scholarly journals In vivo imaging of the developing cerebral cortex to elucidate the mechanism for activity-dependent circuit maturation

IBRO Reports ◽  
2019 ◽  
Vol 6 ◽  
pp. S53
Author(s):  
Hidenobu Mizuno
NeuroImage ◽  
2021 ◽  
pp. 118260
Author(s):  
Wei Qin ◽  
Qi Gan ◽  
Lei Yang ◽  
Yongchao Wang ◽  
Weizhi Qi ◽  
...  

The Analyst ◽  
2021 ◽  
Author(s):  
Yongbin Zhang ◽  
le wen ◽  
Weijie Zhang ◽  
yongkang yue ◽  
Jianbin Chao ◽  
...  

Reactive sulfur species (RSS) plays pivotal roles in various pathological and physiological processes. There exists an intricate relevance in generation and metabolism among these substances. Although they are nucleophilic, there...


Neuroscience ◽  
2012 ◽  
Vol 212 ◽  
pp. 190-200 ◽  
Author(s):  
K. Masamoto ◽  
Y. Tomita ◽  
H. Toriumi ◽  
I. Aoki ◽  
M. Unekawa ◽  
...  

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez

Noninvasive fluorescent imaging requires far-red and near-infrared fluorescent proteins for deeper imaging. Near-infrared light penetrates biological tissue with blood vessels due to low absorbance, scattering, and reflection of light and has a greater signal-to-noise due to less autofluorescence. Far-red and near-infrared fluorescent proteins absorb light >600 nm to expand the color palette for imaging multiple biosensors and noninvasive in vivo imaging. The ideal fluorescent proteins are bright, photobleach minimally, express well in the desired cells, do not oligomerize, and generate or incorporate exogenous fluorophores efficiently. Coral-derived red fluorescent proteins require oxygen for fluorophore formation and release two hydrogen peroxide molecules. New fluorescent proteins based on phytochrome and phycobiliproteins use biliverdin IXα as fluorophores, do not require oxygen for maturation to image anaerobic organisms and tumor core, and do not generate hydrogen peroxide. The small Ultra-Red Fluorescent Protein (smURFP) was evolved from a cyanobacterial phycobiliprotein to covalently attach biliverdin as an exogenous fluorophore. The small Ultra-Red Fluorescent Protein is biophysically as bright as the enhanced green fluorescent protein, is exceptionally photostable, used for biosensor development, and visible in living mice. Novel applications of smURFP include in vitro protein diagnostics with attomolar (10−18 M) sensitivity, encapsulation in viral particles, and fluorescent protein nanoparticles. However, the availability of biliverdin limits the fluorescence of biliverdin-attaching fluorescent proteins; hence, extra biliverdin is needed to enhance brightness. New methods for improved biliverdin bioavailability are necessary to develop improved bright far-red and near-infrared fluorescent proteins for noninvasive imaging in vivo.


2005 ◽  
Vol 25 (1_suppl) ◽  
pp. S588-S588
Author(s):  
Vladimir Kepe ◽  
Gregory M Cole ◽  
Jie Liu ◽  
Dorothy G Flood ◽  
Stephen P Trusko ◽  
...  

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