Publications

The MyoPulser field stimulator, a do it yourself programmable electronic pacemaker for contracting cells and tissues. Ott, C.; Jung, T. Sci Rep., 13(1):2461, 2023.
High glucose leads to redistribution of the proteasomal system. Grune, T.; Schnell, V.; Jung, T. Biofactors, 2023.
High-fat, sucrose and salt-rich diet during rat spermatogenesis lead to the development of chronic kidney disease in the female offspring of the F2 generation. Zhang, X.; Hasan, A.A.; Wu, H.; Gaballa, M.M.S.; Zeng, S.; Liu, L.; Xie, L.; Jung, T.; Grune, T.; Krämer, B.K.; Kleuser, B.; Li, J.; Hocher, B. FASEB J., 36(4):e22259, 2022.
Low-Grade Systemic Inflammation Interferes with Anabolic and Catabolic Characteristics of the Aged Human Skeletal Muscle. Draganidis, D, Jamurtas, A.Z.; Chondrogianni, N.; Mastorakos, G.; Jung, T.; Grune, T.; Papadopoulos, C.; Papanikolaou, K.; Papassotiriou, I.; Papaevgeniou, N.; Poulios, A.; Batrakoulis, A.; Deli, C.K.; Georgakouli, K.; Chatzinikolaou, A.; Karagounis, L.G.; Fatouros, I.G. Oxid Med Cell Longev., 2021:8376915, 2021.
Hypertrophy-Reduced Autophagy Causes Cardiac Dysfunction by Directly Impacting Cardiomyocyte Contractility. Ott, C.; Jung, T.; Brix, S.; John, C.; Betz, I.R.; Foryst-Ludwig, A.; Deubel, S.; Kuebler, W.M.; Grune, T.; Kintscher, U.; Grune, J. Cells, 10(4):805, 2021.
Reduced Liver Autophagy in High-Fat Diet Induced Liver Steatosis in New Zealand Obese Mice. Korovila, I.; Höhn, A.; Jung, T.; Grune, T.; Ott, C. Antioxidants (Basel), 10(4):501, 2021.
Sarcopenia - Molecular mechanisms and open questions. Wiedmer, P.; Jung, T.; Castro, J.P.; Pomatto, L.C.D.; Sun, P.Y.; Davies, K.J.A.; Grune, T. Ageing Res Rev., 65:101200, 2021. Review.
Redox homeostasis and cell cycle activation mediate beta-cell mass expansion in aged, diabetes-prone mice under metabolic stress conditions: Role of thioredoxin-interacting protein (TXNIP). Kehm, R.; Jähnert, M.; Deubel, S.; Flore, T.; König, J.; Jung, T.; Stadion, M.; Jonas, W.; Schürmann, A.; Grune, T.; Höhn, A., Redox Biol., 37:101748, 2020.
Punicalagin Attenuates Palmitate-Induced Lipid Droplet Content by Simultaneously Improving Autophagy in Hepatocytes. Korovila, I.; Jung, T.; Deubel, S.; Grune, T.; Ott, C. Mol Nutr Food Res., 64(20):e2000816, 2020.
Cardiomyocyte Contractility and Autophagy in a Premature Senescence Model of Cardiac Aging. Häseli, S.; Deubel, S.; Jung, T.; Grune, T.; Ott, C. Oxid Med Cell Longev., 2020:8141307, 2020.
Low steady-state oxidative stress inhibits adipogenesis by altering mitochondrial dynamics and decreasing cellular respiration. Fernando, R.; Wardelmann, K.; Deubel, S.; Kehm, R.; Jung, T.; Mariotti, M.; Vasilaki, A.; Gladyshev, V.N.; Kleinridders, A.; Grune, T.; Castro, J.P. Redox Biol., 32:101507, 2020.
The "MYOCYTER" - Convert cellular and cardiac contractions into numbers with ImageJ. Grune, T.; Ott, C.; Häseli, S.; Höhn, A.; Jung, T. Sci Rep., 9(1):15112, 2019.
Proteomic approach for understanding milder neurotoxicity of Carfilzomib against Bortezomib. Karademir, B.; Sari, G.; Jannuzzi, A.T.; Musunuri, S.; Wicher, G.; Grune, T.; Mi, J.; Hacioglu-Bay, H.; Forsberg-Nilsson, K.; Bergquist, J.; Jung, T. Sci Rep., 8(1):16318, 2018.
Low proteasomal activity in fast skeletal muscle fibers is not associated with increased age-related oxidative damage. Fernando, R.; Drescher, C.; Deubel, S.; Jung, T.; Ost, M.; Klaus, S.; Grune, T.; Castro, J.P. Exp Gerontol., 117:45-52, 2019.
Protein aggregates and proteostasis in aging: Amylin and β-cell function. Press, M.; Jung, T.; König, J.; Grune, T.; Höhn, A. Mech Ageing Dev., pii: S0047-6374(18)30045-30049, 2018. Review.
Age-related oxidative changes in pancreatic islets are predominantly located in the vascular system. Kehm, R.; König, J.; Nowotny, K.; Jung, T.; Deubel, S.; Gohlke, S.; Schulz, T.J.; Höhn, A. Redox Biol., 15:387-393, 2018.
“Cyt/Nuc”, a customizable and documenting ImageJ macro for evaluation of protein distributions between cytosol and nucleus. Grune, T.; Kehm, R.; Höhn, A.; Jung, T. Biotechnol. J., 13(5):e1700652, 2018.
4-Hydroxynonenal (HNE) modified proteins in metabolic diseases. Castro, J.P.; Jung, T.; Grune, T.; Siems, W. Free Radic Biol Med., 111:309-315, 2017.
Happily (n)ever after: Aging in the context of oxidative stress, proteostasis loss and cellular senescence. Höhn, A.; Weber, D.; Jung, T.; Ott, C.; Hugo, M.; Kochlik, B.; Kehm, R.; König, J.; Grune, T.; Castro, J.P. Redox Biol., 11:482-501, 2017. Review.
SIPS as a model to study age-related changes in proteolysis and aggregate formation. Ott, C.; Jung, T.; Grune, T.; Höhn, A. Mech Ageing Dev., pii: S0047-6374(17)30065-9, 2017. Review.
Proteostasis, oxidative stress and aging. Korovila, I.; Hugo, M.; Castro, J.P.; Weber, D.; Höhn, A.; Grune, T. Jung T. Redox Biol., 13:550-567, 2017. Review.
Mitochondrial contribution to lipofuscin formation. König, J.; Ott, C.; Hugo, M.; Jung, T.; Bulteau, A.L.; Grune, T.; Höhn A. Redox Biol., 11:673-681, 2017.
Reduced autophagy leads to an impaired ferritin turnover in senescent fibroblasts. Ott, C.; König, J.; Höhn, A.; Jung, T.; Grune, T. Free Radic Biol Med., 101:325-333, 2016.
Metabolic Syndrome, Redox State, and the Proteasomal System. Höhn, A.; König, J.; Jung, T. Antioxid Redox Signal., 25:902-917, 2016. Review.
Macroautophagy is impaired in old murine brain tissue as well as in senescent human fibroblasts. Ott, C.; König, J.; Höhn, A.; Jung, T.; Grune, T. Redox Biol., 10:266-273, 2016.
The molecular chaperone Hsp70 promotes the proteolytic removal of oxidatively damaged proteins by the proteasome. Reeg, S.; Jung, T.; Castro, J.P.; Davies, K.J.; Henze, A.; Grune, T. Free Radic Biol Med., 99:153-166, 2016.
Identification of an unstable 4-hydroxynonenal modification on the 20S proteasome subunit α7 by recombinant antibody technology. Just, J.; Jung, T.; Friis, N.A.; Lykkemark, S.; Drasbek, K.; Siboska, G.; Grune, T.; Kristensen, P. Free Radic Biol Med., 89:786-92, 2015.
Actual Isothermal Effects of Water-Filtered Infrared A (wIRA)-Irradiation. Höhn, A.; Hartmann, P.; Gebhart, V.; Sonntag, J.; Grune, T.; Jung, T. Photochem Photobiol., 91:887-894, 2015.
Advanced Glycation End Products and Oxidative Stress in Type 2 Diabetes Mellitus. Nowotny, K.; Jung, T.; Höhn, A.; Weber, D.; Grune, T. Biomolecules, 5:194-222, 2015. Review.
The proteasome and the degradation of oxidized proteins: Part III - Redox regulation of the proteasomal system. Jung, T.; Höhn, A.; Grune, T. Redox Biol., 2:388-394, 2014. Review.
The proteasome and the degradation of oxidized proteins: Part II - Protein oxidation and proteasomal degradation. Jung, T.; Höhn, A.; Grune, T. Redox Biol., 2:99-104, 2014. Review.
Accumulation of modified proteins and aggregate formation in aging. Nowotny, K.; Jung, T.; Grune, T.; Höhn, A. Exp Gerontol., 57:122-31, 2014.
Pathophysiological importance of aggregated damaged proteins. Höhn, A.; Jung, T.; Grune, T. Free Radic Biol Med., 71:70-89, 2014. Review.
The proteasome and the degradation of oxidized proteins: Part I - Structure of proteasomes. Jung, T.; Grune, T. Redox Biol., 1:178-182, 2013. Review.
Actin carbonylation: From cell dysfunction to organism disorder. Castro, J.P.; Jung, T.; Grune, T.; Almeida, H.J. Proteomics, 92:171-180, 2013.
Experimental basis for discriminating between thermal and athermal effects of water-filtered infrared A irradiation. Jung, T.; Grune, T. Ann N Y Acad Sci., 1259:33-38, 2012. Review.
Lipofuscin is formed independently of macroautophagy and lysosomal activity in stress-induced prematurely senescent human fibroblasts. Höhn, A.; Sittig, A.; Jung, T.; Grimm, S.; Grune, T. Free Radic Biol Med., 53:1760-1769, 2012.
“Protein Oxidation and Aging”, 2012, ASIN: B00A4ZKTVG
Carbonylation of the cytoskeletal protein actin leads to aggregate formation. Castro, J.P.; Ott, C.; Jung, T.; Grune, T.; Almeida, H. Free Radic Biol Med., 53:916-925, 2012.
“The Proteasomal System in Aging and Disease”, Vol. 109 (Progress in Molecular Biology & Translational Science), 1. Chapter: “Structure of the Proteasome” 2012, ISBN-10: 0123978637.
An experimental setup for the measurement of nonthermal effects during water-filtered infrared A-irradiation of mammalian cell cultures. Jung, T.; Höhn, A.; Lau, A.-M.; Piazena, H.; Grune, T. Photochem Photobiol., 88:371-380, 2011.
Lipofuscin inhibits the proteasome by binding to surface motifs. Höhn, A.; Jung, T.; Grimm, S.; Catalgol, B.; Weber, D.; Grune, T. Free Radic. Biol. Med., 50:585-591, 2011.
“The effects of water-filtered infrared A (wIRA) in tissue cultures: the example of human fibroblasts”. Jung, T.; Piazena, H.; Grune, T., Contribution to the book: “wIRA in tissue culture to study mechanistic effects of IR-action”, 2011.
Age-related loss of stress-induced nuclear proteasome activation is due to low PARP-1 activity. Bakondi, E.; Catalgol, B.; Bak, I.; Jung, T.; Bozaykut, P.; Bayramicli, M.; Ozer, N.K.; Grune, T. Free Radic Biol Med., 50:86-92, 2011.
Lipofuscin: detection and quantification by microscopic techniques. Jung, T.; Höhn, A.; Grune, T. Methods Mol Biol., 594:173-193, 2010. Review.
“Advanced Protocols in Oxidative Stress II: Methods in Molecular Biology” (2010), Chapter 13: Lipofuscin: Detection and Quantification by Microscopic Techniques, Tobias Jung, Annika Höhn, and Tilman Grune; ISBN: 1607614103; EAN: 9781607614104; Libri: 2661144.
Tau protein degradation is catalyzed by the ATP/ubiquitin-independent 20S proteasome under normal cell conditions. Grune, T.; Botzen, D.; Engels, M.; Voss, P.; Kaiser, B.; Jung, T.; Grimm, S.; Ermak, G.; Davies, K.J. Arch Biochem Biophys., 500:181-188, 2010.
Lipofuscin-bound iron is a major intracellular source of oxidants: Role in senescent cells. Höhn, A.; Jung, T.; Grimm, S.; Grune, T. Free Radic Biol Med., 48:1100-1108, 2010.
Effects of water-filtered infrared-A (wIRA) irradiation on human fibroblasts. Jung, T.; Höhn, A.; Piazena, H.; Grune, T. Free Radic Biol Med., 48:153-160, 2010.
The proteasomal system. Jung, T.; Catalgol, B.; Grune, T. Mol Aspects Med., 30:191-296, 2009. Review.
Impact of magnetic labeling on human and mouse stem cells and their long-term magnetic resonance tracking in a rat model of Parkinson disease. Stroh, A.; Boltze, J.; Sieland, K.; Hild, K.; Gutzeit, C.; Jung, T.; Kressel, J.; Hau, S.; Reich, D.; Grune, T.; Zimmer, C. Mol Imaging, 8:166-178, 2009.
The proteasome is an integral part of solar ultraviolet A radiation-induced gene expression. Catalgol, B.; Ziaja, I.; Breusing, N.; Jung, T.; Höhn, A.; Alpertunga, B.; Schröder, P.; Chondrogianni, N.; Gonos, E.S.; Petropoulos, I.; Friguet, B.; Klotz, L.O.; Krutmann, J.; Grune, T. J Biol Chem., 284:30076-30086, 2009.
Metabolism-induced oxidative stress is a mediator of glucose toxicity in HT22 neuronal cells. Rackova, L.; Snirc, V.; Jung, T.; Stefek, M.; Karasu, C.; Grune, T. Free Radic Res., 43:876-886, 2009.
Age-related differences in oxidative protein-damage in young and senescent fibroblasts. Jung, T.; Höhn, A.; Catalgol, B.; Grune, T. Arch Biochem Biophys., 483:127-135, 2009.
The proteasome and its role in the degradation of oxidized proteins. Jung, T.; Grune, T. IUBMB Life, 60:743-752, 2008. Review.
Freie Radikale – Antioxidanzien. Jung, T.; Grune, T. Haut, 1:6-9, 2008. Review.
Oxidative stress related changes in the brain of hypercholesterolemic rabbits. Aytan, N.; Jung, T.; Tamtürk, F.; Grune, T.; Kartal-Ozer, N. Biofactors, 33:225-236, 2008.
Lipofuscin: formation, distribution, and metabolic consequences. Jung, T.; Bader, N.; Grune, T. Ann N Y Acad Sci., 1119:97-111, 2007. Review.
Oxidized proteins: intracellular distribution and recognition by the proteasome. Jung, T.; Bader, N.; Grune, T. Arch Biochem Biophys., 462:231-237, 2007. Review.
Protein modification elicited by oxidized low-density lipoprotein (LDL) in endothelial cells: protection by (-)-epicatechin. Steffen, Y.; Jung, T.; Klotz, L.O.; Schewe, T.; Grune, T.; Sies, H. Free Radic Biol Med., 42:955-970, 2007.
Nitrotyrosine and protein carbonyls are equally distributed in HT22 cells after nitrosative stress. Jung, T.; Engels, M.; Klotz, L.O.; Kröncke, K.D.; Grune, T. Free Radic Biol Med., 42:773-86, 2007.
Vimentin is the specific target in skin glycation. Structural prerequisites, functional consequences, and role in skin aging. Kueper, T.; Grune, T.; Prahl, S.; Lenz, H.; Welge, V.; Biernoth, T.; Vogt, Y.; Muhr, G.M.; Gaemlich, A.; Jung, T.; Boemke, G.; Elsässer, H.P.; Wittern, K.P.; Wenck, H.; Stäb, F.; Blatt, T. J Biol Chem., 282:23427-23436, 2007.
The proteasome and its role in nuclear protein maintenance. Bader, N.; Jung, T.; Grune, T. Exp Gerontol., 42:864-870, 2007. Review.
Hyperammonemia causes protein oxidation and enhanced proteasomal activity in response to mitochondria-mediated oxidative stress in rat primary astrocytes. Widmer, R.; Kaiser, B.; Engels, M.; Jung, T.; Grune, T. Arch Biochem Biophys., 464:1-11, 2007.
Intracellular distribution of oxidized proteins and proteasome in HT22 cells during oxidative stress. Jung, T.; Engels, M.; Kaiser, B.; Poppek, D.; Grune, T. Free Radic Biol Med., 40:1303-1312, 2006.
Phosphorylation inhibits turnover of the tau protein by the proteasome: influence of RCAN1 and oxidative stress. Poppek, D.; Keck, S.; Ermak, G.; Jung, T.; Stolzing, A.; Ullrich, O.; Davies, K.J.; Grune, T. Biochem J., 400:511-520, 2006.
Tocopherol-mediated modulation of age-related changes in microglial cells: turnover of extracellular oxidized protein material. Stolzing, A.; Widmer, R.; Jung, T.; Voss, P.; Grune, T. Free Radic Biol Med., 40:2126-2135, 2006.
Degradation of glycated bovine serum albumin in microglial cells. Stolzing, A.; Widmer, R.; Jung, T.; Voss, P.; Grune, T. Free Radic Biol Med., 40:1017-1027, 2006.
Distribution of oxidized and HNE-modified proteins in U87 cells. Jung, T.; Engels, M.; Kaiser, B.; Grune, T. Biofactors, 24:165-170, 2005.
Protein oxidation and degradation during postmitotic senescence. Grune, T.; Merker, K.; Jung, T.; Sitte, N.; Davies, K. J. Free Radic Biol Med., 39:1208-1215, 2005.
Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Grune, T.; Jung, T.; Merker, K.; Davies, K. J. Int J Biochem Cell Biol., 36:2519-2530, 2004. Review.
Iron oxide particles for molecular magnetic resonance imaging cause transient oxidative stress in rat macrophages. Stroh, A.; Zimmer, C.; Gutzeit, C.; Jakstadt, M.; Marschinke, F.; Jung, T.; Pilgrimm, H.; Grune, T. Free Radic Biol Med., 36:976-984, 2004.