home ]

2020 ]  [ 2019 ]  [ 2018 ]  [ 2017 ]  [ 2016 ]  [ 2015 ]  [ 2014 ]  [ 2013 ]  [ 2012 ]  [ 2011 ]  [ 2010 ]  [ 2009 ]  [ 2008 ]  [ 2007 ]  [ 2005 ]  [ 2004 ]  [ 2003 ]  [ 2001 ]  [ 1999 ] 
For full text PDF's and bibliographic data, see also:
Google Scholar profile
ResearchGate.net profile

Gellert M, Hossain MF, Berens FJF, Bruhn LW, Urbainsky C, Liebscher V, Lillig CH. Substrate specificity of thioredoxins and glutaredoxins - towards a functional classification. Heliyon 5:e02943 (2020)
Nietzel T, Mostertz J, Ruberti C, Nee G, Fuchs P, Wagner S, Moseler A, Müller-Schüssele SJ, Benamar A, Poschet G, Büttner M, Möller IM, Lillig CH, Macherel D, Wirtz M, Hell R, Finkemeier I, Meyer AJ, Hochgräfe F, Schwarzländer M. Redox-mediated kick-start of mitochondrial energy metabolism drives resource-efficient seed germination. Proc Natl Acad Sci U S A 117:741-751 (2020)
Holubiec MI, Galeano P, Romero JI, Hanschmann EM, Lillig CH, Capani F. Thioredoxin 1 Plays a Protective Role in Retinas Exposed to Perinatal Hypoxia-Ischemia. Neuroscience 425:235-250 (2019)
Urbainsky C, Nölker R, Imber M, Lübken A, Mostertz J, Hochgräfe F, Godoy JR, Hanschmann EM, Lillig CH Nucleoredoxin-Dependent Targets and Processes in Neuronal Cells. Oxid Med Cell Longev 2018:4829872 (2018)
Lemmerhirt H, Behnisch S, Bodtke A, Lillig CH, Pazderova L, Kasparkova J, Brabec V, Bednarski PJ. Effects of cytotoxic cis- and trans-diammine monochlorido platinum(II) complexes on selenium-dependent redox enzymes and DNA. J Inorg Biochem 178:94-105 (2017)
Möller D, Gellert M, Langel W, Lillig CH. Molecular dynamics simulations and in vitro analysis of the CRMP2 thiol switch.Mol Biosyst 13:1744-1753 (2017)
Romero JI, Holubiec MI, Tornatore TL, Riviere S, Hanschmann EM, Kölliker-Frers RA, Tau J, Blanco E, Galeano P, Rodríguez de Fonseca F, Lillig CH, Capani F. Neuronal Damage Induced by Perinatal Asphyxia Is Attenuated by Postinjury Glutaredoxin-2 Administration. Oxid Med Cell Longev 2017:4162465 (2017)
Roman-Sosa G, Karger A, Kraatz F, Aebischer A, Wernike K, Maksimov P, Lillig CH, Reimann I, Brocchi E, Keller M, Beer M. The amino terminal subdomain of glycoprotein Gc of Schmallenberg virus: disulfide bonding and structural determinants of neutralization. J Gen Virol 98:1259-1273 (2017)
Lepka K, Volbracht K, Bill E, Schneider R, Rios N, Hildebrandt T, Ingwersen J,Prozorovski T, Lillig CH, van Horssen J, Steinman L, Hartung HP, Radi R, Holmgren A, Aktas O, Berndt C. Iron-sulfur glutaredoxin 2 protects oligodendrocytes against damage induced by nitric oxide release from activated microglia. Glia 65:1521-1534 (2017)
Berndt C, Lillig CH. Glutathione, Glutaredoxins, and Iron. Antioxid Redox Signal. 27:1235-1251 (2017)
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]

[2020-02-26]  [ page top ]