List of works - Eilika Weber-Ban

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

scientific journal article

Activity of the mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation

scientific article published on 30 December 2011

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

scientific article published on 26 September 2008

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

scientific article published on 4 May 2007

Bacterial proteasome activator bpa (rv3780) is a novel ring-shaped interactor of the mycobacterial proteasome

scientific journal article

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

scientific journal article

Both ATPase domains of ClpA are critical for processing of stable protein structures

scientific article published on 2 September 2009

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

scientific article

Chaperone rings in protein folding and degradation.

scientific article

Chaperone-Proteases of Mycobacteria

scientific article

Characterization of a new AAA+ protein from archaea

scientific article

Clp chaperone-proteases: structure and function.

scientific article published on 02 September 2009

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

scientific article published on 10 April 2009

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

scientific article

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

scientific journal article

Depupylase Dop Requires Inorganic Phosphate in the Active Site for Catalysis

scientific article published on 24 January 2017

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

scientific journal article

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

scientific article published on 24 November 2012

Genome-wide Interaction Screen for Mycobacterium tuberculosis ClpCP Protease Reveals Toxin-Antitoxin Systems as a Major Substrate Class

scientific article published on 17 April 2020

Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.

scientific article

Intersubunit cross-talk in pyridoxal 5'-phosphate synthase, coordinated by the C terminus of the synthase subunit

scientific article

Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated pup intermediate.

scientific article

Mycobacterium smegmatis PafBC is involved in regulation of DNA damage response

scientific article published on 25 October 2017

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

scientific article published in April 2009

Pilus chaperones represent a new type of protein-folding catalyst.

scientific article

Prokaryotic Ubiquitin-Like Protein and Its Ligase/Deligase Enyzmes

scientific article

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

scientific journal article

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

scientific article (publication date: February 2017)

Protein post-translational modifications in bacteria

scientific article published on 04 September 2019

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

article by Juerg Laederach et al published 2019 in PLOS ONE

Pupylation as a signal for proteasomal degradation in bacteria

scientific article

Pupylation-dependent and -independent proteasomal degradation in mycobacteria

scientific article published on August 2015

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

scientific article

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

scientific article published on 9 November 2016

Structural basis of enzyme encapsulation into a bacterial nanocompartment

scientific article

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

scientific article published on 11 October 2019

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

scientific article

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

scientific article published on 17 November 2021

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

scientific article published on 08 July 2009

Targeted Delivery of an ssrA-Tagged Substrate by the Adaptor Protein SspB to Its Cognate AAA+ Protein ClpX ⬇️

scientific article published on August 1, 2003

The Bacterial Proteasome at the Core of Diverse Degradation Pathways

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

scientific article published on 01 June 2018

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

scientific article published on May 2015

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

scientific article published in September 2009

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

scientific article

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

scientific journal article

The pupylation pathway and its role in mycobacteria ⬇️

scientific article published on November 30, 2012

Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.

scientific article

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

scientific article published on 13 June 2019

Transcriptional control of mycobacterial DNA damage response by sigma adaptation

scientific article published on 01 December 2021

List of works by Eilika Weber-Ban

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

Activity of the mycobacterial proteasomal ATPase Mpa is reversibly regulated by pupylation

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

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

Bacterial proteasome activator bpa (rv3780) is a novel ring-shaped interactor of the mycobacterial proteasome

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

Both ATPase domains of ClpA are critical for processing of stable protein structures

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

Chaperone rings in protein folding and degradation.

Chaperone-Proteases of Mycobacteria

Characterization of a new AAA+ protein from archaea

Clp chaperone-proteases: structure and function.

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

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

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

Depupylase Dop Requires Inorganic Phosphate in the Active Site for Catalysis

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

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

Genome-wide Interaction Screen for Mycobacterium tuberculosis ClpCP Protease Reveals Toxin-Antitoxin Systems as a Major Substrate Class

Global unfolding of a substrate protein by the Hsp100 chaperone ClpA.

Intersubunit cross-talk in pyridoxal 5'-phosphate synthase, coordinated by the C terminus of the synthase subunit

Mycobacterial ubiquitin-like protein ligase PafA follows a two-step reaction pathway with a phosphorylated pup intermediate.

Mycobacterium smegmatis PafBC is involved in regulation of DNA damage response

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

Pilus chaperones represent a new type of protein-folding catalyst.

Prokaryotic Ubiquitin-Like Protein and Its Ligase/Deligase Enyzmes

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

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

Protein post-translational modifications in bacteria

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

Pupylation as a signal for proteasomal degradation in bacteria

Pupylation-dependent and -independent proteasomal degradation in mycobacteria

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

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

Structural basis of enzyme encapsulation into a bacterial nanocompartment

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

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

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

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

Targeted Delivery of an ssrA-Tagged Substrate by the Adaptor Protein SspB to Its Cognate AAA+ Protein ClpX ⬇️

The Bacterial Proteasome at the Core of Diverse Degradation Pathways

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

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

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

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

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

The pupylation pathway and its role in mycobacteria ⬇️

Thermotolerance requires refolding of aggregated proteins by substrate translocation through the central pore of ClpB.

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

Transcriptional control of mycobacterial DNA damage response by sigma adaptation