Astrid Grudziecki

TL;DR: The structure of a mammalian cryptochrome1 protein may catalyze the development of CRY chemical probes and the design of therapeutic metabolic modulators.

TL;DR: The crystal structure of a complex comprising the photolyase homology region of mouse CRY1 (mCRY1) and a C-terminal mouse PER2 (mPER2) fragment is determined, providing evidence that mCRy1/mper2 complex formation is modulated by an interplay of zinc binding and mCRY 1 disulfide bond formation, which may be influenced by the redox state of the cell.

TL;DR: Structural and quantitative differences are revealed between the homodimeric interactions of the three mouse PERIOD homologues, which are likely to contribute to their distinct clock functions.

TL;DR: Despite the extreme variability characterizing the Antarctic seasonal day length, the conserved light mediated degradation of the photoreceptor EsCRY1 suggests a persisting pivotal role of light as a Zeitgeber.

TL;DR: Genomic alterations at the Fbxl3 locus occurred with very high efficiency and specificity at both alleles, resulting in insertions and deletions that led to premature stop codons and hence FBXL3 knockout.