Lifeact: a versatile marker to visualize F-actin

By J. Riedl, Á. Crevenna, K. Kessenbrock, J. Yu, Dorothee Neukirchen, M. Bista, F. Bradke, D. Jenne, T. Holak, Zena Werb and 2 more. Nature Methods, 2008

2,245 citations recorded by the source corpus.

Subfields: Biophysics, Cell Biology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/99b17c5cf64ed0d215c5c9a6c79290aea6a1d4a9

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In Biophysics

1. Teresa Klein
2. Eric Betzig
3. S. Wolter
4. Denis Wirtz
5. Markus Sauer
6. M. Heidbreder
7. M. Heilemann
8. A. Löschberger

In Cell Biology

1. Peter C. Searson
2. Denis Wirtz

In Molecular Biology

1. Peter C. Searson
2. Denis Wirtz
3. Michael W. Davidson

Citations in the corpus

• A perinuclear actin cap regulates nuclear shape (2009, methodology): “This article contains supporting information online at www.pnas.org/cgi/content/full/ 0908686106/DCSupplemental. www.pnas.org cgi doi 10.1073 pnas.0908686106 PNAS November 10, 2009 vol. 106 no. 45 19017–19022 CE LL BI O LO G Y transfected with GFP-lifeact (7) focusing on top of the nucleus show that”
• Direct stochastic optical reconstruction microscopy with standard fluorescent probes (2011, methodology): “Reliable and commonly used procedures to specifically label target biomolecules in fixed cells with organic fluorophores are labeled antibodies, DNA oligonucleotides or small specifically binding peptides such as phalloidin and Lifeac”
• Robust and Bright Genetically Encoded Fluorescent Markers for Highlighting Structures and Compartments in Mammalian Cells (2017, background): “To this end, peptide sequences or protein domains have been identified that preferentially bind F-actin, such as lifeact (Riedl et al., 2008), Utrophin-CH (Burkel et al., 2007) and ITPKA(9-52)/F-tractin (Johnson and Schell, 2009).”
• Rapid three-dimensional isotropic imaging of living cells using Bessel beam plane illumination (2011, background): “For example, we recorded 100 three-dimensional image stacks detailing the dynamics of numerous actin-base”
• Ribosomal frameshifting and transcriptional slippage: From genetic steganography and cryptography to adventitious use (2016, background): “However, the conserved Nterminal 17 amino acids of ABP140 is an actin binding domain (336,337) that co-translationally causes its mRNA to associate with actin cables and be transported to the distant pole of the mother cell, rather than to the daughter cell.”