Lista de obras - Eilika Weber-Ban - Dominio Público Uruguay

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

artículo científico publicado en 2011

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

artículo científico publicado en 2008

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

artículo científico publicado en 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

artículo científico publicado en 2009

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

artículo científico publicado en 2018

Chaperone rings in protein folding and degradation.

artículo científico publicado en 1999

Chaperone-Proteases of Mycobacteria

artículo científico publicado en 2014

Characterization of a new AAA+ protein from archaea

artículo científico publicado en 2006

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

artículo científico publicado en 2013

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

artículo científico publicado en 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.

artículo científico publicado en 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.

artículo científico publicado en 1999

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

artículo científico publicado en 2008

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

artículo científico publicado en 2010

Mycobacterium smegmatis PafBC is involved in regulation of DNA damage response

artículo científico publicado en 2017

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

artículo científico publicado en 2009

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

artículo científico publicado en 2004

Prokaryotic Ubiquitin-Like Protein and Its Ligase/Deligase Enyzmes

artículo científico publicado en 2017

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

artículo científico publicado en 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

artículo científico publicado en 2014

Pupylation-dependent and -independent proteasomal degradation in mycobacteria

artículo científico

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

artículo científico publicado en 2011

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

artículo científico publicado en 2016

Structural basis of enzyme encapsulation into a bacterial nanocompartment

artículo científico publicado en 2008

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

artículo científico publicado en 2019

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

artículo científico publicado en 2012

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

artículo científico publicado en 2021

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

artículo científico publicado en 2009

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

artículo científico publicado el 1 de agosto de 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

artículo científico publicado en 2018

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

artículo científico publicado en 2015

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

artículo científico publicado en 2009

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

artículo científico publicado en 2008

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 ⬇️

artículo científico publicado el 30 de noviembre de 2012

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

artículo científico publicado en 2004

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

artículo científico publicado en 2019

Transcriptional control of mycobacterial DNA damage response by sigma adaptation

artículo científico publicado en 2021

Lista de obras de 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