Ursula Jakob

Ursula Jakob

Department of Molecular, University of Michigan

Affiliated withUniversity of Michigan

Research Area

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JoVE Journal Publications

ArticleTotal : 1
Year
Detection of the pH-dependent Activity of <em>Escherichia coli</em> Chaperone HdeB <em>In Vitro</em> and <em>In Vivo</em>
Publication title
2016

Other Publications

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

Journal of bacteriology| PubMed ID: 11976298

2002
Active site in RrmJ, a heat shock-induced methyltransferase.

The Journal of biological chemistry| PubMed ID: 12181314

2002
The roles of the two zinc binding sites in DnaJ.

The Journal of biological chemistry| PubMed ID: 12941935

2003
2003
2003
Identification of a redox-regulated chaperone network.

The EMBO journal| PubMed ID: 14685279

2004
Activation of the redox-regulated chaperone Hsp33 by domain unfolding.

The Journal of biological chemistry| PubMed ID: 15023991

2004
2004
Substrate binding analysis of the 23S rRNA methyltransferase RrmJ.

Journal of bacteriology| PubMed ID: 15375145

2004
2004
Protein thiol modifications visualized in vivo.

PLoS biology| PubMed ID: 15502869

2004
2005
Beyond transcription--new mechanisms for the regulation of molecular chaperones.

Critical reviews in biochemistry and molecular biology| PubMed ID: 15763707

2004
2006
CoSMoS: Conserved Sequence Motif Search in the proteome.

BMC bioinformatics| PubMed ID: 16433915

2006
2006
Global methods to monitor the thiol-disulfide state of proteins in vivo.

Antioxidants & redox signaling| PubMed ID: 16771668

2006
Zinc center as redox switch--new function for an old motif.

Antioxidants & redox signaling| PubMed ID: 16771674

2006
The redox-switch domain of Hsp33 functions as dual stress sensor.

Nature structural & molecular biology| PubMed ID: 17515905

2007
2007
Quantifying changes in the thiol redox proteome upon oxidative stress in vivo.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 18287020

2008
Special issue: redox regulation of protein folding. Preface.

Biochimica et biophysica acta| PubMed ID: 18395585

2008
Thiol-based redox switches in eukaryotic proteins.

Antioxidants & redox signaling| PubMed ID: 18999917

2009
Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 19321422

2009
Redox-regulated chaperones.

Biochemistry| PubMed ID: 19368357

2009
2009
2009
2010
Protein refolding by pH-triggered chaperone binding and release.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 20080625

2010
2010
2011
Is overoxidation of peroxiredoxin physiologically significant?

Antioxidants & redox signaling| PubMed ID: 20964547

2011
2011
The redoxome: Proteomic analysis of cellular redox networks.

Current opinion in chemical biology| PubMed ID: 21130023

2011
2011
Genetic selection designed to stabilize proteins uncovers a chaperone called Spy.

Nature structural & molecular biology| PubMed ID: 21317898

2011
Using quantitative redox proteomics to dissect the yeast redoxome.

The Journal of biological chemistry| PubMed ID: 21976664

2011
2011
2012
2012
Redox, haem and CO in enzymatic catalysis and regulation.

Biochemical Society transactions| PubMed ID: 22616859

2012
2012
Conditional disorder in chaperone action.

Trends in biochemical sciences| PubMed ID: 23018052

2012
2013
Redox control: A black hole for oxidized glutathione.

Nature chemical biology| PubMed ID: 23334544

2013
2013
The roles of conditional disorder in redox proteins.

Current opinion in structural biology| PubMed ID: 23477949

2013
NemR is a bleach-sensing transcription factor.

The Journal of biological chemistry| PubMed ID: 23536188

2013
2013
Bacterial responses to reactive chlorine species.

Annual review of microbiology| PubMed ID: 23768204

2013
Oxidant sensing by reversible disulfide bond formation.

The Journal of biological chemistry| PubMed ID: 23861395

2013
2013
2014
Polyphosphate is a primordial chaperone.

Molecular cell| PubMed ID: 24560923

2014
Thiol-based redox switches.

Biochimica et biophysica acta| PubMed ID: 24657586

2014
Bile salts act as effective protein-unfolding agents and instigators of disulfide stress in vivo.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 24706920

2014
About the dangers, costs and benefits of living an aerobic lifestyle.

Biochemical Society transactions| PubMed ID: 25109979

2014
2014
2014
HdeB functions as an acid-protective chaperone in bacteria.

The Journal of biological chemistry| PubMed ID: 25391835

2015
Oxidative stress protection by polyphosphate--new roles for an old player.

Current opinion in microbiology| PubMed ID: 25589044

2015
Mitochondrial peroxiredoxin functions as crucial chaperone reservoir in Leishmania infantum.

Proceedings of the National Academy of Sciences of the United States of America| PubMed ID: 25646478

2015
Protein quality control under oxidative stress conditions.

Journal of molecular biology| PubMed ID: 25698115

2015
2015
HdeB functions as an acid-protective chaperone in bacteria.

The Journal of biological chemistry| PubMed ID: 25888567

2015
2015
2016
Do nucleic acids moonlight as molecular chaperones?

Nucleic acids research| PubMed ID: 27105849

2016
2016