piwik-script

    Chair of Biochemistry

    Publications (complete list)

    Original Publications

    Prieto-Garcia C, Hartmann O, Reissland M, Braun F, Bozkurt S, Pahor N, Fuss C, Schirbel A, Schülein-Völk C, Buchberger A, Calzado Canale MA, Rosenfeldt M, Dikic I, Münch C, Diefenbacher ME (2022). USP28 enables oncogenic transformation of respiratory cells and its inhibition potentiates molecular therapy targeting mutant EGFR, BRAF and PI3K. Mol Oncol. doi: 10.1002/1878-0261.13217

    Tolay N and Buchberger A (2021). Comparative profiling of stress granule clearance reveals differential contributions of the ubiquitin system. Life Sci Alliance 4:.

    Turakhiya A, Meyer SR, Marincola G, Böhm S, Vanselow JT, Schlosser A, Hofmann K and Buchberger A (2018). ZFAND1 recruits p97 and the 26S proteasome to promote the clearance of arsenite-induced stress granules. Mol Cell 70:906-919. Recommended by Faculty of 1000.
    [Read press release by University of Würzburg, research news by Alzforum]

    Takiuchi T, Nakagawa T, Tamiya H, Fujita H, Sasaki Y, Saeki Y, Takeda H, Sawasaki T, Buchberger A, Kimura T and Iwai K (2014). Suppression of LUBAC-mediated linear ubiquitination by a specific interaction between LUBAC and the deubiquitinases CYLD and OTULIN. Genes Cells 19:254-272.

    Böhm S  and Buchberger A (2013). The budding yeast Cdc48-Shp1 complex promotes cell cycle progression by positive regulation of Protein Phosphatase 1 (Glc7). PLoS One 8:e56486.

    Stapf C, Cartwright E, Bycroft M, Hofmann K and Buchberger A (2011). The general definition of the p97/valosin-containing protein (VCP)-interacting motif (VIM) delineates a new family of p97 cofactors. J Biol Chem 286:38670-38678.

    Hänzelmann P, Buchberger A and Schindelin H (2011). Hierarchical binding of cofactors to the AAA ATPase p97. Structure 19:833-843.

    Böhm S, Lamberti G, Fernández-Sáiz V, Stapf C and Buchberger A (2011). Cellular functions of Ufd2 and Ufd3 in proteasomal protein degradation depend on Cdc48 binding. Mol Cell Biol 31:1528-1539.

    Fernández-Sáiz V and Buchberger A (2010). Imbalances in p97 co-factor interactions in human proteinopathy. EMBO Rep 11:479-485.

    Knauth K, Cartwright E, Freund S, Bycroft M and Buchberger A (2009). VHL mutations linked to type 2C von Hippel-Lindau disease cause extensive structural perturbations in pVHL. J Biol Chem 284:10514-10522.

    Kern M, Fernandez-Saiz V, Schäfer Z and Buchberger A (2009). UBXD1 binds p97 through two independent binding sites. Biochem Biophys Res Comm 380:303-307.

    Bex C, Knauth K, Dambacher S and Buchberger A (2007). A yeast two-hybrid system reconstituting substrate recognition of the von Hippel-Lindau tumor suppressor protein. Nucleic Acids Res 35:e142.

    Allen M, Buchberger A* and Bycroft M (2006). The PUB domain functions as a p97 binding module in human peptide N-glycanase. J Biol Chem 281:25502-25508. *co-corresponding author

    Knauth K, Bex C, Jemth P and Buchberger A (2006). Renal cell carcinoma risk in type 2 von Hippel-Lindau disease correlates with defects in pVHL stability and HIF-1alpha interactions. Oncogene 25:370-377.

    Schuberth C and Buchberger A (2005). Membrane-bound Ubx2 recruits Cdc48 to ubiquitin ligases and their substrates to ensure efficient ER-associated degradation. Nat Cell Biol 7:999-1006.
    [Read Dispatch in Current Biology, Research Focus in Trends Cell Biol.Research Highlight in Nature Rev. Mol. Cell Biol.]

    Schuberth C, Richly H, Rumpf S and Buchberger A (2004). Shp1 and Ubx2 are adaptors of Cdc48 involved in ubiquitin-dependent protein degradation. EMBO Rep 5:818-824.

    Buchberger A, Howard MJ, Proctor M and Bycroft M (2001). The UBX domain: a widespread ubiquitin-like module. J Mol Biol 307:17-24.

    Buchberger A, Howard MJ, Freund SMV, Proctor M, Butler PJG, Fersht AR and Bycroft M (2000). Biophysical characterization of Elongin C from Saccharomyces cerevisiae. Biochemistry 39:11137-11146.

    Woodward ER, Buchberger A, Clifford SC, Hurst LD, Affara NA and Maher ER (2000). Comparative sequence analysis of the VHL tumor suppressor gene. Genomics 65:253-265.

    Buchberger A, Gässler C, Büttner M, McMacken R and Bukau B (1999). Functional defects of the DnaK756 mutant chaperone of Escherichia coli indicate distinct roles for amino- and carboxyl-terminal residues in substrate and co-chaperone interaction and interdomain communication. J Biol Chem 274:38017-38026.

    Gässler CS, Buchberger A, Laufen T, Mayer MP, Schröder H, Valencia A and Bukau B (1998). Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone. Proc Natl Acad Sci USA 95:15229-15234.

    Packschies L, Theyssen H, Buchberger A, Bukau B, Goody RS and Reinstein J (1997). GrpE accelerates nucleotide exchange of the molecular chaperone DnaK with an associative displacement mechanism. Biochemistry 36:3417-3422.

    Buchberger A, Schröder H, Hesterkamp T, Schönfeld HJ and Bukau B (1996). Substrate shuttling between the DnaK and GroEL systems indicates a chaperone network promoting protein folding. J Mol Biol 261:328-333.

    Buchberger A, Theyssen H, Schröder H, McCarty JS, Virgallita G, Milkereit P, Reinstein J and Bukau B (1995). Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication. J Biol Chem 270:16903-16910.

    McCarty JS, Buchberger A, Reinstein J and Bukau B (1995). The role of ATP in the functional cycle of the DnaK chaperone system. J Mol Biol 249:126-137.

    Buchberger A, Schröder H, Büttner M, Valencia A and Bukau B (1994). A conserved loop in the ATPase domain of the DnaK chaperone is essential for stable binding of GrpE. Nat Struct Biol 1:95-101.

    Buchberger A, Valencia A, McMacken R, Sander C and Bukau B (1994). The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. EMBO J 13:1687-1695.

     


    Reviews and Book Chapters

    Tolay N and Buchberger A (2022). Role of the ubiquitin system in stress granule metabolism. Int J Mol Sci 23:3624.

    Buchberger A (2022). Unfolding by Cdc48/p97: different strokes for different folks. Trends Cell Biol 32:278-280.

    Buchberger A, Schindelin H and Hänzelmann P (2015). Control of p97 function by cofactor binding. FEBS Lett 589:2578-2589.

    Buchberger A (2014). ERQC Autophagy: Yet Another Way to Die. Mol Cell 54:3-4.

    Buchberger A (2013). Roles of Cdc48 in regulated protein degradation in yeast. Subcell Biochem 66:195-222.

    Stolz A, Hilt W, Buchberger A and Wolf DH (2011). Cdc48: a power machine in protein degradation. Trends Biochem Sci 36:515-523.

    Buchberger A, Bukau B and Sommer T (2010). Protein Quality Control in the Cytosol and the Endoplasmic Reticulum: Brothers in Arms. Mol Cell 40:238-251.

    Buchberger A (2010). Control of ubiquitin conjugation by Cdc48 and its cofactors. Subcell Biochem 54:17-30.

    Schuberth C and Buchberger A (2008). UBX domain proteins: major regulators of the AAA ATPase Cdc48/p97. Cell Mol Life Sci 65:2360-2371.

    Buchberger A (2006). Cdc48 (p97) and its cofactors. In: Protein Degradation, Vol. 3: Cell Biology of the Ubiquitin-Proteasome System. RJ Mayer, AJ Ciechanover, M Rechsteiner (eds.), Wiley-VCH, Weinheim, pp. 194-211.

    Buchberger A (2002). From UBA to UBX: new words in the ubiquitin vocabulary. Trends Cell Biol 12:216-221.

    Wiederkehr T, Bukau B and Buchberger A (2002). Protein turnover: a CHIP programmed for proteolysis. Curr Biol 12:R26-R28.

    Buchberger A, Reinstein J and Bukau B (1999). The DnaK chaperone system: Mechanism and comparison with other Hsp70 systems. In: Molecular Chaperones and Folding Catalysts: Regulation, Cellular Function and Mechanisms. B Bukau (ed.), Harwood Academic Publishers, Amsterdam, pp. 609-635.

    Laufen T, Zuber U, Buchberger A and Bukau B (1998). DnaJ proteins. In: Molecular Chaperones in the Life Cycle of Proteins. AL Fink, Y Goto (eds.), Marcel Dekker, New York, pp. 241-274.

    Buchberger A and Bukau B (1997). Escherichia coli DnaK. In: Guidebook to Molecular Chaperones and Protein-Folding Catalysts. M-J Gething (ed.), Sambrook and Tooze, Oxford University Press, Oxford, pp. 22-25.

    Buchberger A and Bukau B (1997). Escherichia coli GrpE. In: Guidebook to Molecular Chaperones and Protein-Folding Catalysts. M-J Gething (ed.), Sambrook and Tooze, Oxford University Press, Oxford, pp. 137-139.

    Rüdiger S, Buchberger A and Bukau B (1997). Interaction of Hsp70 chaperones with substrates. Nat Struct Biol 4:342-349.