scholarly journals Seminaphthofluorescein-Based Fluorescent Probes for Imaging Nitric Oxide in Live Cells

2011 ◽  
Vol 50 (19) ◽  
pp. 9385-9392 ◽  
Author(s):  
Michael D. Pluth ◽  
Maria R. Chan ◽  
Lindsey E. McQuade ◽  
Stephen J. Lippard
Keyword(s):  
Nitric Oxide ◽  
Fluorescent Probes ◽  
Live Cells

Targetable, two-photon fluorescent probes for local nitric oxide capture in the plasma membranes of live cells and brain tissues

The Analyst ◽  
2018 ◽  
Vol 143 (17) ◽  
pp. 4180-4188 ◽  
Author(s):  
Xinfu Zhang ◽  
Benlei Wang ◽  
Yi Xiao ◽  
Chao Wang ◽  
Ling He
Keyword(s):  
Nitric Oxide ◽  
Plasma Membrane ◽  
Fluorescent Probe ◽  
Fluorescent Probes ◽  
Plasma Membranes ◽  
Live Cells ◽  
Two Photon ◽  
In Cells ◽  
Brain Tissues

A plasma membrane-targetable two-photon fluorescent probe for capturing nitric oxide in cells and brain tissues.

scholarly journals Bioinspired Design of Reversible Fluorescent Probes for Tracking Nitric Oxide Dynamics in Live Cells

CCS Chemistry ◽  
2021 ◽  
pp. 116-128
Author(s):  
Rui-Ying Guo ◽  
Yu-Tian Zhang ◽  
Supphachok Chanmungkalakul ◽  
Hao-Ran Guo ◽  
Yongzhou Hu ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Fluorescent Probes ◽  
Live Cells ◽  
Bioinspired Design

scholarly journals Bioinspired Design of Reversible Fluorescent Probes for Tracking Nitric Oxide Dynamics in Live Cells

CCS Chemistry ◽  
2020 ◽  
pp. 1-35
Author(s):  
Rui-Ying Guo ◽  
Yu-Tian Zhang ◽  
Supphachok Chanmungkalakul ◽  
Hao-Ran Guo ◽  
Yongzhou Hu ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Fluorescent Probes ◽  
Live Cells ◽  
Bioinspired Design

scholarly journals Fluorescent Probes for Live Cell Thiol Detection

Molecules ◽  
2021 ◽  
Vol 26 (12) ◽  
pp. 3575
Author(s):  
Shenggang Wang ◽  
Yue Huang ◽  
Xiangming Guan
Keyword(s):  
Fluorescent Probes ◽  
Biological System ◽  
High Sensitivity ◽  
Intracellular Distribution ◽  
Live Cell ◽  
Live Cells ◽  
High Demand ◽  
Non Invasive

Thiols play vital and irreplaceable roles in the biological system. Abnormality of thiol levels has been linked with various diseases and biological disorders. Thiols are known to distribute unevenly and change dynamically in the biological system. Methods that can determine thiols’ concentration and distribution in live cells are in high demand. In the last two decades, fluorescent probes have emerged as a powerful tool for achieving that goal for the simplicity, high sensitivity, and capability of visualizing the analytes in live cells in a non-invasive way. They also enable the determination of intracellular distribution and dynamitic movement of thiols in the intact native environments. This review focuses on some of the major strategies/mechanisms being used for detecting GSH, Cys/Hcy, and other thiols in live cells via fluorescent probes, and how they are applied at the cellular and subcellular levels. The sensing mechanisms (for GSH and Cys/Hcy) and bio-applications of the probes are illustrated followed by a summary of probes for selectively detecting cellular and subcellular thiols.

Mechanisms of calcium signaling by cyclic ADP-ribose and NAADP

1997 ◽  
Vol 77 (4) ◽  
pp. 1133-1164 ◽  
Author(s):  
H. C. Lee
Keyword(s):  
Nitric Oxide ◽  
Nicotinic Acid ◽  
Live Cells ◽  
Release Mechanism ◽  
Major Mechanism ◽  
Signaling Mechanisms ◽  
Signaling Function ◽  
Cyclic Adp Ribose ◽  
Inositol 1,4,5 Trisphosphate ◽  
External Signals

Cells possess various mechanisms for transducing external signals to intracellular responses. The discovery of inositol 1,4,5-trisphosphate (IP3) as a messenger for mobilizing internal Ca2+ stores has centralized Ca2+ mobilization among signaling mechanisms. Results reviewed in this article establish that, in addition to IP3, the internal Ca2+ stores can be mobilized by at least two other molecules, cyclic ADP-ribose (cADPR) and nicotinic acid adenine dinucleotide phosphate (NAADP), via totally independent mechanisms. Cyclic ADP-ribose is a newly discovered cyclic nucleotide derived from NAD, but, unlike adenosine 3',5'-cyclic monophosphate, its main signaling function is modulation of Ca(2+)-induced Ca2+ release, a major mechanism of Ca2+ mobilization in addition to the IP3 pathway. Evidence shows that cADPR may in fact be responsible for mediating the Ca(2+)-mobilizing activity of the gaseous messenger nitric oxide. Cells responsive to cADPR are widespread and include species from plant to mammal, indicating the generality of cADPR as a signaling molecule. In addition to cADPR, NAADP, a metabolite of NADP, can also mobilize Ca2+ stores. The release mechanism and the stores on which NAADP acts are distinct from cADPR and IP3. Nicotinic acid adenine dinucleotide phosphate may play a role in generating Ca2+ oscillations, since liberation of NAADP in live cells by photolyzing its caged analog produces long lasting Ca2+ oscillations. These two new Ca2+ agonists are intimately related, since the same metabolic enzymes can, under appropriate conditions, synthesize either one, suggesting a unified mechanism may regulate both pathways. Elucidation of these two new Ca2+ mobilization pathways is likely to have an important impact on our understanding of cellular signaling mechanisms.

scholarly journals Fluorescent Probes with Unnatural Amino Acids to Monitor Proteasome Activity in Real-Time

2020 ◽  
Author(s):  
Breanna L. Zerfas ◽  
Rachel A. Coleman ◽  
Andres Salazar Chaparro ◽  
Nathaniel J. Macatangay ◽  
Darci Trader
Keyword(s):  
Amino Acids ◽  
Small Molecule ◽  
Fluorescent Probes ◽  
Unnatural Amino Acids ◽  
Cell Types ◽  
Proteasome Activity ◽  
Live Cells ◽  
Fluorescent Substrate ◽  
The Individual ◽  
Small Molecule Modulators

<div> <div> <div> <p>The proteasome is an essential protein complex that, when dysregulated, can result in various diseases in eukaryotic cells. As such, understanding the enzymatic activity of the proteasome and what can alter it is crucial to elucidating its roles in these diseases. This can be done effectively by using activity-based fluorescent substrate probes, of which there are many commercially available that target the individual protease-like subunits in the 20S CP of the proteasome. Unfortunately, these probes have not displayed appropriate characteristics for their use in live cell-based assays. In the work presented here, we have developed a set of probes which have shown improved fluorescence properties and selectivity towards the proteasome compared to other cellular proteases. By including unnatural amino acids, we have found probes which can be utilized in various applications, including monitoring the effects of small molecule stimulators of the proteasome in live cells and comparing the relative proteasome activity across different cancer cell types. In future studies, we expect the fluorescent probes presented here will serve as tools to support the discovery and characterization of small molecule modulators of proteasome activity. </p> </div> </div> </div>

Harnessing Se=N to develop novel fluorescent probes for visualizing the variation of endogenous hypobromous acid (HOBr) during the administration of immunotherapeutic agent

2021 ◽  
Author(s):  
Jian Zhang ◽  
kaiqiang Liu ◽  
Jingwen Li ◽  
Yingying Xie ◽  
Yong Li ◽  
...  
Keyword(s):  
Fluorescent Probes ◽  
Live Cells ◽  
Immunotherapeutic Agent ◽  
Hypobromous Acid ◽  
In Virtue Of

In virtue of the formation of Se=N, ABT-Se and NDI-Se were developed to detect and visualize endogenous HOBr in live cells. Specifically, the upregulation of HOBr was monitored by NDI-Se...

Turn-on visible and ratiometric near-infrared fluorescent probes for distinction endogenous esterases and chymotrypsins in live cells

2020 ◽  
Vol 306 ◽  
pp. 127567 ◽  
Author(s):  
Jiemin Wang ◽  
Zhidong Teng ◽  
Ting Cao ◽  
Jing Qian ◽  
Lei Zheng ◽  
...  
Keyword(s):  
Fluorescent Probes ◽  
Near Infrared ◽  
Live Cells ◽  
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