Publications Madl Group, Medical University Graz

Selected Publications (since 2015)

Structural basis of nucleic-acid recognition and double-strand unwinding by the essential neuronal protein Pur-alpha.
Weber J, Bao H, Hartlmüller C, Wang Z, Windhager A, Janowski R, Madl T, Jin P, Niessing D.
Elife (2016). link

The activity of protein phosphatase 5 towards native clients is modulated by the middle- and C-terminal domains of Hsp90.
Haslbeck V, Eckl JM, Drazic A, Rutz DA, Lorenz OR, Zimmermann K, Kriehuber T, Lindemann C, Madl T, Richter K.
Sci Rep. (2015);5:17058. link

Optimization of lipid production with a genome-scale model of Yarrowia lipolytica.
Kavšček M, Bhutada G, Madl T, Natter K.
BMC Syst Biol. (2015);9:72. link

The Solution Structure of the Lantibiotic Immunity Protein NisI and Its Interactions with Nisin.
Hacker C, Christ NA, Duchardt-Ferner E, Korn S, Göbl C, Berninger L, Düsterhus S, Hellmich UA, Madl T, Kötter P, Entian KD, Wöhnert J.
J Biol Chem. (2015);290(48):28869-86. link

Type-II NADH:quinone oxidoreductase from Staphylococcus aureus has two distinct binding sites and is rate limited by quinone reduction.
Sena FV, Batista AP, Catarino T, Brito JA, Archer M, Viertler M, Madl T, Cabrita EJ, Pereira MM.
Mol Microbiol (2015);98(2):272-88. link

A Crystallin Fold in the Interleukin-4-inducing Principle of Schistosoma mansoni Eggs (IPSE/α-1) Mediates IgE Binding for Antigen-independent Basophil Activation.
Meyer NH, Mayerhofer H, Tripsianes K, Blindow S, Barths D, Mewes A, Weimar T, Köhli T, Bade S, Madl T, Frey A, Haas H, Mueller-Dieckmann J, Sattler M, Schramm G.
J Biol Chem. (2015);290(36):22111-26. link

Hsp90 regulates the dynamics of its cochaperone Sti1 and the transfer of Hsp70 between modules.
Röhl A, Wengler D, Madl T, Lagleder S, Tippel F, Herrmann M, Hendrix J, Richter K, Hack G, Schmid AB, Kessler H, Lamb DC, Buchner J.
Nat Commun. (2015);6:6655. link

Introduction of germline residues improves the stability of anti-HIV mAb 2G12-IgM.
Chromikova V, Mader A, Hofbauer S, Göbl C, Madl T, Gach JS, Bauernfried S, Furtmüller PG, Forthal DN, Mach L, Obinger C, Kunert R.
Biochim Biophys Acta (2015);1854(10 Pt A):1536-44. link

AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control.
Gersch M, Famulla K, Dahmen M, Göbl C, Malik I, Richter K, Korotkov VS, Sass P, Rübsamen-Schaeff H, Madl T, Brötz-Oesterhelt H, Sieber SA.
Nat Commun. (2015);6:6320. link

A compact native 24-residue supersecondary structure derived from the villin headpiece subdomain.
Hocking HG, Häse F, Madl T, Zacharias M, Rief M, Žoldák G.
Biophys J. (2015);108(3):678-86. link

Hop/Sti1 phosphorylation inhibits its co-chaperone function.
Röhl A, Tippel F, Bender E, Schmid AB, Richter K, Madl T, Buchner J.
EMBO Rep. (2015);16(2):240-9. link