PubRank

Ursula Jakob

Author PubWeight™ 61.64‹?›

Top papers

Rank Title Journal Year PubWeight™‹?›
1 Quantifying changes in the thiol redox proteome upon oxidative stress in vivo. Proc Natl Acad Sci U S A 2008 2.65
2 Protein thiol modifications visualized in vivo. PLoS Biol 2004 2.13
3 Thiol-based redox switches in eukaryotic proteins. Antioxid Redox Signal 2009 1.97
4 Order out of disorder: working cycle of an intrinsically unfolded chaperone. Cell 2012 1.89
5 The redox-switch domain of Hsp33 functions as dual stress sensor. Nat Struct Mol Biol 2007 1.69
6 Severe oxidative stress causes inactivation of DnaK and activation of the redox-regulated chaperone Hsp33. Mol Cell 2005 1.60
7 Overexpression of two different GTPases rescues a null mutation in a heat-induced rRNA methyltransferase. J Bacteriol 2002 1.56
8 Genetic selection designed to stabilize proteins uncovers a chaperone called Spy. Nat Struct Mol Biol 2011 1.52
9 XIAP Is a copper binding protein deregulated in Wilson's disease and other copper toxicosis disorders. Mol Cell 2006 1.50
10 Identification of a redox-regulated chaperone network. EMBO J 2003 1.46
11 Structural plasticity of an acid-activated chaperone allows promiscuous substrate binding. Proc Natl Acad Sci U S A 2009 1.46
12 Active site in RrmJ, a heat shock-induced methyltransferase. J Biol Chem 2002 1.45
13 Not every disulfide lasts forever: disulfide bond formation as a redox switch. Antioxid Redox Signal 2003 1.37
14 Protein refolding by pH-triggered chaperone binding and release. Proc Natl Acad Sci U S A 2009 1.35
15 Global methods to monitor the thiol-disulfide state of proteins in vivo. Antioxid Redox Signal 2006 1.35
16 Quantitative in vivo redox sensors uncover oxidative stress as an early event in life. Mol Cell 2012 1.34
17 The roles of the two zinc binding sites in DnaJ. J Biol Chem 2003 1.33
18 Activation of the redox-regulated chaperone Hsp33 by domain unfolding. J Biol Chem 2004 1.23
19 Conditional disorder in chaperone action. Trends Biochem Sci 2012 1.20
20 Redox-regulated chaperones. Biochemistry 2009 1.19
21 Oxidant sensing by reversible disulfide bond formation. J Biol Chem 2013 1.18
22 Heme regulatory motifs in heme oxygenase-2 form a thiol/disulfide redox switch that responds to the cellular redox state. J Biol Chem 2009 1.18
23 Effects of oxidative stress on behavior, physiology, and the redox thiol proteome of Caenorhabditis elegans. Antioxid Redox Signal 2010 1.16
24 Bacterial responses to reactive chlorine species. Annu Rev Microbiol 2013 1.13
25 Beyond transcription--new mechanisms for the regulation of molecular chaperones. Crit Rev Biochem Mol Biol 2005 1.13
26 Time line of redox events in aging postmitotic cells. Elife 2013 1.10
27 NemR is a bleach-sensing transcription factor. J Biol Chem 2013 1.09
28 Nitrosative stress treatment of E. coli targets distinct set of thiol-containing proteins. Mol Microbiol 2007 1.02
29 Zinc center as redox switch--new function for an old motif. Antioxid Redox Signal 2006 0.99
30 Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperone. J Biol Chem 2010 0.97
31 Thioredoxin 2, an oxidative stress-induced protein, contains a high affinity zinc binding site. J Biol Chem 2003 0.97
32 Using quantitative redox proteomics to dissect the yeast redoxome. J Biol Chem 2011 0.96
33 Get3 is a holdase chaperone and moves to deposition sites for aggregated proteins when membrane targeting is blocked. J Cell Sci 2012 0.95
34 The redoxome: Proteomic analysis of cellular redox networks. Curr Opin Chem Biol 2010 0.95
35 Interplay of cellular cAMP levels, {sigma}S activity and oxidative stress resistance in Escherichia coli. Microbiology 2009 0.94
36 The crystal structure of the reduced, Zn2+-bound form of the B. subtilis Hsp33 chaperone and its implications for the activation mechanism. Structure 2004 0.94
37 Is overoxidation of peroxiredoxin physiologically significant? Antioxid Redox Signal 2010 0.89
38 Substrate binding analysis of the 23S rRNA methyltransferase RrmJ. J Bacteriol 2004 0.89
39 E. coli chaperones DnaK, Hsp33 and Spy inhibit bacterial functional amyloid assembly. Prion 2011 0.87
40 The RclR protein is a reactive chlorine-specific transcription factor in Escherichia coli. J Biol Chem 2013 0.86
41 The zinc-dependent redox switch domain of the chaperone Hsp33 has a novel fold. J Mol Biol 2004 0.84
42 Hsp33 confers bleach resistance by protecting elongation factor Tu against oxidative degradation in Vibrio cholerae. Mol Microbiol 2012 0.84
43 Special issue: redox regulation of protein folding. Preface. Biochim Biophys Acta 2008 0.84
44 Thermodynamic analysis of a molecular chaperone binding to unfolded protein substrates. Biochemistry 2010 0.83
45 Redox, haem and CO in enzymatic catalysis and regulation. Biochem Soc Trans 2012 0.82
46 Bile salts act as effective protein-unfolding agents and instigators of disulfide stress in vivo. Proc Natl Acad Sci U S A 2014 0.81
47 Nonnative disulfide bond formation activates the σ32-dependent heat shock response in Escherichia coli. J Bacteriol 2013 0.80
48 Chlorinated phenols control the expression of the multidrug resistance efflux pump MexAB-OprM in Pseudomonas aeruginosa by interacting with NalC. Mol Microbiol 2011 0.80
49 CoSMoS: Conserved Sequence Motif Search in the proteome. BMC Bioinformatics 2006 0.79
50 Are zinc-finger domains of protein kinase C dynamic structures that unfold by lipid or redox activation? Antioxid Redox Signal 2011 0.79
51 Transarterial chemoembolization in the treatment of hepatoblastoma in children. Eur Radiol 2005 0.78
52 The roles of conditional disorder in redox proteins. Curr Opin Struct Biol 2013 0.77
53 About the dangers, costs and benefits of living an aerobic lifestyle. Biochem Soc Trans 2014 0.76
54 Redox control: A black hole for oxidized glutathione. Nat Chem Biol 2013 0.76
55 HdeB functions as an acid-protective chaperone in bacteria. J Biol Chem 2015 0.75