J
Justin Link
Researcher at Xavier University
Publications - 9
Citations - 331
Justin Link is an academic researcher from Xavier University. The author has contributed to research in topics: Cryptochrome & Flavin group. The author has an hindex of 7, co-authored 9 publications receiving 258 citations. Previous affiliations of Justin Link include Ohio State University.
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Journal ArticleDOI
Blue-light induced biosynthesis of ROS contributes to the signaling mechanism of Arabidopsis cryptochrome.
Mohamed A. El-Esawi,Louis-David Arthaut,Nathalie Jourdan,Alain d'Harlingue,Justin Link,Carlos F. Martino,Margaret Ahmad,Margaret Ahmad +7 more
TL;DR: It is shown by fluorescence imaging and microscopy that H202 and ROS accumulate in the plant nucleus after cryptochrome activation and this may lead to novel applications using blue light induced oxidative bursts to prime crop plants against the deleterious effects of environmental stresses and toxins.
Journal ArticleDOI
Magnetic sensitivity mediated by the Arabidopsis blue-light receptor cryptochrome occurs during flavin reoxidation in the dark
Marootpong Pooam,Louis-David Arthaut,Derek Burdick,Derek Burdick,Justin Link,Carlos F. Martino,Margaret Ahmad,Margaret Ahmad +7 more
TL;DR: Investigating the response of Arabidopsis cryptochrome-1 in vivo to a static magnetic field using both plant growth and light-dependent phosphorylation as an assay indicates that the magnetically sensitive reaction step in the Cryptochrome photocycle must occur during flavin reoxidation, and likely involves the formation of reactive oxygen species.
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Ultrafast proteinquake dynamics in cytochrome c.
TL;DR: The dynamics mainly occur at the local site, including ultrafast internal conversion in hundreds of femtoseconds, vibrational cooling on the similar picosecond time scale, and complete ground-state recovery in 10 ps, and no global conformation relaxation was observed.
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Cellular metabolites modulate in vivo signaling of Arabidopsis cryptochrome-1.
TL;DR: It is shown that in vivo modulation by metabolites in the cellular environment may play an important role in cryptochrome signaling, and possible effects on the conformation of the C-terminal domain to generate the biologically active conformational state are discussed.
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Ultrafast dynamics of resonance energy transfer in myoglobin: probing local conformation fluctuations.
TL;DR: Systematic characterization of resonance energy transfer between intrinsic tryptophan and the prosthetic heme group in myoglobin is reported in order to develop a novel energy-transfer pair as a molecular ruler in heme proteins to study local conformation fluctuations.