Selected publications

  • Barandun J, Delley CL, Ban N, Weber-Ban E* (2013) Crystal Structure of the Complex between Prokaryotic Ubiquitin-like Protein and Its Ligase PafA. JACS 135 (18), 6794 – 6797.

  • Özcelik D, Barandun J, Schmitz N, Sutter M, Guth E, Damberger FF, Allain FHT, Ban N & Weber-Ban E* (2012) Structures of Pup ligase PafA and depupylase Dop from the prokaryotic, ubiquitin-like modification pathway. Nature Communications 3, 1014.

  • Ranjan N, Damberger FF, Sutter M, Allain FH, Weber-Ban E* (2010) Solution structure and activation mechanism of ubiquitin-like small archaeal modifier proteins. J Mol Biol, Jan 28;405(4):1040-55.

  • Imkamp F, Striebel F, Sutter M, Ozcelik D, Zimmermann N, Sander P, Weber-Ban E* (2010) Dop functions as a depupylase in the prokaryotic ubiquitin-like modification pathway. EMBO Rep., 11(10): 791-7.

  • Striebel F, Hunkeler M, Summer H and Weber-Ban E* (2010) The mycobacterial Mpa-proteasome unfolds and degrades pupylated substrates by engaging Pup's N-terminus. EMBO Journal 29, 1262 – 1271.

  • Striebel F, Imkamp F, Sutter M, Steiner M, Mamedov A and Weber-Ban E* (2009) Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nature Struct. Mol. Biol. 16 : 647-652.

  • Kress W, Mutschler H and Weber-Ban E* (2009) Both ATPase domains of ClpA are critical for processing of stable protein structures. J. Biol. Chem. 284(45): 31441-52.

  • Kolygo K, Ranjan N, Kress W, Striebel F, Hollenstein K, Neelsen K, Steiner M, Summer H and Weber-Ban E* (2009) Studying Chaperone-Proteases using a Real-Time Approach based on FRET. J. Struct. Biol. 168(2): 267-77.

  • Kress W, Mutschler H and Weber-Ban E* (2007) Assembly Pathway of an AAA+ Protein: Tracking ClpA and ClpAP Complex Formation in Real Time. Biochemistry 46: 6183-93.



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