Rüdiger group

2022

Koopman MB, Ferrari L, Rüdiger SGD, Berghoff SA, Spieth L, Saher G, Stacho M, Manahan-Vaughan D, Shrestha P, Klann E, Cisneros J. 254 Dopamine ramps for accurate value learning under uncertainty. Neurosciences 2022 45:0166-2236.

Garfagnini T, Ferrari L, Koopman MB, Halters S, Van Kappel E, Mayer G, Maurice MM, Rüdiger SGD, Friedler A. A peptide strategy for inhibiting different protein aggregation pathways in disease. BioRXiv 2022 Link

Koopman MB, Ferrari L, Rüdiger SGD. How do protein aggregates escape quality control in neurodegeneration?. Trends in Neurosciences. 2022 45:257-71 Link

2021

Jarosińska OD, Rüdiger SGD. Molecular Strategies to Target Protein Aggregation in Huntington’s Disease. Front. Mol. Biosci. 2021 8:1068 Link

Lashley T, Tossounian MA, Heaven NC, Wallworth S, Peak-Chew S, Bradshaw A, Cooper JM, de Silva R, Srai SK, Malanchuk O, Filonenko V, Koopman MB, Rüdiger SGD, Skehel M, Gout I. Extensive Anti-CoA Immunostaining in Alzheimer’s Disease and Covalent Modification of Tau by a Key Cellular Metabolite Coenzyme A. Front. Cell. Neurosci. 2021 15:411 Link

Dekker FA and Rüdiger SGD. The Mitochondrial Hsp90 TRAP1 and Alzheimer’s Disease. Front. Mol. Biosci. 2021 8: 697913 Link

Aragonès Pedrola J, Rüdiger SGD. Double J-domain piloting of an Hsp70 substrate. J. Biol. Chem. 2021 100717 Link

2020

Bhattacharya K, Weidenauer L, Luengo TM, Pieters EC, Echeverría PC, Bernasconi L, Wider D, Sadian Y, Koopman MB, Villemin M, Bauer C, Rüdiger SGD, Quadroni M, Picard D. The Hsp70-Hsp90 co-chaperone Hop/Stip1 shifts the proteostatic balance from folding towards degradation. Nat. Comm. 2020 11:1-21 Link

Koopman MB, Rüdiger SGD. Alzheimer cells on their way to derailment show selective changes in protein quality control network. Front. Mol. Biosci. 2020 fmolb.2020.00214 Link

Koopman MB, Rüdiger SGD. Behind closed gates–chaperones and charged residues determine protein fate. EMBO J. 2020 e104939 Link

Weickert S, Wawrzyniuk M, John LH, Rüdiger SGD, Drescher M. The mechanism of Hsp90-induced oligomerizaton of Tau. Science Adv. 2020 11:eaax6999 Link

Ferrari L, Stucchi R, Konstantoulea K, van der Kamp G, Kos R, Geerts WJC, van Bezouwen LS, Förster FG, Altelaar M, Hoogenraad CC, Rüdiger SGD. Arginine π-stacking drives binding to fibrils of the Alzheimer protein Tau. Nat Commun. 2020 11:571 Link

Burmann BM, Gerez JA, Matečko-Burmann I, Campioni S, Kumari P, Ghosh D, Mazur A, Aspholm EE, Šulskis D, Wawrzyniuk M, Bock T, Schmidt A, Rüdiger SGD, Riek R & Hiller S. Regulation of α-synuclein by chaperones in mammalian cells. Nature 2020 577:127-32 Link

2019

Ferrari L, Rüdiger SGD. (2019) Hsp90 Chaperone in Disease. In: Asea A., Kaur P. (eds) Heat Shock Protein 90 in Human Diseases and Disorders. Heat Shock Proteins, vol 19. Springer, Cham. Link

Hooikaas PJ, Martin M, Mühlethaler T, Kuijntjes G-J, Peeters CAE, Katrukha EA, Ferrari L, Stucchi R, Verhagen DGF, van Riel WE, Grigoriev I, Altelaar AFM, Hoogenraad CC, Rüdiger SGD, Steinmetz MO, Kapitein LC, Akhmanova A. MAP7 family proteins regulate kinesin-1 recruitment and activation. J Cell Biol. 2019 218(4):1298-1318. Link

Morán Luengo T, Mayer MP, Rüdiger SGD. The Hsp70-Hsp90 chaperone cascade in protein folding. Trends Cell Biol. 2019 29(2):164-177. Link

2018

Ferrari L, Rüdiger SGD. Recombinant production and purification of the human protein Tau. Protein Eng Des Sel 2018 31(12):447-455. Link

Radli M, Rüdiger SGD. Dancing with the diva: Hsp90-client interactions J Mol Biol. 2018 in press Link

Morán Luengo T, Kityk R, Mayer MP, Rüdiger SGD. Hsp90 breaks the deadlock of the Hsp70 chaperone system. Mol Cell. 2018 70:545-552 (cover story). Link

2017

Radli M, Rüdiger SGD. Picky Hsp90 – every game with a different mate. Mol Cell. 2017 67:899-900 (invited preview). Link

Radli M, Veprintsev DB, Rüdiger SGD. Production and purification of human Hsp90β in Escherichia coli. PLoS One. 2017 12(6):e0180047. doi:10.1371/journal.pone.0180047. Link

2016

Anvarian Z, Nojima H, van Kappel EC, Madl T, Spit M, Viertler M, Jordens I, Low TY, van Scherpenzeel R, Kuper I, Richter K, Heck AJR, Boelens R, Vincent JP, Rüdiger SGD, Maurice MM. Axin cancer mutants form nano-aggregates to rewire the Wnt signaling network. Nature Struct Mol Biol. 2016 23:324-32. Link

2015

Hagemans D, van Belzen IAEM, Morán Luengo T, Rüdiger SGD. A script to highlight hydrophobicity and charge on protein surfaces. Frontiers Mol Biosci. 2015 2:56. Link

Sinnige T, Karagöz GE, Rüdiger SGD. Protein Folding and Chaperones. Encyclopedia of Life Sciences (ELS). 2015 Link

Karagöz GE, Rüdiger SGD. Hsp90 interaction with clients. Trends Biol Sci. 2015 40:117-125. Link

2014

Karagöz GE, Duarte AMS, Akoury E, Ippel H, Biernat J, Morán Luengo T, Radli M, Didenko T, Nordhues BA, Veprintsev DB, Dickey CA, Mandelkow E, Zweckstetter M, Boelens R, Madl T, Rüdiger SGD. Hsp90-Tau complex reveals molecular basis for specificity in chaperone action. Cell. 2014 156:963-974. Link

2013

Minde DP, Radli M, Forneris F, Maurice MM, Rüdiger SGD. Large extent of disorder in Adenomatous Polyposis Coli offers a strategy to guard Wnt signalling against point mutations. PLoS One. 2013 8:e77257. Link

Xue B, Romero PR, Noutsou M, Maurice MM, Rüdiger SGD, William AM Jr, Mizianty MJ, Kurgan L, Uversky VN, Dunker AK. Stochastic machines as a colocalization mechanism for scaffold protein function. FEBS Lett. 2013 587:1587-91. Link

2012

Minde DP, Maurice MM, Rüdiger SGD. Determining biophysical protein stability in lysates by a fast proteolysis assay, FASTpp. PLoS One. 2012 7:e46147. Link

Suijkerbuijk SJ, van Dam TJ, Karagöz GE, von Castelmur E, Hubner NC, Duarte AMS, Vleugel M, Perrakis A, Rüdiger SGD, Snel B, Kops GJ. The vertebrate mitotic checkpoint protein BUBR1 is an unusual pseudokinase. Dev Cell. 2012 22:1321-9. Link

Li Y, Karagöz GE, Seo YH, Zhang T, Jiang Y, Yu Y, Duarte AMS, Schwartz SJ, Boelens R, Carroll K, Rüdiger SGD, Sun D. Sulforaphane inhibits pancreatic cancer through disrupting Hsp90-p50(Cdc37) complex and direct interactions with amino acids residues of Hsp90. J Nutr Biochem. 2012 23:1617-26. Link

Tauriello DV, Jordens I, Kirchner K, Slootstra JW, Kruitwagen T, Bouwman BA, Noutsou M, Rüdiger SGD, Schwamborn K, Schambony A, Maurice MM. Wnt/β-catenin signaling requires interaction of the Dishevelled DEP domain and C terminus with a discontinuous motif in Frizzled. Proc Natl Acad Sci U S A. 2012 109:E812-20. Link

Didenko T, Duarte AM, Karagöz GE, Rüdiger SGD. Hsp90 structure and function studied by NMR spectroscopy. Biochim Biophys Acta. 2012 1823:636-47. Link

2011

Minde DP, Anvarian Z, Rüdiger SGD, Maurice MM. Messing up disorder: how do missense mutations in the tumor suppressor protein APC lead to cancer? Mol Cancer. 2011 10:101. Link

Karagöz GE, Sinnige T, Hsieh O, Rüdiger SGD. Expressed protein ligation for a large dimeric protein. Protein Eng Des Sel. 2011 24:495-501. Link

Katz C, Levy-Beladev L, Rotem-Bamberger S, Rito T, Rüdiger SGD, Friedler A. Studying protein-protein interactions using peptide arrays. Chem Soc Rev. 2011 40:2131-45. Link

Karagöz GE, Duarte AMS, Ippel H, Uetrecht C, Sinnige T, van Rosmalen M, Hausmann J, Heck AJR, Boelens R, Rüdiger SGD. N-terminal domain of human Hsp90 triggers binding to the cochaperone p23. Proc Natl Acad Sci U S A. 2011 108:580-5. Link

Noutsou M, Duarte AMS, Anvarian Z, Didenko T, Minde DP, Kuper I, de Ridder I, Oikonomou C, Friedler A, Boelens R, Rüdiger SGD, Maurice MM. Critical scaffolding regions of the tumor suppressor Axin1 are natively unfolded. J Mol Biol. 2011 405:773-86. Link

Didenko T, Boelens R, Rüdiger SGD. 3D DOSY-TROSY to determine the translational diffusion coefficient of large protein complexes. Protein Eng Des Sel. 2011 24:99-103. Link

2010

Sinnige T, Karagöz GE, Rüdiger SGD. Protein Folding and Chaperones. Encyclopedia of Life Sciences (ELS). 2010 Link (Updated in 2015)

2009

Tsaytler PA, Krijgsveld J, Goerdayal SS, Rüdiger S, Egmond MR. Novel Hsp90 partners discovered using complementary proteomic approaches. Cell Stress Chaperones. 2009 14:629-38. Link

2008

Rotem S, Katz C, Benyamini H, Lebendiker M, Veprintsev D, Rüdiger S, Danieli T, Friedler A. The structure and interactions of the proline-rich domain of ASPP2. J Biol Chem. 2008 283:18990-9. Link

Katz C, Benyamini H, Rotem S, Lebendiker M, Danieli T, Iosub A, Refaely H, Dines M, Bronner V, Bravman T, Shalev DE, Rüdiger S, Friedler A. Molecular basis of the interaction between the antiapoptotic Bcl-2 family proteins and the proapoptotic protein ASPP2. Proc Natl Acad Sci U S A. 2008 105:12277-82. Link

Rodriguez F, Arséne-Ploetze F, Rist W, Rüdiger S, Schneider-Mergener J, Mayer MP, Bukau B. Molecular basis for regulation of the heat shock transcription factor σ32 by the DnaK and DnaJ chaperones. Mol Cell. 2008 32:347-58. Link

2007

Mayer S, Rüdiger S, Ang HC, Joerger AC, Fersht AR. Correlation of levels of folded recombinant p53 in escherichia coli with thermodynamic stability in vitro. J Mol Biol. 2007 372:268-76. Link

2006

Vega CA, Kurt N, Chen Z, Rüdiger S, Cavagnero S. Binding specificity of an alpha-helical protein sequence to a full-length Hsp70 chaperone and its minimal substrate-binding domain. Biochemistry. 2006 45:13835-46. Link

Yu GW, Rüdiger S, Veprintsev D, Freund S, Fernandez-Fernandez MR, Fersht AR. The central region of HDM2 provides a second binding site for p53. Proc Natl Acad Sci U S A. 2006 103:1227-32. Link

Sinnige T, Karagöz GE, Rüdiger SGD. Protein Folding and Chaperones. Encyclopedia of Life Sciences (ELS). 2006 Link (Updated 2010 & 2015)

2004

Friedler A, DeDecker BS, Freund SMV, Blair C, Rüdiger S, Fersht AR. Structural distortion of p53 by the mutation R249S and its rescue by a designed peptide: implications for “mutant conformation”. J Mol Biol. 2004;336:187-96. Link

2002

Vandenbroeck K, Alloza I, Brehmer D, Billiau A, Proost P, McFerran N, Rüdiger S, Walker B. The conserved helix C region in the superfamily of interferon-gamma/interleukin-10-related cytokines corresponds to a high-affinity binding site for the HSP70 chaperone DnaK. J Biol Chem. 2002;277:25668-76. Link

Rüdiger S, Freund SMV, Veprintsev DB, Fersht AR. CRINEPT-TROSY NMR reveals p53 core domain bound in an unfolded form to the chaperone Hsp90. Proc Natl Acad Sci U S A. 2002;99:11085-90. Link

Hansson LO, Friedler A, Freund S, Rüdiger S, Fersht AR. Two sequence motifs from HIF-1alpha bind to the DNA-binding site of p53. Proc Natl Acad Sci U S A. 2002;99:10305-9. Link

Friedler A, Hansson LO, Veprintsev DB, Freund SMV, Rippin TM, Nikolova PV, Proctor MR, Rüdiger S, Fersht AR. A peptide that binds and stabilizes p53 core domain: chaperone strategy for rescue of oncogenic mutants. Proc Natl Acad Sci U S A. 2002;99:937-42. Link

2001

Patzelt H, Rüdiger S, Brehmer D, Kramer G, Vorderwülbecke S, Schaffitzel E, Waitz A, Hesterkamp T, Dong L, Schneider-Mergener J, Bukau B, Deuerling E. Binding specificity of Escherichia coli trigger factor. Proc Natl Acad Sci U S A. 2001;98:14244-9. Link

Schaffitzel E, Rüdiger S, Bukau B, Deuerling E. Functional dissection of trigger factor and DnaK: interactions with nascent polypeptides and thermally denatured proteins. Biol Chem. 2001;382:1235-43. Link

Brehmer D, Rüdiger S, Gässler CS, Klostermeier D, Packschies L, Reinstein J, Mayer MP, Bukau B. Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange. Nature Struct Biol. 2001;8:427-32. Link

Rüdiger S, Schneider-Mergener J, Bukau B. Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. EMBO J. 2001;20:1042-50. Link

2000

Rüdiger S, Mayer MP, Schneider-Mergener J, Bukau B. Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch. J Mol Biol. 2000;304:245-51. Link

Mayer MP, Rüdiger S, Bukau B. Molecular basis for interactions of the DnaK chaperone with substrates. Biol Chem. 2000;381:877-85. Link

Mayer MP, Schröder H, Rüdiger S, Paal K, Laufen T, Bukau B. Multistep mechanism of substrate binding determines chaperone activity of Hsp70. Nature Struct Biol. 2000;7:586-93. Link

1999

Mogk A, Tomoyasu T, Goloubinoff P, Rüdiger S, Röder D, Langen H, Bukau B. Identification of thermolabile Escherichia coli proteins: prevention and reversion of aggregation by DnaK and ClpB. EMBO J. 1999;18:6934-49. Link

Knoblauch NT, Rüdiger S, Schönfeld HJ, Driessen AJ, Schneider-Mergener J, Bukau B. Substrate specificity of the SecB chaperone. J Biol Chem. 1999;274:34219-25. Link

Brix J, Rüdiger S, Bukau B, Schneider-Mergener J, Pfanner N. Distribution of binding sequences for the mitochondrial import receptors Tom20, Tom22, and Tom70 in a presequence-carrying preprotein and a non-cleavable preprotein. J Biol Chem. 1999;274:16522-30. Link

1997

Rüdiger S, Buchberger A, Bukau B. Interaction of Hsp70 chaperones with substrates. Nature Struct Biol. 1997;4:342-9. Link

Rüdiger S, Germeroth L, Schneider-Mergener J, Bukau B. Substrate specificity of the DnaK chaperone determined by screening cellulose-bound peptide libraries. EMBO J. 1997;16:1501-7. Link

1996

McCarty JS, Rüdiger S, Schönfeld HJ, Schneider-Mergener J, Nakahigashi K, Yura T, Bukau B. Regulatory region C of the E. coli heat shock transcription factor, sigma32, constitutes a DnaK binding site and is conserved among eubacteria. J Mol Biol. 1996;256:829-37. Link

Gamer J, Multhaup G, Tomoyasu T, McCarty JS, Rüdiger S, Schönfeld HJ, Schirra C, Bujard H, Bukau B. A cycle of binding and release of the DnaK, DnaJ and GrpE chaperones regulates activity of the Escherichia coli heat shock transcription factor sigma32. EMBO J. 1996;15:607-17. Link

1994

Herdegen T, Rüdiger S, Mayer B, Bravo R, Zimmermann M. Expression of nitric oxide synthase and colocalisation with Jun, Fos and Krox transcription factors in spinal cord neurons following noxious stimulation of the rat hindpaw. Brain Res Mol Brain Res. 1994;22:245-58. Link