Engineering an improved light-induced dimer (iLID) for controlling the localization and activity of signaling proteins
By Gurkan Guntas, Ryan A. Hallett, S. Zimmerman, T. Williams, Hayretin Yumerefendi, J. Bear, Brian Kuhlman. Proceedings of the National Academy of Sciences of the United States of America, 2014
596 citations recorded by the source corpus.
Subfields: Materials Chemistry, Molecular Biology, Plant Science
View Paper: https://www.semanticscholar.org/paper/ae0f77ce3143fde359d21e4d27efa498c176f385
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In Molecular Biology
Citations in the corpus
- Protein Engineering by Combined Computational and In Vitro Evolution Approaches. (2016, methodology): “[31] used such an approach to generate a photoswitchable binding protein based on a naturally occurring photoswitch, the light-oxygen-voltage 2 (LOV2) domain, which partially unfolds upon exposure to light.”
- Competing protein-RNA interaction networks control multiphase intracellular organization (2020, unknown): “To test this, we replaced G3BP’s NTF2 with synthetic light-activated (iLID- and sspB- [iLID/sspB]) (Guntas et al., 2015) or constitutive (FKBP) (Rollins et al.”
- Liquid Nuclear Condensates Mechanically Sense and Restructure the Genome. (2018, unknown): “The second construct linking genomic preseeding to optogenetic assembly involves single-chain variable fragment (scFv) antibody, cognate for the ST, fused to superfolder GFP (sfGFP) and the optogenetic dimerization protein iLID (Guntas et al., 2015).”