Antikörper-freie Zellfärbung (SNAP-tag)

Publikationen

Reviews

Lukinavičius, G. et al. (2015) “Fluorescent labeling of SNAP-tagged proteins in cells” Methods Mol. Biol. 1266, 107-118.Corrêa Jr., I. R. (2015) “Considerations and protocols for the synthesis of custom protein labeling probes” Methods Mol. Biol. 1266, 55-79.Corrêa Jr., I. R. (2014) “Live-cell reporters for fluorescence imaging” Curr. Opin. Chem. Biol. 20, 36-45.

STEDGuzmán, C. et al. (2014) “The efficacy of Raf kinase recruitment to the GTPase H-ras depends on H-ras membrane conformer specific nanoclustering” J. Biol. Chem. 289, 9519-9533.Stagge, F. et al. (2013) “Snap-, CLIP- and Halo-Tag Labelling of Budding Yeast Cells” PLoS One 8(10): e78745.Lukinavičius, G. et al. (2013) “Selective Chemical Crosslinking Reveals a Cep57-Cep63-Cep152 Centrosomal Complex” Curr. Biol. 23, 265-270.Lukinavičius, G. et al. (2013) “A near-infrared fluorophore for live-cell super-resolution microscopy of cellular proteins” Nat. Chem. 5, 132-139.Pellett P. A. et al. (2011) “Two-color STED microscopy in living cells.” Biomed. Opt. Expr. 2, 2364-2371.Testa I. et al. (2010) “Multicolor Fluorescence Nanoscopy in Fixed and Living Cells by Exciting Conventional Fluorophores with a Single Wavelength” Biophys. J. 99, 2686-94.Hein B. et al. (2010) “Stimulated Emission Depletion Nanoscopy of Living Cells Using SNAP-Tag Fusion Proteins.” Biophys. J. 98, 158–163.

STORMLiu, Z. et al. (2014) “Super-resolution imaging and tracking of protein-protein interactions in sub-diffraction cellular space” Nat. Commun. 5, 4443.Perkovic, M. et al. (2014) “Correlative Light- and Electron Microscopy with chemical tags” J. Struct. Biol. 186, 205-213.Carlini, L. et al. (2014) “Reduced Dyes Enhance Single-Molecule Localization Density for Live Superresolution Imaging” ChemPhysChem 15, 750-755.Sateriale, A. et al. (2013) “SNAP-Tag Technology Optimized for Use in Entamoeba histolytica” PLoS One 8(12), e83997.Lukinavičius, G. et al. (2013) “A near-infrared fluorophore for live-cell super-resolution microscopy of cellular proteins” Nat. Chem. 5, 132-139.Malkusch, S. et al. (2013) “Single-molecule coordinate-based analysis of the morphology of HIV-1 assembly sites with near-molecular spatial resolution” Histochem. Cell Biol. 139, 173-179.van de Linde, S. et al. (2011) “Direct stochastic optical reconstruction microscopy with standard fluorescent probes” Nat. Protoc. 6, 991-1009.Eckhardt M. et al. (2011) “A SNAP-Tagged Derivative of HIV-1-A Versatile Tool to Study Virus-Cell Interactions.” PLoS One 6(7), e22007.Jones S. A. et al. (2011) “Fast, three-dimensional super-resolution imaging of live cells.” Nat. Methods 8, 499-505.Klein T. et al. (2011) “Live-cell dSTORM with SNAP-tag fusion proteins.” Nat. Methods 8, 7-9.Dellagiacoma C. et al. (2010) “Targeted Photoswitchable Probe for Nanoscopy of Biological Structures” ChemBioChem 11, 1361–1363.

PALMBenke, A. et al. (2012) “Multicolor Single Molecule Tracking of Stochastically Active Synthetic Dyes” Nano Lett. 12, 2619-2624.Banala, S. et al. (2012) “A caged, localizable rhodamine for superresolution microscopy” ACS Chem. Biol. 7, 289-293

RLS-SRMZhao, Z. W. et al. (2014) “Spatial organization of RNA polymerase II inside a mammalian cell nucleus revealed by reflected light-sheet superresolution microscopy” Proc. Natl. Acad. Sci. USA 111, 681-686.

Tissue and Animal Imaging:

Yang, G. et al. (2015) “Genetic targeting of chemical indicators in vivo” Nat. Methods 12, 137-139.Kohl, J. et al. (2014) “Ultrafast tissue staining with chemical tags” Proc. Natl. Acad. Sci. USA 111, E3805-E3814.Ivanova, A. et al. (2013) “Age-dependent labeling and imaging of insulin secretory granules” Diabetes 62, 3687-3696.Gong, H. et al. (2012) “Near-Infrared Fluorescence Imaging of Mammalian Cells and Xenograft Tumors with SNAP-Tag” PLoS ONE 7(3): e34003.Bojkowska K. et al. (2011) “Measuring in vivo protein half-life.” Chem. Biol. 18, 805-815.

Cell-Surface Protein Labeling and Internalization Analysis:

Bitsikas, V. et al. (2014) “Clathrin-independent pathways do not contribute significantly to endocytic flux” eLife 3, e03970.Jaensch, N. et al. (2014) “Stable Cell Surface Expression of GPI-Anchored Proteins, but not Intracellular Transport, Depends on their Fatty Acid Structure” Traffic 15, 1305-1329.Cole, N. B. and Donaldson, J. G. (2012) “Releasable SNAP-tag Probes for Studying Endocytosis and Recycling” ACS Chem. Biol. 7, 464-469.

Pulse-Chase Analysis:

Rošić, S. et al. (2014) “Repetitive centromeric satellite RNA is essential for kinetochore formation and cell division” J. Cell Biol. 207, 335-349.Stoops, E. H. et al. (2014) “SNAP-Tag to Monitor Trafficking of Membrane Proteins in Polarized Epithelial Cells” Methods Mol. Biol. 1174, 171-182.Bordor, D. L. et al. (2012) “Analysis of Protein Turnover by Quantitative SNAP-Based Pulse-Chase Imaging” Curr. Protoc. Cell Biol. 55, 8.8.1-8.8.34.

Pull-Down Studies:

Register, A. C. et al. (2014) “SH2-Catalytic Domain Linker Heterogeneity Influences Allosteric Coupling across the SFK Family” Biochemistry 53, 6910-6923.Shi, G. et al. (2012) “SNAP-tag based proteomics approach for the study of the retrograde route” Traffic 13, 914-925.Bieling, P. et al. (2010) “A minimal midzone protein module controls formation and length of antiparallel microtubule overlaps” Cell 142, 420-432.

Protein-Protein and Protein-Ligand Interactions:

Griss, R. et al. (2014) “Bioluminescent sensor proteins for point-of-care therapeutic drug monitoring” Nat. Chem. Biol. 10, 598-603.Chidley, C. et al. (2011) “A yeast-based screen reveals that sulfasalazine inhibits tetrahydrobiopterin biosynthesis.” Nat. Chem. Biol. 7, 375-383.Gautier A. et al. (2009) “Selective Cross-Linking of Interacting Proteins using Self-Labeling Tags” J. Am. Chem. Soc. 131, 17954-17962.Maurel D. et al. (2008) “Cell-surface protein-protein interaction analysis with time-resolved FRET and SNAP-tag technologies: application to GPCR oligomerization.” Nat. Methods 5, 561-567.

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