E. Weber-Ban

发表

The flexible attachment of the N-domains to the ClpA ring body allows their use on demand.

Zeljka Maglica, Susanne Cranz-Mileva, F. Imkamp, 2008, Journal of molecular biology.

Studying chaperone-proteases using a real-time approach based on FRET.

K. Neelsen, K. Hollenstein, F. Striebel, 2009, Journal of structural biology.

Survival in Hostile Conditions: Pupylation and the Proteasome in Actinobacterial Stress Response Pathways

L. Keller, E. Weber-Ban, Tatjana von Rosen, 2021, Frontiers in Molecular Biosciences.

The Bacterial Proteasome at the Core of Diverse Degradation Pathways

E. Weber-Ban, A. U. Müller, 2019, Front. Mol. Biosci..

Structural Analysis of the Bacterial Proteasome Activator Bpa in Complex with the 20S Proteasome.

D. Boehringer, N. Ban, M. Leibundgut, 2016, Structure.

Pupylation-dependent and -independent proteasomal degradation in mycobacteria

Michal Ziemski, F. Imkamp, E. Weber-Ban, 2015, Biomolecular concepts.

Activity of the Mycobacterial Proteasomal ATPase Mpa Is Reversibly Regulated by Pupylation*

Cyrille L. Delley, F. Striebel, D. Özcelik, 2011, The Journal of Biological Chemistry.

The mycobacterial Mpa–proteasome unfolds and degrades pupylated substrates by engaging Pup's N‐terminus

F. Striebel, M. Hunkeler, E. Weber-Ban, 2010, The EMBO journal.

The pupylation pathway and its role in mycobacteria

J. Barandun, Cyrille L. Delley, Jonas Barandun, 2012, BMC Biology.

Cdc 48-like protein of actinobacteria ( Cpa ) is a novel proteasome interactor in 1 mycobacteria and related organisms 2

D. Veprintsev, C. Giese, A. Jomaa, 2018 .

Prokaryotic Ubiquitin-Like Protein and Its Ligase/Deligase Enyzmes.

Cyrille L. Delley, Michal Ziemski, E. Weber-Ban, 2017, Journal of molecular biology.

Crystal structure of the complex between prokaryotic ubiquitin-like protein and its ligase PafA.

N. Ban, J. Barandun, Cyrille L. Delley, 2013, Journal of the American Chemical Society.

Clp chaperone-proteases: structure and function.

Zeljka Maglica, Wolfgang Kress, E. Weber-Ban, 2009, Research in microbiology.

Prokaryotic ubiquitin-like protein (Pup) is coupled to substrates via the side chain of its C-terminal glutamate.

F. Damberger, M. Sutter, F. Allain, 2010, Journal of the American Chemical Society.

Dop functions as a depupylase in the prokaryotic ubiquitin‐like modification pathway

M. Sutter, P. Sander, F. Striebel, 2010, EMBO reports.

Structures of Pup ligase PafA and depupylase Dop from the prokaryotic ubiquitin-like modification pathway

N. Ban, F. Damberger, M. Sutter, 2012, Nature Communications.

Toxic Activation of an AAA+ Protease by the Antibacterial Drug Cyclomarin A.

Kamila B. Franke, M. Mayer, B. Bukau, 2019, Cell chemical biology.

Chaperone-Proteases of Mycobacteria

E. Weber-Ban, Juerg Laederach, Julia Leodolter, 2014 .

Structure and functional implications of WYL domain-containing bacterial DNA damage response regulator PafBC

N. Ban, M. Leibundgut, E. Weber-Ban, 2019, Nature Communications.

Intersubunit Cross-talk in Pyridoxal 5′-Phosphate Synthase, Coordinated by the C Terminus of the Synthase Subunit*

P. Gehrig, N. Amrhein, C. Moccand, 2009, Journal of Biological Chemistry.

Antibacterial peptide CyclomarinA creates toxicity by deregulating the Mycobacterium tuberculosis ClpC1–ClpP1P2 protease

I. Sinning, M. Carroni, A. Mogk, 2022, The Journal of biological chemistry.

Pupylated proteins are subject to broad proteasomal degradation specificity and differential depupylation

H. Cui, E. Weber-Ban, Juerg Laederach, 2019, PloS one.

Assembly pathway of an AAA+ protein: tracking ClpA and ClpAP complex formation in real time.

H. Mutschler, Wolfgang Kress, E. Weber-Ban, 2007, Biochemistry.

Optimal efficiency of ClpAP and ClpXP chaperone-proteases is achieved by architectural symmetry.

Zeljka Maglica, Kristina Kolygo, E. Weber-Ban, 2009, Structure.

Protein post-translational modifications in bacteria

B. Maček, K. Forchhammer, I. Mijakovic, 2019, Nature Reviews Microbiology.

Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes

M. Sutter, F. Striebel, Markus Sutter, 2009, Nature Structural &Molecular Biology.

Structure and functional implications of WYL-domain-containing transcription factor PafBC involved in the mycobacterial DNA damage response

N. Ban, M. Leibundgut, E. Weber-Ban, 2019, bioRxiv.

Transcriptional control of mycobacterial DNA damage response by sigma adaptation

N. Ban, E. Kummer, E. Weber-Ban, 2021, Science advances.

Mycobacterial Ubiquitin-like Protein Ligase PafA Follows a Two-step Reaction Pathway with a Phosphorylated Pup Intermediate*

Michael Thommen, E. Guth, Eilika Weber-Ban, 2010, The Journal of Biological Chemistry.

Global unfolding of a substrate protein by the Hsp100 chaperone ClpA

A. Horwich, A. Miranker, B. Reid, 1999, Nature.

Targeted protein degradation: from small molecules to complex organelles—a Keystone Symposia report

J. Frydman, M. Słabicki, C. Bertozzi, 2022, Annals of the New York Academy of Sciences.

Mycobacterium smegmatis PafBC is involved in regulation of DNA damage response

B. Roschitzki, F. Imkamp, E. Weber-Ban, 2017, Scientific Reports.

Structural basis of enzyme encapsulation into a bacterial nanocompartment

S. Günther, D. Boehringer, N. Ban, 2008, Nature Structural &Molecular Biology.

Thermotolerance Requires Refolding of Aggregated Proteins by Substrate Translocation through the Central Pore of ClpB

Bernd Bukau, Axel Mogk, Zeljka Maglica, 2004, Cell.

Protein post-translational modifications in bacteria

B. Maček, K. Forchhammer, I. Mijakovic, 2019, Nature Reviews Microbiology.

An intrinsic degradation tag on the ClpA C-terminus regulates the balance of ClpAP complexes with different substrate specificity.

Zeljka Maglica, F. Striebel, E. Weber-Ban, 2008, Journal of molecular biology.

Pupylation as a signal for proteasomal degradation in bacteria.

F. Striebel, D. Özcelik, F. Imkamp, 2014, Biochimica et biophysica acta.

Solution structure and activation mechanism of ubiquitin-like small archaeal modifier proteins.

F. Damberger, M. Sutter, F. Allain, 2011, Journal of molecular biology.

Structural basis of prokaryotic ubiquitin-like protein engagement and translocation by the mycobacterial Mpa-proteasome complex

A. Jomaa, E. Weber-Ban, Mikhail Kavalchuk, 2022, Nature communications.

Deletion of dop in Mycobacterium smegmatis abolishes pupylation of protein substrates in vivo

Beat Amstutz, P. Sander, F. Striebel, 2010, Molecular microbiology.

A distinct structural region of the prokaryotic ubiquitin‐like protein (Pup) is recognized by the N‐terminal domain of the proteasomal ATPase Mpa

F. Damberger, M. Sutter, F. Allain, 2009, FEBS letters.

Chaperone rings in protein folding and degradation.

A. Horwich, D. Finley, E. Weber-Ban, 1999, Proceedings of the National Academy of Sciences of the United States of America.

ClpA mediates directional translocation of substrate proteins into the ClpP protease

A. Horwich, W. Fenton, B. Reid, 2001, Proceedings of the National Academy of Sciences of the United States of America.

Structures of prokaryotic ubiquitin-like protein Pup in complex with depupylase Dop reveal the mechanism of catalytic phosphate formation

N. Ban, M. Leibundgut, H. Cui, 2021, Nature Communications.

Depupylase Dop Requires Inorganic Phosphate in the Active Site for Catalysis*

N. Ban, M. Leibundgut, C. Vahlensieck, 2017, The Journal of Biological Chemistry.

The Mycobacterial LexA/RecA-Independent DNA Damage Response Is Controlled by PafBC and the Pup-Proteasome System.

F. Imkamp, E. Weber-Ban, A. U. Müller, 2018, Cell reports.

Pilus chaperones represent a new type of protein-folding catalyst

R. Glockshuber, U. Grauschopf, Thomas Spirig, 2004, Nature.

Targeted delivery of an ssrA-tagged substrate by the adaptor protein SspB to its cognate AAA+ protein ClpX.

B. Bukau, D. Dougan, E. Weber-Ban, 2003, Molecular cell.

Genome‐wide interaction screen for Mycobacterium tuberculosis ClpCP protease reveals toxin–antitoxin systems as a major substrate class

G. Taylor, Michal Ziemski, E. Weber-Ban, 2020, The FEBS journal.

Correction: The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1

E. Weber-Ban, Julia Leodolter, Jannis Warweg, 2015, PloS one.

The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1

Eilika Weber-Ban, Julia Leodolter, Jannis Warweg, 2015, PloS one.

FixK2, a key regulator in Bradyrhizobium japonicum, is a substrate for the protease ClpAP in vitro

H. Hennecke, S. Mesa, Zeljka Maglica, 2013, FEBS letters.

Controlled destruction: AAA+ ATPases in protein degradation from bacteria to eukaryotes.

F. Striebel, Wolfgang Kress, E. Weber-Ban, 2009, Current opinion in structural biology.

Cdc48-like protein of actinobacteria (Cpa) is a novel proteasome interactor in mycobacteria and related organisms

D. Veprintsev, C. Giese, A. Jomaa, 2018, eLife.

The pupylation pathway and its role in mycobacteria

J. Barandun, E. Weber-Ban, C. Delley, 2012, BMC Biology.

Characterization of a new AAA+ protein from archaea.

E. Weber-Ban, Heike Summer, R. Bruderer, 2006, Journal of structural biology.

The alternating power stroke of a 6-cylinder AAA protease chaperone engine.

Wolfgang Kress, E. Weber-Ban, 2009, Molecular cell.

An emerging class of nucleic acid-sensing regulators in bacteria: WYL domain-containing proteins.

L. Keller, E. Weber-Ban, 2023, Current opinion in microbiology.

ClpC2 protects mycobacteria against a natural antibiotic targeting ClpC1-dependent protein degradation

G. Taylor, C. Giese, H. Cui, 2023, Communications Biology.

Prokaryotic ubiquitin-like protein remains intrinsically disordered when covalently attached to proteasomal target proteins

F. Damberger, J. Barandun, F. Allain, 2017, BMC Structural Biology.

Both ATPase Domains of ClpA Are Critical for Processing of Stable Protein Structures

H. Mutschler, Wolfgang Kress, E. Weber-Ban, 2009, The Journal of Biological Chemistry.

Bacterial Proteasome Activator Bpa (Rv3780) Is a Novel Ring-Shaped Interactor of the Mycobacterial Proteasome

D. Boehringer, Michal Ziemski, E. Weber-Ban, 2014, PloS one.

Investigation of allosteric linkages in the regulation of tryptophan synthase: the roles of salt bridges and monovalent cations probed by site-directed mutation, optical spectroscopy, and kinetics.

U. Banik, M. Dunn, E. W. Miles, 2001, Biochemistry.

Mycobacterium smegmatis PafBC is involved in regulation of DNA damage response

B. Roschitzki, F. Imkamp, E. Weber-Ban, 2017, Scientific Reports.

Catching proteins for degradation

E. Weber-Ban, C. Schilling, 2023, Science.

Structural basis of enzyme encapsulation into a bacterial nanocompartment

K. Stetter, M. Sutter, M. Loessner, 2008, Nature Structural &Molecular Biology.

Electrostatic interactions guide substrate recognition of the prokaryotic ubiquitin-like protein ligase PafA

L. Keller, E. Weber-Ban, C. Delley, 2023, Nature communications.

In situ analysis of osmolyte mechanisms of proteome thermal stabilization

M. Pepelnjak, U. C. Palmiero, E. Weber-Ban, 2024, Nature chemical biology.