New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications.

By S. Adams, Robert E. Campbell, L. Gross, Brent R. Martin, G. Walkup, Yong Yao, J. Llopis, Roger Tsien. Journal of the American Chemical Society, 2002

878 citations recorded by the source corpus.

Subfields: Cell Biology, Molecular Biology, Organic Chemistry

View Paper: https://www.semanticscholar.org/paper/bceca6a0322d9d3815e8b447848105b603ab7eb6

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

1. Carolyn R. Bertozzi
2. Jennifer A. Prescher
3. A. Ting
4. M. Finn
5. Craig S Mckay
6. Ellen M. Sletten
7. Benjamin P. Roscoe
8. Daniel N. A. Bolon

In Organic Chemistry

1. Carolyn R. Bertozzi
2. Jennifer A. Prescher
3. M. Finn
4. Craig S Mckay
5. Ellen M. Sletten
6. Benjamin P. Roscoe
7. Daniel N. A. Bolon

Citations in the corpus

• Chemistry in living systems (2005, background): “This elite group comprises peptide sequences that can be ligated with small-molecule imaging probe”
• Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase (2005, background): “For instance, the FlAsH technology, which targets arsenic-functionalized fluorophores to tetracysteine motifs displayed on recombinant proteins, requires complex washout procedures to remove the probe from monothiols inside cell”