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Eilika Weber-Ban
Eilika Weber-Ban
Professor at ETH Zurich
Verified email at mol.biol.ethz.ch - Homepage
Title
Cited by
Cited by
Year
Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB
J Weibezahn, P Tessarz, C Schlieker, R Zahn, Z Maglica, S Lee, ...
Cell 119 (5), 653-665, 2004
5362004
Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
EU Weber-Ban, BG Reid, AD Miranker, AL Horwich
Nature 401 (6748), 90-93, 1999
5191999
Structural basis of enzyme encapsulation into a bacterial nanocompartment
M Sutter, D Boehringer, S Gutmann, S Günther, D Prangishvili, ...
Nature structural & molecular biology 15 (9), 939-947, 2008
4382008
Protein post-translational modifications in bacteria
B Macek, K Forchhammer, J Hardouin, E Weber-Ban, C Grangeasse, ...
Nature Reviews Microbiology 17 (11), 651-664, 2019
2812019
Chaperone rings in protein folding and degradation
AL Horwich, EU Weber-Ban, D Finley
Proceedings of the National Academy of Sciences 96 (20), 11033-11040, 1999
2591999
Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes
F Striebel, F Imkamp, M Sutter, M Steiner, A Mamedov, E Weber-Ban
Nature structural & molecular biology 16 (6), 647-651, 2009
2172009
ClpA mediates directional translocation of substrate proteins into the ClpP protease
BG Reid, WA Fenton, AL Horwich, EU Weber-Ban
Proceedings of the National Academy of Sciences 98 (7), 3768-3772, 2001
1882001
Clp chaperone–proteases: structure and function
W Kress, Ž Maglica, E Weber-Ban
Research in microbiology 160 (9), 618-628, 2009
1532009
Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX
DA Dougan, E Weber-Ban, B Bukau
Molecular cell 12 (2), 373-380, 2003
1502003
Pilus chaperones represent a new type of protein-folding catalyst
M Vetsch, C Puorger, T Spirig, U Grauschopf, EU Weber-Ban, ...
Nature 431 (7006), 329-333, 2004
1492004
Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes
F Striebel, W Kress, E Weber-Ban
Current opinion in structural biology 19 (2), 209-217, 2009
1442009
Protein architecture, dynamics and allostery in tryptophan synthase channeling
P Pan, E Woehl, MF Dunn
Trends in biochemical sciences 22 (1), 22-27, 1997
1341997
The mycobacterial Mpa–proteasome unfolds and degrades pupylated substrates by engaging Pup's N‐terminus
F Striebel, M Hunkeler, H Summer, E Weber‐Ban
The EMBO journal 29 (7), 1262-1271, 2010
1332010
Role of the proximal ligand in peroxidase catalysis. Crystallographic, kinetic, and spectral studies of cytochrome c peroxidase proximal ligand mutants.
K Choudhury, M Sundaramoorthy, A Hickman, T Yonetani, E Woehl, ...
Journal of Biological Chemistry 269 (32), 20239-20249, 1994
1231994
Dop functions as a depupylase in the prokaryotic ubiquitin‐like modification pathway
F Imkamp, F Striebel, M Sutter, D Özcelik, N Zimmermann, P Sander, ...
EMBO reports 11 (10), 791-797, 2010
1012010
A distinct structural region of the prokaryotic ubiquitin-like protein (Pup) is recognized by the N-terminal domain of the proteasomal ATPase Mpa
M Sutter, F Striebel, FF Damberger, FHT Allain, E Weber-Ban
FEBS letters 583 (19), 3151-3157, 2009
1012009
Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated pup intermediate
E Guth, M Thommen, E Weber-Ban
Journal of Biological Chemistry 286 (6), 4412-4419, 2011
952011
Monovalent metal ions play an essential role in catalysis and intersubunit communication in the tryptophan synthase bienzyme complex
EU Woehl, MF Dunn
Biochemistry 34 (29), 9466-9476, 1995
841995
Pupylation as a signal for proteasomal degradation in bacteria
F Striebel, F Imkamp, D Özcelik, E Weber-Ban
Biochimica et Biophysica Acta (BBA)-Molecular Cell Research 1843 (1), 103-113, 2014
812014
Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo
F Imkamp, T Rosenberger, F Striebel, PM Keller, B Amstutz, P Sander, ...
Molecular microbiology 75 (3), 744-754, 2010
792010
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