Publikationen von P. Zwickl

Kocabiyik, S.; Ozdemir, I.; Zwickl, P.; Ozdogan, S.: Molecular cloning and co-expression of Thermoplasma volcanium proteasome subunit genes. Protein Expression and Purification 73 (2), S. 223 - 230 (2010)

Medalia, N.; Beer, A.; Zwickl, P.; Mihalache, O.; Beck, M.; Medalia, O.; Navon, A.: Architecture and Molecular Mechanism of PAN, the Archaeal Proteasome Regulatory ATPase. Journal of Biological Chemistry 284 (34), S. 22952 - 22960 (2009)

Djuranovic, S.; Hartmann, M. D.; Habeck, M.; Ursinus, A.; Zwickl, P.; Martin, J.; Lupas, A. N.; Zeth, K.: Structure and Activity of the N-Terminal Substrate Recognition Domains in Proteasomal ATPases. Molecular Cell 34 (5), S. 580 - 590 (2009)

Rothballer, A.; Tzvetkov, N.; Zwickl, P.: Mutations in p97/VCP induce unfolding activity. FEBS Letters 581 (6), S. 1197 - 1201 (2007)

Lupas, A. N.; Martin, J.; Zwickl, P.: AAA plus proteins. Journal of Structural Biology 156, S. 1 - 1 (2006)

Medalia, N.; Sharon, M.; Martinez-Arias, R.; Mihalache, O.; Robinson, C. V.; Medalia, O.; Zwickl, P.: Functional and structural characterization of the Methanosarcina mazei proteasome and PAN complexes. Journal of Structural Biology 156 (1), S. 84 - 92 (2006)

Lin, G.; Hu, G. Q.; Tsu, C.; Kunes, Y. Z.; Li, H. L.; Dick, L.; Parsons, T.; Li, P.; Chen, Z. Q.; Zwickl, P. et al.; Weich, N.; Nathan, C.: Mycobacterium tuberculosis prcBA genes encode a gated proteasome with broad oligopeptide specificity. Molecular Microbiology 59 (5), S. 1405 - 1416 (2006)

Besche, H.; Navon, A.; Zwickl, P.: The membrane-bound lon protease from Thermoplasma displays unfolding activity. Israel Journal of Chemistry 46, S. 225 - 229 (2006)

Santos, L.; Zwickl, P.: Interaction analysis of the AAA ATPase TAA43 by the bacterial two-hybrid system. FEMS Microbiology Letters 254 (2), S. 293 - 299 (2006)

Gerega, A.; Rockel, B.; Peters, J.; Tamura, T.; Baumeister, W.; Zwickl, P.: VAT, the Thermoplasma homolog of mammalian p97/VCP, is an N domain-regulated protein unfoldase. Journal of Biological Chemistry 280 (52), S. 42856 - 42862 (2005)

Besche, H.; Zwickl, P.: The Thermoplasma acidophilum Lon protease has a Ser-Lys dyad active site. European Journal of Biochemistry 271 (22), S. 4361 - 4365 (2004)

Santos, L.; Frickey, T.; Peters, J.; Baumeister, W.; Lupas, A.; Zwickl, P.: Thermoplasma acidophilum TAA43 is an archaeal member of the eukaryotic meiotic branch of AAA ATPases. Biological Chemistry 385 (11), S. 1105 - 1111 (2004)

Besche, H.; Tamura, N.; Tamura, T.; Zwickl, P.: Mutational analysis of conserved AAA(+) residues in the archaeal Lon protease from Thermoplasma acidophilum. FEBS Letters 574 (1-3), S. 161 - 166 (2004)

Zhang, X. J.; Stoffels, K.; Wurzbacher, S.; Schoofs, G.; Pfeifer, G.; Banerjee, T.; Parret, A. H. A.; Baumeister, W.; De Mot, R.; Zwickl, P.: The N-terminal coiled coil of the Rhodococcus erythropolis ARC AAA ATPase is neither necessary for oligomerization nor nucleotide hydrolysis. Journal of Structural Biology 146 (1-2), S. 155 - 165 (2004)

Benaroudj, N.; Zwickl, P.; Seemüller, E.; Baumeister, W.; Goldberg, A. L.: ATP hydrolysis by the proteasome regulatory complex PAN serves multiple functions in protein degradation. Molecular Cell 11 (1), S. 69 - 78 (2003)

Zwickl, P.; Baumeister, W.; Steven, A.: Dis-assembly lines: the proteasome and related ATPase-assisted proteases. Current Opinion in Structural Biology 10 (2), S. 242 - 250 (2000)

Voges, D.; Zwickl, P.; Baumeister, W.: The 26S proteasome: A molecular machine designed for controlled proteolysis. Annual Review of Biochemistry 68, S. 1015 - 1068 (1999)

Zwickl, P.; Baumeister, W.: AAA-ATPases at the crossroads of protein life and death. Nature Cell Biology 1 (4), S. E97 - E98 (1999)

Zwickl, P.; Ng, D.; Woo, K.M.; Klenk, H.P.; Goldberg, A.: An Archaebacterial ATPase, Homologous to the ATPases in the Eukaryotic 26S Proteasome, Activates Protein Breakdown by the 20S Proteasome. J. Biol. Chem. 274, S. 26008 - 26014 (1999)

Zwickl, P.; Voges, D.; Baumeister, W.: The proteasome: a macromolecular assembly designed for controlled proteolysis. Philosophical Transactions of the Royal Society of London - Series B: Biological Sciences 354 (1389), S. 1501 - 1511 (1999)