Michael Moser
University of Freiburg
25 Papers
389 Citations
Michael Moser is an academic researcher from University of Freiburg. The author has contributed to research in topics: Signal peptide & Twin-arginine translocation pathway. The author has an hindex of 21, co-authored 25 publications. Previous affiliations of Michael Moser include Iwate University & University of Washington.
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Papers
Signal recognition particle-dependent protein targeting, universal to all kingdoms of life.
TL;DR: SRP-dependent protein targeting in bacteria and chloroplasts slightly deviate from the canonical mechanism found in eukaryotes, but the preferential substrates of SRP possess especially hydrophobic signal sequences.
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Ca2+-calmodulin promotes survival of pheromone-induced growth arrest by activation of calcineurin and ca2+-calmodulin-dependent protein kinase
TL;DR: Two observations indicate that activation of the Ca2+-calmodulin-dependent protein phosphatase calcineurin contributes to survival of pheromone-induced arrest, thus revealing a new function for this enzyme.
108
WRN mutations in Werner syndrome.
TL;DR: The spectrum of WS‐associated WRN mutations, the organization and potential functions of the WRN protein, and potential mechanistic links between the loss of WRN function and pathogenesis of the WS clinical and cellular phenotypes are reviewed.
95
Calmodulin localizes to the spindle pole body of Schizosaccharomyces pombe and performs an essential function in chromosome segregation
TL;DR: The observed spindle and chromosome segregation defects suggest that calmodulin performs an essential role during mitosis at the fission yeast SPB.
94
WRN helicase expression in Werner syndrome cell lines.
Michael Moser,Ashwini S. Kamath-Loeb,Jessica E. Jacob,Samuel E. Bennett,Junko Oshima,Raymond J. Monnat +5 more
TL;DR: The results indicate that most WRN mutations result in functionally equivalent null alleles, that WRN heterozygote effects may result from haploinsufficiency and that successful modeling of WRN pathogenesis in the mouse or in other model systems will require the use ofWRN mutations that eliminate WRN protein expression.
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