An improved cyan fluorescent protein variant useful for FRET

By M. Rizzo, Gerald H. Springer, Butch Granada, David W. Piston. Nature Biotechnology, 2004

1,137 citations recorded by the source corpus.

Subfields: Biophysics, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/091f5e5f7f95a82b9cafbf307a00ea06c123b597

How researchers see this paper

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

In Biophysics

In Molecular Biology

Citations in the corpus

A Novel Role for the TIR Domain in Association with Pathogen-Derived Elicitors (2007, methodology): “For this, we used improved EYFP and ECFP variants, Citrine and Cerulean, respectively, which produce greater fluorescence signal and hence allow easier detection of our fusion proteins [35,36].”
A quantitative protocol for dynamic measurements of protein interactions by Förster resonance energy transfer-sensitized fluorescence emission (2009, methodology): “In the work presented here, enhancedCFP (ECFP), enhancedYFP (EYFP) (Rizzo et al. 2004) and cerulean (Cer), an improved form of CFP (Shaner et al. 2005), were used.”
Recruitment and activation of PLCγ1 in T cells: a new insight into old domains (2006, methodology): “The Cerulean CFP plasmid was created from pECFP-N1 (Clontech) by A206, S72A, Y145A and H148D substitutions (Zacharias et al, 2002; Rizzo et al, 2004).”
Fluorescent proteins and their applications in imaging living cells and tissues. (2010, background): “Directed evolution of ECFP resulted in substantial progress, with the best variants reported being Cerulean (360) SCFPs (231), TagCFP (Evrogen JSC), and mTurquoise (122), all characterized by enhanced brightness and/or maturation rate (table in Fig.”
Development of an optimized backbone of FRET biosensors for kinases and GTPases (2011, background): “Although several research groups have generated a number of FP variants that are optimized for FRET applications (Karasawa et al., 2004; Rizzo et al., 2004; Nguyen and Daugherty, 2005), the development of FP pairs for FRET is still one of the greatest challenges in FRET biosensor development (Li et ”
A guide to choosing fluorescent proteins (2005, neutral): “Ceruleang Piston (3) 433 475 27* 36 4.”
Measuring single-cell gene expression dynamics in bacteria using fluorescence time-lapse microscopy (2011, background): “Antivibration table (11).”
Genetically encoded calcium indicators for multi-color neural activity imaging and combination with optogenetics (2013, background): “…often by mutating positions near the chromophore to improve folding, maturation, brightness, and photostability (Griesbeck et al., 2001; Nagai et al., 2002; Rizzo et al., 2004; Nguyen and Daugherty, 2005; Ai et al., 2006, 2007; Kremers et al., 2006, 2007; Mena et al., 2006; Goedhart et al., 2010).”
Progressive activation of CyclinB1-Cdk1 coordinates entry to mitosis. (2010, methodology): “As the FRET pair we used mCerulean (Rizzo et al., 2004) and YPet (Nguyen and Daugherty, 2005) fluorescent proteins, and as the phosphobinding domain we used the polo box domain (PBD) of Plk1 that binds to CDK phosphorylation sites in vivo (Elia et al.”
Evolutionary optimization of fluorescent proteins for intracellular FRET (2005, background): “The small dynamic range of fluorescent protein FRET yields poor sensitivity for many application”
Rapid, combinatorial analysis of membrane compartments in intact plants with a multicolor marker set. (2009, methodology): “FPs with high spectral compatibility and increased sensitivity were selected (Rizzo et al., 2004; Shaner et al., 2004; Ai et al., 2007), and epitope tags were added for use in immuno-EM and biochemical fractionations (Figure 1a).”