Eilika Weber-Ban

1968 -

educated at: University of California, Riverside

Eilika Weber-Ban (born 15 November 1968 in Karlsruhe) is a German biochemist. Her research considers protein degradation pathways. She was elected to the European Molecular Biology Organization in 2021. Source: Wikipedia (en)

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Articles 50

Date

Title

Authors

2021-12-01

Transcriptional control of mycobacterial DNA damage response by sigma adaptation

Andreas U Müller, Eva Kummer, Nenad Ban, Eilika Weber-Ban
2021-11-17

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

Andreas U Müller, Nenad Ban, Eilika Weber-Ban
2020-04-17

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

Michal Ziemski, Gabrielle Taylor, Eilika Weber-Ban
2019

The Bacterial Proteasome at the Core of Diverse Degradation Pathways

Eilika Weber-Ban
2019

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

Eilika Weber-Ban
2019-10-11

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

Andreas U Müller, Nenad Ban, Eilika Weber-Ban
2019-06-13

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

Bernd Bukau, Eilika Weber-Ban
2019-09-04

Protein post-translational modifications in bacteria

Boris Macek, Julie Hardouin, Eilika Weber-Ban, Christophe Grangeasse
2018-05-29

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

Eilika Weber-Ban, Michal Ziemski, Ahmad Jomaa, Dmitry B Veprintsev
2018-06-01

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

Eilika Weber-Ban, Andreas U Müller
2017-02-01

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

Fred F. Damberger, Jonas Barandun, Eilika Weber-Ban, Cyrille L. Delley
2017-05-03

Prokaryotic Ubiquitin-Like Protein and Its Ligase/Deligase Enyzmes

Eilika Weber-Ban, Andreas U Müller, Michal Ziemski, Cyrille L. Delley
2017-10-25

Mycobacterium smegmatis PafBC is involved in regulation of DNA damage response

Eilika Weber-Ban, Andreas U Müller
2017-01-24

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

Eilika Weber-Ban, Nenad Ban, Marcel Bolten
2016-11-09

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

Nenad Ban, Eilika Weber-Ban, Marcel Bolten, Cyrille L. Delley, Daniel Boehringer
2015-05-01

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

Julia Leodolter, Eilika Weber-Ban
2015-08-01

Pupylation-dependent and -independent proteasomal degradation in mycobacteria

Eilika Weber-Ban, Michal Ziemski
2014-01-01

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

Marcel Bolten, Eilika Weber-Ban, Michal Ziemski, Cyrille L. Delley, Daniel Boehringer
2014

Chaperone-Proteases of Mycobacteria

Julia Leodolter, Eilika Weber-Ban
2013-04-02

Pupylation as a signal for proteasomal degradation in bacteria

Dennis Özcelik, Eilika Weber-Ban
2013-05-08

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

Nenad Ban, Eilika Weber-Ban, Jonas Barandun, Cyrille L. Delley
2012-01-01

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

Dennis Özcelik, Jonas Barandun, Markus Sutter, Fred F. Damberger, Eilika Weber-Ban
2012-11-30

The pupylation pathway and its role in mycobacteria

Jonas Barandun, Eilika Weber-Ban, Cyrille L. Delley
2012-11-24

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

Željka Maglica, Eilika Weber-Ban, Socorro Mesa
2011-01-28

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

Markus Sutter, Frédéric H-T Allain, Eilika Weber-Ban, Fred F. Damberger
2011-12-30

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

Eilika Weber-Ban, Dennis Özcelik, Franziska M Heydenreich, Cyrille L. Delley
2010-08-27

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

Markus Sutter, Dennis Özcelik, Peter Sander, Eilika Weber-Ban
2010-03-04

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

Moritz Hunkeler, Eilika Weber-Ban
2010-04-28

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

Eilika Weber-Ban, Markus Sutter
2010-11-16

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

Michael Thommen, Eilika Weber-Ban
2009-09-15

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

Markus Sutter, Fred F. Damberger, Eilika Weber-Ban
2009-06-01

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

Markus Sutter, Eilika Weber-Ban

Human - wd:Q21258761

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