Kristine Groth Kirkensgaard

ORCID: 0000-0003-2882-3597
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About
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Research Areas
  • Redox biology and oxidative stress
  • Insect and Pesticide Research
  • Mycotoxins in Agriculture and Food
  • Photosynthetic Processes and Mechanisms
  • Endoplasmic Reticulum Stress and Disease
  • Metal-Catalyzed Oxygenation Mechanisms
  • Polyamine Metabolism and Applications
  • Enzyme Structure and Function
  • Mass Spectrometry Techniques and Applications
  • Advanced Proteomics Techniques and Applications
  • Electron Spin Resonance Studies

Technical University of Denmark
2009-2013

Carlsberg Laboratory
2009-2013

Carlsberg Group (Denmark)
2013

Thioredoxins (Trxs) are protein disulfide reductases that regulate the intracellular redox environment and important for seed germination in plants. Trxs turn regulated by NADPH-dependent thioredoxin (NTRs), which provide reducing equivalents to Trx using NADPH recycle active form. Here, first crystal structure of a cereal NTR, HvNTR2 from Hordeum vulgare (barley), is presented, also monocot plant NTR. The was determined at 2.6 A resolution refined an R(cryst) 19.0% R(free) 23.8%. dimeric...

10.1107/s0907444909021817 article EN cc-by Acta Crystallographica Section D Biological Crystallography 2009-08-13

MINI REVIEW article Front. Plant Sci., 21 May 2013Sec. Physiology https://doi.org/10.3389/fpls.2013.00151

10.3389/fpls.2013.00151 article EN cc-by Frontiers in Plant Science 2013-01-01

The ubiquitous disulfide reductase thioredoxin (Trx) regulates several important biological processes such as seed germination in plants. Oxidized cytosolic Trx is regenerated by nicotinamide adenine dinucleotide phosphate (NADPH)-dependent (NTR) a multistep transfer of reducing equivalents from NADPH to via tightly NTR-bound flavin. Here, interactions between NTR and are predicted molecular modelling the barley NTR:Trx complex (HvNTR2:HvTrxh2) probed site directed mutagenesis. Enzyme...

10.1002/prot.24437 article EN Proteins Structure Function and Bioinformatics 2013-10-12
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