Ursula Jakob

Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase.

Active site in RrmJ, a heat shock-induced methyltransferase.

The roles of the two zinc binding sites in DnaJ.

Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site.

Not every disulfide lasts forever: disulfide bond formation as a redox switch.

Identification of a redox-regulated chaperone network.

Activation of the redox-regulated chaperone Hsp33 by domain unfolding.

The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold.

Substrate binding analysis of the 23S rRNA methyltransferase RrmJ.

The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism.

Protein thiol modifications visualized in vivo.

Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33.

Beyond transcription--new mechanisms for the regulation of molecular chaperones.

Transarterial chemoembolization in the treatment of hepatoblastoma in children.

CoSMoS: Conserved Sequence Motif Search in the proteome.

XIAP Is a copper binding protein deregulated in Wilson's disease and other copper toxicosis disorders.

Global methods to monitor the thiol-disulfide state of proteins in vivo.

Zinc center as redox switch--new function for an old motif.

The redox-switch domain of Hsp33 functions as dual stress sensor.

Nitrosative stress treatment of E. coli targets distinct set of thiol-containing proteins.

Quantifying changes in the thiol redox proteome upon oxidative stress in vivo.

Special issue: redox regulation of protein folding. Preface.

Thiol-based redox switches in eukaryotic proteins.

Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding.

Redox-regulated chaperones.

Interplay of cellular cAMP levels, {sigma}S activity and oxidative stress resistance in Escherichia coli.

Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state.

Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates.

Protein refolding by pH-triggered chaperone binding and release.

Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone.

Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans.

Is overoxidation of peroxiredoxin physiologically significant?

Are zinc-finger domains of protein kinase C dynamic structures that unfold by lipid or redox activation?

The redoxome: Proteomic analysis of cellular redox networks.

Chlorinated phenols control the expression of the multidrug resistance efflux pump MexAB-OprM in Pseudomonas aeruginosa by interacting with NalC.

Genetic selection designed to stabilize proteins uncovers a chaperone called Spy.

Using quantitative redox proteomics to dissect the yeast redoxome.

E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly.

Hsp33 confers bleach resistance by protecting elongation factor Tu against oxidative degradation in Vibrio cholerae.

Order out of disorder: working cycle of an intrinsically unfolded chaperone.

Redox, haem and CO in enzymatic catalysis and regulation.

Quantitative in vivo redox sensors uncover oxidative stress as an early event in life.

Conditional disorder in chaperone action.

Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked.

Redox control: A black hole for oxidized glutathione.

Time line of redox events in aging postmitotic cells.

The roles of conditional disorder in redox proteins.

NemR is a bleach-sensing transcription factor.

Nonnative disulfide bond formation activates the σ32-dependent heat shock response in Escherichia coli.

Bacterial responses to reactive chlorine species.

Oxidant sensing by reversible disulfide bond formation.

The RclR protein is a reactive chlorine-specific transcription factor in Escherichia coli.

Conditionally and transiently disordered proteins: awakening cryptic disorder to regulate protein function.

Polyphosphate is a primordial chaperone.

Thiol-based redox switches.

Bile salts act as effective protein-unfolding agents and instigators of disulfide stress in vivo.

About the dangers, costs and benefits of living an aerobic lifestyle.

The protein targeting factor Get3 functions as ATP-independent chaperone under oxidative stress conditions.

The 'mitoflash' probe cpYFP does not respond to superoxide.

HdeB functions as an acid-protective chaperone in bacteria.

Oxidative stress protection by polyphosphate--new roles for an old player.

Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum.

Protein quality control under oxidative stress conditions.

Does the Transcription Factor NemR Use a Regulatory Sulfenamide Bond to Sense Bleach?

HdeB functions as an acid-protective chaperone in bacteria.

Janus-faced Sestrin2 controls ROS and mTOR signalling through two separate functional domains.

Protein unfolding as a switch from self-recognition to high-affinity client binding.

Do nucleic acids moonlight as molecular chaperones?

Polyphosphate: A Conserved Modifier of Amyloidogenic Processes.