Results 31 to 40 of about 930,400 (311)

Electrochemical fluorescence switching of enhanced green fluorescent protein

open access: yesBiosensors and Bioelectronics, 2023
Switchable fluorescent proteins, for which fluorescence can be switched ON and OFF, are widely used for molecule tracking and super resolution imaging. However, the robust use of the switchable fluorescent proteins is still limited as either the switching is not repeatable, or such switching requires irradiation with coupled lasers of different ...
Yang, Y   +8 more
openaire   +3 more sources

Green fluorescent protein-based monitoring of endoplasmic reticulum redox poise [PDF]

open access: yes, 2013
Pathological endoplasmic reticulum (ER) stress is tightly linked to the accumulation of reactive oxidants, which can be both upstream and downstream of ER stress.
Julia Birk   +11 more
core   +1 more source

Origin of the Intrinsic Fluorescence of the Green Fluorescent Protein [PDF]

open access: yesJournal of the American Chemical Society, 2017
Green fluorescent protein, GFP, has revolutionized biology, due to its use in bioimaging. It is widely accepted that the protein environment makes its chromophore fluoresce, whereas the fluorescence is completely lost when the native chromophore is taken out of GFP.
Annette Svendsen   +4 more
openaire   +3 more sources

Fluorescent Protein-Based Metal Biosensors

open access: yesChemosensors, 2023
Fluorescent proteins (FPs) are optical probes that are used to track the functions of genetically encoded target molecules in molecular and cellular biology.
Ki Hyun Nam
doaj   +1 more source

Photochromicity and Fluorescence Lifetimes of Green Fluorescent Protein [PDF]

open access: yesThe Journal of Physical Chemistry B, 1999
The green fluorescent protein (GFP) of the bioluminescent jellyfish Aequorea and its mutants have gained widespread usage as an indicator of structure and function within cells. Proton transfer has been implicated in the complex photophysics of the wild-type molecule, exhibiting a protonated A species excited at 400 nm, and two deprotonated excited ...
Striker, G.   +3 more
openaire   +2 more sources

ATP changes the fluorescence lifetime of cyan fluorescent protein via an interaction with His148 [PDF]

open access: yes, 2010
Contains fulltext : 87235.pdf (Publisher’s version ) (Open Access)Recently, we described that ATP induces changes in YFP/CFP fluorescence intensities of Fluorescence Resonance Energy Transfer (FRET) sensors based on CFP-YFP.
Marieke Willemse   +28 more
core   +1 more source

On the Origin of Fluorescence in Bacteriophytochrome Infrared Fluorescent Proteins [PDF]

open access: yesThe Journal of Physical Chemistry B, 2010
Tsien et al. (Science, 2009, 324, 804-807) recently reported the creation of the first infrared fluorescent protein (IFP). It was engineered from bacterial phytochrome by removing the PHY and histidine kinase-related domains, by optimizing the protein to prevent dimerization, and by limiting the biliverdins conformational freedom, especially around its
Alex A, Samma   +4 more
openaire   +2 more sources

FMDV replicons encoding green fluorescent protein are replication competent [PDF]

open access: yes, 2014
The study of replication of viruses that require high bio-secure facilities can be accomplished with less stringent containment using non-infectious 'replicon' systems. The FMDV replicon system (pT7rep) reported by Mclnerney et al. (2000) was modified by
Stonehouse, Nicola J.   +32 more
core   +1 more source

Ratiometric Matryoshka biosensors from a nested cassette of green- and orange-emitting fluorescent proteins

open access: yesNature Communications, 2017
Single fluorescent protein biosensors are susceptible to expression and instrumental artifacts. Here Ast et al. describe a dual fluorescent protein design whereby a reference fluorescent protein is nested within a reporter fluorescent protein to control ...
Cindy Ast   +6 more
doaj   +1 more source

Homotransfer FRET Reporters for Live Cell Imaging

open access: yesBiosensors, 2018
Förster resonance energy transfer (FRET) between fluorophores of the same species was recognized in the early to mid-1900s, well before modern heterotransfer applications.
Nicole E. Snell   +6 more
doaj   +1 more source

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