig, C.H., Blanco, E., and Capani, F. Dual role of astrocytes in perinatal asphyxia injury and neuroprotection. Neurosci. Lett. 565: 42-46 (2014) [medline]
Stope, M.B., Bradl, J., Peters, S., Streitbörger, A., Weiss, M., Zimmermann, U., Walther, R., Lillig, C.H., and Burchardt, M. Shortened Isoforms of the Androgen Receptor Are Regulated by the Cytoprotective Heat-shock Protein HSPB1 and the Tumor-suppressive MicroRNA miR-1 in Prostate Cancer Cells. Anticancer Res. 33: 4921-4926 (2013) [medline]
Romero, J., Muniz, J., Tornatore, T.L., Holubiec, M., Gonzalez, J., Barreto, G.E., Guelman, L., Lillig, C.H., Blanco, E., and Capani, F. Dual role of astrocytes in perinatal asphyxia injury and neuroprotection. Neurosci. Lett. accepted (2013) [medline]
Saleh, M., Bartual, S.G., Abdullah, M.R., Jensch, I., Asmat, T.M., Petruschka, L., Pribyl, T., Gellert, M., Lillig, C.H., Antelmann, H., Hermoso, J.A., and Hammerschmidt, S. Molecular architecture of Streptococcus pneumoniae surface thioredoxin-fold lipoproteins crucial for extracellular oxidative stress resistance and maintenance of virulence. EMBO Mol. Med. accepted (2013) [medline]
Gellert, M., Venz, S., Mitlöhner, J., Cott, C., Hanschmann, E.M., and Lillig, C.H. Identification of a dithiol-disulfide switch in collapsin response mediator protein 2 (CRMP2) that is toggled in a model of neuronal differentiation J. Biol. Chem. accepted (2013) medline]
Schütte, L.D., Baumeister, S., Weis, B., Hudemann, C., Hanschmann, E.M., and Lillig, C.H. Identification of potential protein dithiol-disulfide substrates of mammalian Grx2 Biochim. Biophys. Acta 1830:4999-5005 (2013) [medline]
Haunhorst, P., Hanschmann, E.M., Bräutigam, L., Stehling, O., Hoffmann, B., Mühlenhoff, U., Lill, R., Berndt, C., and Lillig C.H. Crucial function of vertebrate glutaredoxin 3 (PICOT) in iron homeostasis and hemoglobin maturation. Mol. Cell. Biol. 24:1895-1903 (2013) [medline]
Lillig, C.H., and Berndt C. [Special issue on] Cellular functions of glutathione. Biochim. Biophys. Acta - Gen. Sub. 1830: 3137-1338 (2013) [medline]
Hanschmann, E.M., Godoy, J.R., Berndt, C., Hudemann, C., and Lillig, C.H. Thioredoxins, glutaredoxins, and peroxiredoxins - molecular mechanisms and health significance: from cofactors to antioxidants to redox signaling. Antioxid. Redox Signal. 19: 1539-1605 (2013) [medline]
Lillig, C.H., and Berndt, C. Glutaredoxins in Thiol/Disulfide Exchange. Antioxid. Redox Signal. 18: 1654-1665 (2013) [medline]
Goette, A., Bukowska, A., Lillig, C.H., and Lendeckel, U. Oxidative stress and microcirculatory flow abnormalities in the ventricles during atrial fibrillation. Frontiers in Physiology 3: 236 (2012) [medline]
Cavicchia, J.C., Fóscolo, M., Ibañez, J.,Lillig, C.H., and Capani, F. The actin filament network associated to Sertoli cell ectoplasmic specializations. Biocell 35: 81-89 (2011) [medline]
Bräutigam L, Schütte LD, Godoy JR, Prozorovski T, Gellert M, Hauptmann G, Holmgren A, Lillig, C.H.*, and Berndt C.* Vertebrate-specific glutaredoxin is essential for brain development. Proc. Natl. Acad. Sci. USA 108: 20532-20537 (2011) [medline]
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) [medline]
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]
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]
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) [medline]
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) [medline]
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) [medline]
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) [medline]
Lillig, C.H. and Lill, R. Lights on iron sulfur clusters. Chem. Biol. 16: 1213 (2009) [medline]
Lillig, C.H., and Arner, E. Special issue on selenoprotein expression and function. Biochim. Biophys. Acta - Gen. Sub. 1790: 1387-1388 (2009) [medline]
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) [medline]
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) [medline]
Lillig, C.H., Berndt, C., and Holmgren, A. Glutaredoxin systems. Biochim. Biophys. Acta - Gen. Sub. 1780: 1304-1317 (2008) [medline]
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) [medline] 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) [medline]
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) [medline]
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) [medline]
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) [medline]
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) [medline]
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) [medline]
Lillig, C.H., and Holmgren, A., Thioredoxin and related molecules - from biology to health and disease. Antioxid. Redox Signal. 9: 25-47 (2007) [medline]
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) [medline]
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) [medline]
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) [medline]
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) [medline]
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) [medline]
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) [medline]
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) [medline]
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) [medline]
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) medline]
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) [medline]
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) [medline]
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) [medline]
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) [medline]

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