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Results: 6,121
Number of items: 6,121
  • van Velzen, E. J. J., Westerhuis, J. A., Grün, C. H., Jacobs, D. M., Eilers, P. H. C., Mulder, T. P., Foltz, M., Garczarek, U., Kemperman, R., Vaughan, E. E., van Duynhoven, J. P. M., & Smilde, A. K. (2014). Population-based nutrikinetic modeling of polyphenol exposure. Metabolomics, 10(6), 1059-1073. https://doi.org/10.1007/s11306-014-0645-y
  • Schouten, M., De Luca, G. M. R., Alatriste González, D. K., de Jong, B. E., Timmermans, W., Xiong, H., Krugers, H., Manders, E. M. M., & Fitzsimons, C. P. (2014). Imaging dendritic spines of rat primary hippocampal neurons using structured illumination microscopy. Journal of Visualized Experiments, 87, Article e51276. https://doi.org/10.3791/51276
  • Joosen, L., Hink, M. A., Gadella, T. W. J., & Goedhart, J. (2014). Effect of fixation procedures on the fluorescence lifetimes of Aequorea victoria derived fluorescent proteins. Journal of Microscopy, 256(3), 166-176. https://doi.org/10.1111/jmi.12168
  • Hamers, D., van Voorst Vader, L., Borst, J. W., & Goedhart, J. (2014). Development of FRET biosensors for mammalian and plant systems. Protoplasma, 251(2), 333-347. https://doi.org/10.1007/s00709-013-0590-z
  • Goedhart, J., Hink, M. A., & Jalink, K. (2014). An introduction to fluorescence imaging techniques geared towards biosensor applications. In J. Zhang, Q. Ni, & R. H. Newman (Eds.), Fluorescent protein-based biosensors: methods and protocols (pp. 17-28). (Methods in Molecular Biology; Vol. 1071). Humana Press. https://doi.org/10.1007/978-1-62703-622-1_2
  • Ingaramo, M., York, A. G., Hoogendoorn, E., Postma, M., Shroff, H., & Patterson, G. H. (2014). Richardson-Lucy deconvolution as a general tool for combining images with complementary strengths. ChemPhysChem, 15(4), 794-800. https://doi.org/10.1002/cphc.201300831
  • Jezierska, J., Goedhart, J., Kampinga, H. H., Reits, E. A., & Verbeek, D. S. (2014). SCA14 mutation V138E leads to partly unfolded PKCγ associated with an exposed C-terminus, altered kinetics, phosphorylation and enhanced insolubilization. Journal of neurochemistry, 128(5), 741-751. https://doi.org/10.1111/jnc.12491
  • Schipper-Krom, S., Juenemann, K., Jansen, A. H., Wiemhoefer, A., van den Nieuwendijk, R., Smith, D. L., Hink, M. A., Bates, G. P., Overkleeft, H., Ovaa, H., & Reits, E. (2014). Dynamic recruitment of active proteasomes into polyglutamine initiated inclusion bodies. FEBS Letters, 588(1), 151-159. https://doi.org/10.1016/j.febslet.2013.11.023
  • Munnik, T. (2014). PI-PLC: Phosphoinositide-Phospholipase C in Plant Signaling. In X. Wang (Ed.), Phospholipases in plant signaling (pp. 27-54). (Signaling and communication in plants; No. 20). Springer. https://doi.org/10.1007/978-3-642-42011-5_2
  • Wang, Q., Verweij, E. W. E., Krugers, H. J., Joels, M., Swaab, D. F., & Lucassen, P. J. (2014). Distribution of the glucocorticoid receptor in the human amygdala; changes in mood disorder patients. Brain Structure and Function, 219(5), 1615-1626. https://doi.org/10.1007/s00429-013-0589-4
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