Ultrafast Elementary Events in the Excited State of Wild-Type Green-Fluorescent Protein

2003 ◽  
pp. 611-613
Author(s):  
Kathrin Winkler ◽  
Marco Seidel ◽  
Peter Vöhringer
Keyword(s):  
Excited State ◽  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Wild Type ◽  
Green Fluorescent

The effect of pressure on the excited-state proton transfer in the wild-type green fluorescent protein

2008 ◽  
Vol 455 (4-6) ◽  
pp. 303-306 ◽  
Author(s):  
Pavel Leiderman ◽  
Dan Huppert ◽  
S. James Remington ◽  
Laren M. Tolbert ◽  
Kyril M. Solntsev
Keyword(s):  
Excited State ◽  
Green Fluorescent Protein ◽  
Proton Transfer ◽  
Fluorescent Protein ◽  
Wild Type ◽  
Effect Of Pressure ◽  
Excited State Proton Transfer ◽  
In The Wild ◽  
Green Fluorescent

scholarly journals Ultrafast Excited-State Dynamics in the Green Fluorescent Protein Variant S65T/H148D. 1. Mutagenesis and Structural Studies†,‡

Biochemistry ◽  
2007 ◽  
Vol 46 (43) ◽  
pp. 12005-12013 ◽  
Author(s):  
Xiaokun Shu ◽  
Karen Kallio ◽  
Xinghua Shi ◽  
Paul Abbyad ◽  
Pakorn Kanchanawong ◽  
...  
Keyword(s):  
Excited State ◽  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Structural Studies ◽  
Protein Variant ◽  
Excited State Dynamics ◽  
Green Fluorescent ◽  
Green Fluorescent Protein Variant

scholarly journals Ultrafast dynamics in the excited state of green fluorescent protein (wt) studied by frequency-resolved femtosecond pump-probe spectroscopy

2002 ◽  
Vol 4 (6) ◽  
pp. 1072-1081 ◽  
Author(s):  
Kathrin Winkler ◽  
Jörg Lindner ◽  
Vinod Subramaniam ◽  
Thomas M. Jovin ◽  
Peter Vöhringer
Keyword(s):  
Excited State ◽  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Ultrafast Dynamics ◽  
Pump Probe ◽  
Green Fluorescent ◽  
Probe Spectroscopy

scholarly journals Recombinant Lassa Virus Expressing Green Fluorescent Protein as a Tool for High-Throughput Drug Screens and Neutralizing Antibody Assays

Viruses ◽  
2018 ◽  
Vol 10 (11) ◽  
pp. 655 ◽  
Author(s):  
Yíngyún Caì ◽  
Masaharu Iwasaki ◽  
Brett Beitzel ◽  
Shuīqìng Yú ◽  
Elena Postnikova ◽  
...  
Keyword(s):  
Green Fluorescent Protein ◽  
High Throughput ◽  
Reverse Genetics ◽  
Fluorescent Protein ◽  
Cultured Cells ◽  
Neutralizing Antibody ◽  
Quantitative Detection ◽  
Lassa Virus ◽  
Wild Type ◽  
Green Fluorescent

Lassa virus (LASV), a mammarenavirus, infects an estimated 100,000–300,000 individuals yearly in western Africa and frequently causes lethal disease. Currently, no LASV-specific antivirals or vaccines are commercially available for prevention or treatment of Lassa fever, the disease caused by LASV. The development of medical countermeasure screening platforms is a crucial step to yield licensable products. Using reverse genetics, we generated a recombinant wild-type LASV (rLASV-WT) and a modified version thereof encoding a cleavable green fluorescent protein (GFP) as a reporter for rapid and quantitative detection of infection (rLASV-GFP). Both rLASV-WT and wild-type LASV exhibited similar growth kinetics in cultured cells, whereas growth of rLASV-GFP was slightly impaired. GFP reporter expression by rLASV-GFP remained stable over several serial passages in Vero cells. Using two well-characterized broad-spectrum antivirals known to inhibit LASV infection, favipiravir and ribavirin, we demonstrate that rLASV-GFP is a suitable screening tool for the identification of LASV infection inhibitors. Building on these findings, we established a rLASV-GFP-based high-throughput drug discovery screen and an rLASV-GFP-based antibody neutralization assay. Both platforms, now available as a standard tool at the IRF-Frederick (an international resource), will accelerate anti-LASV medical countermeasure discovery and reduce costs of antiviral screens in maximum containment laboratories.

Limitations on the use of fused green fluorescent protein to investigate structure–function relationships for the cauliflower mosaic virus movement protein

Microbiology ◽  
2000 ◽  
Vol 81 (7) ◽  
pp. 1851-1855 ◽  
Author(s):  
Carole L. Thomas ◽  
Andrew J. Maule
Keyword(s):  
Green Fluorescent Protein ◽  
Mosaic Virus ◽  
Fluorescent Protein ◽  
Movement Protein ◽  
Cauliflower Mosaic Virus ◽  
Virus Movement ◽  
Wild Type ◽  
Tubule Formation ◽  
Mouth Disease Virus ◽  
Green Fluorescent

To investigate the process of tubule formation for the cauliflower mosaic virus movement protein (CaMV MP), the green fluorescent protein (GFP) was fused to the MP to provide a vital marker for MP location after expression in insect cells. In contrast to the long tubular structures seen previously following baculovirus-based expression of the wild-type MP, the fusion protein produced only aggregates of fluorescing material in the cytoplasm. However, by co-expressing wild-type MP and GFP–MP, or by engineering their co-accumulation by introducing a foot-and-mouth disease virus 2A cleavage sequence between GFP and MP, long GFP-fluorescing tubules were formed. The experiments suggest that the presence of GFP at the N or C terminus of the tubule-forming domain of the CaMV MP places steric constraints upon the aggregation of the MP into a tubule but that this can be overcome by providing wild-type protein for inclusion in the aggregate.

scholarly journals Excited-state locked amino analogues of the green fluorescent protein chromophore with a giant Stokes shift

RSC Advances ◽  
2019 ◽  
Vol 9 (66) ◽  
pp. 38730-38734 ◽  
Author(s):  
Snizhana O. Zaitseva ◽  
Dilara A. Farkhutdinova ◽  
Nadezhda S. Baleeva ◽  
Alexander Yu. Smirnov ◽  
Marina B. Zagudaylova ◽  
...  
Keyword(s):  
Excited State ◽  
Green Fluorescent Protein ◽  
Fluorescent Protein ◽  
Stokes Shift ◽  
Large Stokes Shift ◽  
New Class ◽  
Green Fluorescent

We design a new class of excited-state locked GFP chromophores which intrinsically exhibit a very large Stokes shift.

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