Publications
ZFP451-mediated SUMOylation of SATB2 drives embryonic stem cell differentiation. 2021. Urrutia AG, Ramachandran H, Cauchy P, Boo K, Ramamoorthy S, Boller S, Dogan E, Clapes T, Trompouki E, Torres-Padilla ME, Palvimo JJ, Pichler A, Grosschedl R. external pageGenes Devcall_made. 35(15-16):1142-1160.
Stress-induced nuclear condensation of NELF drives transcriptional downregulation. 2021. Rawat P, Boehning M, Hummel B, Aprile-Garcia F, Pandit AS, Eisenhardt N, Khavaran A, Niskanen E, Vos SM, Palvimo JJ, Pichler A, Cramer P and Sawarkar R. external pageMolecular Cellcall_made. 81:1013-1026.
Concomitant constitutive LNK and NFE2 mutation with loss of sumoylation in a case of hereditary thrombocythemia. 2020. Böckelmann LC, Gründer A, Wang W, Breucker J, Kaiser S, Pichler A and Pahl HL. external pageHaematologicacall_made.106(4):1158-1162.
Breucker J and Pichler A. 2019. Analysis of Sumoylation. external pageMethods in Molecular Biologycall_made,1934:223-233.
Eisenhardt N, Ilic D, Nagamalleswari E and Pichler A. 2019. Biochemical characterization of SUMO-conjugating enzymes by in vitro sumoylation assays. Ubiquitination and Protein Stability. external pageMethods in Enzymologycall_made, 618. 167-185.
Pichler A. 2018. How DNA vicinity controls SUMO E3 ligase activity. external pageEMBO J.call_made15;37(12).
Pichler A, Fatouros C, Lee H and Eisenhardt N. 2017. SUMO conjugation – a mechanistic view. external pageBioMolecular Conceptscall_made; 8(1):13-36.
Eisenhardt N, Chaugule VK and Pichler A. 2016. A fluorescent in vitro assay to investigate paralog specific SUMO conjugation. SUMO: Methods and Protocols. external pageMethods Mol Biol.call_made;1475:67-78.
Koidl S, Eisenhardt N, Fatouros C, Droescher M, Chaugule VK, and Pichler A. 2016. The SUMO2/3 specific E3 ligase ZNF451-1 regulates PML stability. external pageInternational Journal of Biochemistry & Cell Biologycall_made;79:478-487.
Tortola L, Nitsch R, Bertrand MJM, Kogler M, Redouane Y, Kozieradzki I, Uribesalgo I, Fennell L, Daugaard M, Klug H, Wirnsberger G, Wimmer R, Perlot T, Sarao R, Rao S, Hanada T, Takahashi N, Kernbauer E, Demiröz D, Superti-Furga G, Decker T, Pichler A, Ikeda F, Kroemer G, Vandenabeele P, Sorensen PH, and Penninger JM. 2016. The tumor suppressor Hace1 is a critical regulator of TNFR1-mediated cell fate. external pageCell Reportscall_made 17; 1481-92.
Eisenhardt N, Chaugule VK, Koidl S, Droescher M, Dogan E, Rettich J, Sutinen P, Imanishi SY, Hofmann K, Palvimo JJ and Pichler A. 2015. A novel vertebrate SUMO enzyme family discloses insights into SUMO-chain assembly. external pageNature Struct Mol Biol.,call_made 12. 959-67.
Cappadocia L, Pichler A and Lima CD. 2015. Structural basis for catalytic activation by the ZNF451 SUMO E3 ligase. external pageNature Struct Mol Biol.call_made, 12. 968-75.
Droescher M, Chaugule V and Pichler A. 2013. SUMO rules: regulatory concepts and their implication in neurologic function. external pageNeuroMolecular Medicinecall_made. 15. 639-660.
Klug H, Xaver M, Chaugule V, Mittler G, Koidl S, Klein F and Pichler A. 2013. Ubc9 sumoylation controls SUMO chain formation and meiotic chromosome synapsis in Saccharomyces cerevisiae. external pageMolecular Cell.call_made 50. 625-36.
Maderböck K and Pichler A. 2010. SUMO control. Chapter in “Conjugation and deconjugation of ubiquitin family modifiers” Landes Biosciences. Chapter 13, 158-69.
Pichler A. 2009. A second E2 for nedd8ylation expands substrate selection. external pageStructurecall_made. 17(3): 321-2.
Knipscheer P, Klug H, Sixma TK and Pichler A. 2009. Preparation of sumoylated substrates for biochemical analysis. external pageMethods in Molecular Biology.call_made 497: 201-10.
Knipscheer P#, Flotho A#, Klug H#, Olsen JV, van Dijk WJ, Fish A, Johnson ES, Mann M, Sixma TK* and Pichler A*. 2008. Ubc9 sumoylation regulates SUMO target discrimination. (*corresponding authors, #these authors contributed equally to this work). external pageMolecular Cellcall_made. 31: 371-382.
Pichler A. 2008. Analysis of Sumoylation. external pageMethods in Molecular Biologycall_made. 446:131-8.
Pichler A*°, Knipscheer P°, Oberhofer E, van Dijk P, Körner R, Olsen JV, Jentsch S, Melchior F and Sixma T*. 2005. SUMO modification of the ubiquitin conjugating enzyme E2-25K. external pageNature Struct Mol Biol.call_made 12: 264-9 (*corresponding authors, °these authors contributed equally to this work).
Bossis G, Chmielarska K, Gärtner U, Pichler A, Stieger E and Melchior F. 2005. A FRET-based assay to study SUMO1 modification in solution. external pageMethods in Enzymologycall_made Vol.398: pp. 20-32.
Pichler A, Knipscheer P, Saitoh H, Sixma T, and Melchior F. 2004. The RanBP2 SUMO E3 ligase is neither HECT nor RING type. external pageNature Struct Mol Biolcall_made.11: 984-91.
Melchior F and Pichler A. 2004. SUMO Modification. Encyclopedia of Biological Chemistry (W.J. Lennarz & M.D.Lane, eds), Elsevier, Oxford, Vol.4, pp. 130-134
Pichler A, and Melchior F. 2004. SUMO E3 ligases. Chapter in: Sumoylation – Molecular Biology and Biochemistry, Horizon Bioscience, 131-174.
Melchior F, Schergaut M, and Pichler A. 2003. SUMO: ligases, isopeptidases and nuclear pores. external pageTrends Biochem Scicall_made. 11:612-8.
Pichler A, and Melchior F. 2002. Ubiquitin-related modifier SUMO1 and nucleocytoplasmic transport. external pageTrafficcall_made 3: 381-7.
Kirsh O, Seeler JS, Pichler A, Gast A, Muller S, Miska E, Mathieu M, Harel-Bellan A, Kouzarides T; Melchior F, and Dejean A. 2002. The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. external pageEMBO Jcall_made. 21: 2682-91.
Pichler A°, Gast A°, Seeler JS, Dejean A, and Melchior F. 2002. The nucleoporin RanBP2 has SUMO1 E3 ligase activity. external pageCellcall_made 108: 109-20 (°these authors contributed equally to this work).
Sachdev S, Bruhn L, Sieber H, Pichler A, Melchior F, and Grosschedl R. 2001. PIASy, a nuclear matrix-associated SUMO E3 ligase, represses LEF1 activity by sequestration into nuclear bodies. external pageGenes Dev.call_made 15(23): 3088-103.
Gast A, Pichler A, Swaminathan S, and Melchior F. 2000. SUMO shifts to new functions. The ELSO Gazette 1 (http://www.the-elso-gazette/magazines/issue1).
Weninger W, Uthman A, Pammer J, Pichler A, Ballaun C, Lang IM, Plettenberg A, Bankl HC, Stürzl M, and Tschachler, E. 1996. Vascular Endothelial Growth Factor Production in Normal Epidermis and in Benign and Malignant Epithelial Skin Tumors. external pageLab. Invest.call_made 75: 647-657.
Ogris E, Rotheneder H, Mudrak I, Pichler A, and Wintersberger E. 1993. A Binding Site for Transcription Factor E2F Is a Target for trans Activation of Murine Thymidine Kinase by Polyomavirus Large T Antigen and Plays an Important Role in Growth Regulation of the Gene. external pageJ. Virol.call_made 67: 1765-1771.
Preprints
Altas B, Ju A, Cruces-Solís H, Karaca S, Winchenbach J, Kaplan Ö, Schwark M, Wieser G, Chaugule V, Majoul I, Hassan M, Goel R, Wojcik S, Pichler A, Mitkovski M, de Hoz L, Urlaub H, Jahn O, Saher G, Rhee JS, and Kawabe H. Physiological and pathophysiological homeostasis of astroglial channel proteins by Nedd4-2. bioRxiv external pagedoi: https://doi.org/10.1101/683441call_made.
Nagamalleswari E, Bakshi K, Breucker J, Gschweitl M, González-Prieto R, Eisenhardt N, Fatouros C,. Chaugule VK, Vertegaal ACO and Pichler A. UBC9 and EME1 sumoylation foster ribosomal DNA damage repair in CPT response. bioRxiv external pagedoi: https://doi.org/10.1101/2022.04.11.487628.call_made
Bakshi K, Nagamalleswari E, Breucker J, Eisenhardt N, Tiwari R, González-Prieto R, Fatouros C, Chaugule VK, Lee H, Ilic D, Trulsson F, Mittler F, Vertegaal ACO, and Pichler A. Multi-level monitoring of the structure-specific endonuclease EME1-MUS81 in CPT induced nucleolar rDNA repair. bioRxiv doi: external pagehttps://doi.org/10.1101/2022.04.11.487769.call_made
Salas-Lloret D, van der Meulen C, Nagamalleswari E, Gracheva E, de Ru AH, Otte AM, van Veelen PA, Pichler A, Goedhart J, Vertegaal ACO and González-Prieto R. SUMO Activated Target Traps (SATTs) enable the identification of a comprehensive E3-specific SUMO proteome- bioRxiv doi: external pagehttps://doi.org/10.1101/2022.06.22.497173call_made.