Paper Roundup – June 2016

  • Quantitative comparison of fluorescent proteins. A great resource with measurements of photobleaching, brightness, and monomericness for a large number of fluorescent proteins [1]
  • Metalenses for focusing visible light with an NA of 0.8 [2]
  • A cyan-excitable orange-emitting fluorescent protein [3]
  • A mutant of UnaG that is nonfluorescent and destabilizing in the absence of ligand, and fluorescent and stable in the presence of ligand [4]
  • Spectral imaging for single particle tracking of motor proteins [5]
  • A fluorescent reporter for beta-galactosidase that can be used for cell and animal imaging [6]
  • All-optical electrophysiology [7]
  • A review of small molecule dyes for super-resolution imaging [8]
  • An improved protocol for expansion microscopy [9]
  • A review of clearing techniques [10]
  • A generative model for testing spatial distributions of puncta within the cell [11]
  • Mammalian protein tagging with CRISPR/Cas9 and split GFP for simple, scalable tagging of endogenous mammalian proteins [12]
  • Miniature light sheet generator modules [13]
  • An electrically-tunable lens to move the waist of a light sheet synchronously with the virtual detection slit on a sCMOS camera to make narrow light sheets over large areas [14]
  • A review of cyanine photobleaching mechanisms and their applications [15]

References

  1. P.J. Cranfill, B.R. Sell, M.A. Baird, J.R. Allen, Z. Lavagnino, H.M. de Gruiter, G. Kremers, M.W. Davidson, A. Ustione, and D.W. Piston, "Quantitative assessment of fluorescent proteins", Nature Methods, vol. 13, pp. 557-562, 2016. http://dx.doi.org/10.1038/nmeth.3891
  2. M. Khorasaninejad, W.T. Chen, R.C. Devlin, J. Oh, A.Y. Zhu, and F. Capasso, "Metalenses at visible wavelengths: Diffraction-limited focusing and subwavelength resolution imaging", Science, vol. 352, pp. 1190-1194, 2016. http://dx.doi.org/10.1126/science.aaf6644
  3. J. Chu, Y. Oh, A. Sens, N. Ataie, H. Dana, J.J. Macklin, T. Laviv, E.S. Welf, K.M. Dean, F. Zhang, B.B. Kim, C.T. Tang, M. Hu, M.A. Baird, M.W. Davidson, M.A. Kay, R. Fiolka, R. Yasuda, D.S. Kim, H. Ng, and M.Z. Lin, "A bright cyan-excitable orange fluorescent protein facilitates dual-emission microscopy and enhances bioluminescence imaging in vivo", Nature Biotechnology, vol. 34, pp. 760-767, 2016. http://dx.doi.org/10.1038/nbt.3550
  4. R. Navarro, L. Chen, R. Rakhit, and T.J. Wandless, "A Novel Destabilizing Domain Based on a Small-Molecule Dependent Fluorophore", ACS Chemical Biology, vol. 11, pp. 2101-2104, 2016. http://dx.doi.org/10.1021/acschembio.6b00234
  5. T. Kakizuka, K. Ikezaki, J. Kaneshiro, H. Fujita, T.M. Watanabe, and T. Ichimura, "Simultaneous nano-tracking of multiple motor proteins via spectral discrimination of quantum dots", Biomedical Optics Express, vol. 7, pp. 2475, 2016. http://dx.doi.org/10.1364/BOE.7.002475
  6. K. Gu, Y. Xu, H. Li, Z. Guo, S. Zhu, S. Zhu, P. Shi, T.D. James, H. Tian, and W. Zhu, "Real-Time Tracking and In Vivo Visualization of β-Galactosidase Activity in Colorectal Tumor with a Ratiometric Near-Infrared Fluorescent Probe", Journal of the American Chemical Society, vol. 138, pp. 5334-5340, 2016. http://dx.doi.org/10.1021/jacs.6b01705
  7. H. Zhang, E. Reichert, and A.E. Cohen, "Optical electrophysiology for probing function and pharmacology of voltage-gated ion channels", eLife, vol. 5, 2016. http://dx.doi.org/10.7554/eLife.15202
  8. Z. Yang, A. Sharma, J. Qi, X. Peng, D.Y. Lee, R. Hu, D. Lin, J. Qu, and J.S. Kim, "Super-resolution fluorescent materials: an insight into design and bioimaging applications", Chemical Society Reviews, vol. 45, pp. 4651-4667, 2016. http://dx.doi.org/10.1039/C5CS00875A
  9. T.J. Chozinski, A.R. Halpern, H. Okawa, H. Kim, G.J. Tremel, R.O.L. Wong, and J.C. Vaughan, "Expansion microscopy with conventional antibodies and fluorescent proteins", Nature Methods, vol. 13, pp. 485-488, 2016. http://dx.doi.org/10.1038/nmeth.3833
  10. J. Seo, M. Choe, and S. Kim, "Clearing and Labeling Techniques for Large-Scale Biological Tissues", Molecules and Cells, vol. 39, pp. 439-446, 2016. http://dx.doi.org/10.14348/molcells.2016.0088
  11. Y. Li, T.D. Majarian, A.W. Naik, G.R. Johnson, and R.F. Murphy, "Point process models for localization and interdependence of punctate cellular structures", Cytometry Part A, vol. 89, pp. 633-643, 2016. http://dx.doi.org/10.1002/cyto.a.22873
  12. M.D. Leonetti, S. Sekine, D. Kamiyama, J.S. Weissman, and B. Huang, "A scalable strategy for high-throughput GFP tagging of endogenous human proteins", Proceedings of the National Academy of Sciences, vol. 113, pp. E3501-E3508, 2016. http://dx.doi.org/10.1073/pnas.1606731113
  13. T. BRUNS, M. BAUER, S. BRUNS, H. MEYER, D. KUBIN, and H. SCHNECKENBURGER, "Miniaturized modules for light sheet microscopy with low chromatic aberration", Journal of Microscopy, vol. 264, pp. 261-267, 2016. http://dx.doi.org/10.1111/jmi.12439
  14. P.N. Hedde, and E. Gratton, "Selective plane illumination microscopy with a light sheet of uniform thickness formed by an electrically tunable lens", Microscopy Research and Technique, vol. 81, pp. 924-928, 2016. http://dx.doi.org/10.1002/jemt.22707
  15. A.P. Gorka, and M.J. Schnermann, "Harnessing cyanine photooxidation: from slowing photobleaching to near-IR uncaging", Current Opinion in Chemical Biology, vol. 33, pp. 117-125, 2016. http://dx.doi.org/10.1016/j.cbpa.2016.05.022