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Christina Brandstädter | Researchclopedia

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Christina Brandstädter

Justus-Liebig-Universität Gießen ORCID

24

Works

154

Citations

6

h-index

3

i10-index

Research Topics

Redox biology and oxidative stress Sulfur Compounds in Biology Crystallization and Solubility Studies

Affiliations

University of Giessen2016–2026

Top Works

Selective, Modular Probes for Thioredoxins Enabled by Rational Tuning of a Unique Disulfide Structure Motif

Jan G. Felber,Lukas Zeisel,et al.

202152 citations

X-ray Diffraction in Crystallography

Genomics, phytochemicals, and oxidative stress

Cyclic 5-membered disulfides are not selective substrates of thioredoxin reductase, but are opened nonspecifically

Jan G. Felber,Lena Poczka,et al.

202242 citations

Characterization of a small molecule inhibitor of disulfide reductases that induces oxidative stress and lethality in lung cancer cells

Fraser Johnson,John R. Ferrarone,et al.

202228 citations

Structural and Functional Characterization of Plasmodium falciparum Nicotinic Acid Mononucleotide Adenylyltransferase

Jochen Bathke,Karin Fritz‐Wolf,et al.

20169 citations

Low level of antioxidant capacity biomarkers but not target overexpression predicts vulnerability to ROS-inducing drugs

Jana Samarin,Piotr Fabrowski,et al.

20239 citations

Cyclic 5-Membered Disulfides Are Not Selective Substrates of Thioredoxin Reductase, but Are Opened Nonspecifically by Thiols

Jan G. Felber,Lena Poczka,et al.

20207 citations

The C-terminus of Sudan ebolavirus VP40 contains a functionally important CXnC motif, a target for redox modifications

Anke Werner,Martin Schauflinger,et al.

20234 citations

Selective, Modular Probes for Thioredoxins Enabled by Rational Tuning of a Unique Disulfide Structure Motif

Jan G. Felber,Lukas Zeisel,et al.

20211 citations

Cyclic 5-Membered Disulfides Are Not Selective Substrates of Thioredoxin Reductase, but Are Opened Nonspecifically

Jan G. Felber,Lena Poczka,et al.

20221 citations