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The Journal of Biological Chemistry|July 18, 2013
Oxidant sensing by reversible disulfide bond formationClaudia M Cremers, Ursula Jakob
The Journal of Biological Chemistry|February 9, 2010
Unfolding of metastable linker region is at the core of Hsp33 activation as a redox-regulated chaperoneClaudia M Cremers, Dana Reichmann, Jens Hausmann, et al.
Proceedings of the National Academy of Sciences of the United States of America|April 8, 2014
Bile salts act as effective protein-unfolding agents and instigators of disulfide stress in vivoClaudia M Cremers, Daniela Knoefler, Victor Vitvitsky, et al.
Cell|March 6, 2012
Order out of disorder: working cycle of an intrinsically unfolded chaperoneDana Reichmann, Ying Xu, Claudia M Cremers, et al.
Biophysical Journal|November 24, 2019
The Anti-Aggregation Holdase Hsp33 Promotes the Formation of Folded Protein StructuresFatemeh Moayed, Sergey Bezrukavnikov, Mohsin M Naqvi, et al.
Biochemical Society Transactions|August 12, 2014
About the dangers, costs and benefits of living an aerobic lifestyleDaniela Knoefler, Lars I O Leichert, Maike Thamsen, et al.
Antioxidants & Redox Signaling|November 12, 2010
Are zinc-finger domains of protein kinase C dynamic structures that unfold by lipid or redox activation?Feng Zhao, Marianne Ilbert, Ranjani Varadan, et al.
Molecular Cell|August 30, 2016
Polyphosphate: A Conserved Modifier of Amyloidogenic ProcessesClaudia M Cremers, Daniela Knoefler, Stephanie Gates, et al.
Antioxidants & Redox Signaling|September 19, 2003
Not every disulfide lasts forever: disulfide bond formation as a redox switchKatrin Linke, Ursula Jakob
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