scholarly journals Bioorthogonal mRNA labeling at the poly(A) tail for imaging localization and dynamics in live zebrafish embryos

2020 ◽  
Vol 11 (11) ◽  
pp. 3089-3095 ◽  
Author(s):  
Kim J. Westerich ◽  
Karthik S. Chandrasekaran ◽  
Theresa Gross-Thebing ◽  
Nadine Kueck ◽  
Erez Raz ◽  
...  
Keyword(s):  
Live Imaging ◽  
Zebrafish Embryos ◽  
In Cells

Live imaging of mRNA in cells and organisms is important for understanding the dynamic aspects underlying its function.

scholarly journals Safe-by-Design CuO Nanoparticles via Fe-Doping, Cu–O Bond Length Variation, and Biological Assessment in Cells and Zebrafish Embryos

ACS Nano ◽  
2017 ◽  
Vol 11 (1) ◽  
pp. 501-515 ◽  
Author(s):  
Hendrik Naatz ◽  
Sijie Lin ◽  
Ruibin Li ◽  
Wen Jiang ◽  
Zhaoxia Ji ◽  
...  
Keyword(s):  
Bond Length ◽  
Cuo Nanoparticles ◽  
Biological Assessment ◽  
Zebrafish Embryos ◽  
Length Variation ◽  
Fe Doping ◽  
Safe By Design ◽  
In Cells

scholarly journals Ultraspecific live imaging of the dynamics of zebrafish neutrophil granules by a histopermeable fluorogenic benzochalcone probe

2019 ◽  
Vol 10 (12) ◽  
pp. 3654-3670 ◽  
Author(s):  
Emma Colucci-Guyon ◽  
Ariane S. Batista ◽  
Suellen D. S. Oliveira ◽  
Magali Blaud ◽  
Ismael C. Bellettini ◽  
...  
Keyword(s):  
Live Imaging ◽  
Zebrafish Embryos ◽  
Wild Type

A fluorogenic benzochalcone specifically labels live neutrophil granules in whole wild-type, GFP- or RFP-expressing zebrafish embryos and larvae.

scholarly journals Actin Organization in Cells Responding to a Perforated Surface, Revealed by Live Imaging and Cryo-Electron Tomography

Structure ◽  
2016 ◽  
Vol 24 (7) ◽  
pp. 1031-1043 ◽  
Author(s):  
Marion Jasnin ◽  
Mary Ecke ◽  
Wolfgang Baumeister ◽  
Günther Gerisch
Keyword(s):  
Electron Tomography ◽  
Live Imaging ◽  
Actin Organization ◽  
Cryo Electron Tomography ◽  
In Cells

The protein product of the zebrafish homologue of the mouse T gene is expressed in nuclei of the germ ring and the notochord of the early embryo

Development ◽  
1992 ◽  
Vol 116 (4) ◽  
pp. 1021-1032 ◽  
Author(s):  
S. Schulte-Merker ◽  
R.K. Ho ◽  
B.G. Herrmann ◽  
C. Nusslein-Volhard
Keyword(s):  
Early Development ◽  
Nuclear Localization ◽  
Protein Product ◽  
Early Embryo ◽  
Paraxial Mesoderm ◽  
Zebrafish Embryos ◽  
Brachydanio Rerio ◽  
Cloning And Sequencing ◽  
Yolk Syncytial Layer ◽  
In Cells

Embryos mutant for the T gene, in mice, make insufficient mesoderm and fail to develop a notochord. We report the cloning and sequencing of the T gene in the zebrafish (Brachydanio rerio) and show the nuclear localization of the protein product. Both RNA and protein are found in cells of the germ ring, including enveloping layer cells, prior to and during gastrulation of zebrafish embryos. Nuclei of the yolk syncytial layer do not express Zf-T. High levels of expression are maintained throughout early development in the notochord, while in paraxial mesoderm cells the gene is turned off during gastrulation. Exposure of animal cap cells to activinA induces Zf-T expression, as does transplantation into the germ ring.

Blue Light Activated Rapamycin for Optical Control of Protein Dimerization in Cells and Zebrafish Embryos

2021 ◽  
Author(s):  
Taylor M. Courtney ◽  
Kristie E. Darrah ◽  
Trevor J. Horst ◽  
Michael Tsang ◽  
Alexander Deiters
Keyword(s):  
Blue Light ◽  
Optical Control ◽  
Zebrafish Embryos ◽  
Protein Dimerization ◽  
In Cells

scholarly journals Spatiotemporal Control of CRISPR/Cas9 Function in Cells and Zebrafish using Light-Activated Guide RNA

2019 ◽  
Author(s):  
Wenyuan Zhou ◽  
Wes Brown ◽  
Anirban Bardhan ◽  
Michael Delaney ◽  
Amber S. Ilk ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Zebrafish Embryos ◽  
Complete Suppression ◽  
Guide Rna ◽  
Guide Rnas ◽  
Ribonucleoprotein Complexes ◽  
Conditional Control ◽  
Rapid Restoration ◽  
Spatiotemporal Control ◽  
In Cells

AbstractWe developed a new method for conditional regulation of CRISPR/Cas9 activity in mammalian cells and zebrafish embryos via photochemically activated, caged guide RNAs. Caged gRNAs are generated by substituting four nucleobases evenly distributed throughout the 5’-protospacer region with caged nucleobases during synthesis. Caging confers complete suppression of gRNA:target dsDNA hybridization and rapid restoration of CRISPR/Cas9 function upon optical activation. This tool offers simplicity and complete programmability in design, high spatiotemporal specificity in cells and zebrafish embryos, excellent off to on switching, and stability by preserving the ability to form Cas9:gRNA ribonucleoprotein complexes. caged gRNAs are novel tools for conditional control of gene editing thereby enabling the investigation of spatiotemporally complex physiological events by obtaining a better understanding of dynamic gene regulation.

scholarly journals TTC26/DYF13 is an intraflagellar transport protein required for transport of motility-related proteins into flagella

eLife ◽  
2014 ◽  
Vol 3 ◽  
Author(s):  
Hiroaki Ishikawa ◽  
Takahiro Ide ◽  
Toshiki Yagi ◽  
Xue Jiang ◽  
Masafumi Hirono ◽  
...  
Keyword(s):  
Chlamydomonas Reinhardtii ◽  
Mammalian Cells ◽  
Intraflagellar Transport ◽  
Live Imaging ◽  
Transport Protein ◽  
Zebrafish Embryos ◽  
Particle Assembly ◽  
Biochemical Analyses ◽  
Related Proteins

Cilia/flagella are assembled and maintained by the process of intraflagellar transport (IFT), a highly conserved mechanism involving more than 20 IFT proteins. However, the functions of individual IFT proteins are mostly unclear. To help address this issue, we focused on a putative IFT protein TTC26/DYF13. Using live imaging and biochemical approaches we show that TTC26/DYF13 is an IFT complex B protein in mammalian cells and Chlamydomonas reinhardtii. Knockdown of TTC26/DYF13 in zebrafish embryos or mutation of TTC26/DYF13 in C. reinhardtii, produced short cilia with abnormal motility. Surprisingly, IFT particle assembly and speed were normal in dyf13 mutant flagella, unlike in other IFT complex B mutants. Proteomic and biochemical analyses indicated a particular set of proteins involved in motility was specifically depleted in the dyf13 mutant. These results support the concept that different IFT proteins are responsible for different cargo subsets, providing a possible explanation for the complexity of the IFT machinery.

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