In vivo imaging of neuroinflammation: a comparative study between [18F]PBR111, [11C]CLINME and [11C]PK11195 in an acute rodent model

2010 ◽  
Vol 37 (5) ◽  
pp. 962-972 ◽  
Author(s):  
Nadja Van Camp ◽  
Raphael Boisgard ◽  
Bertrand Kuhnast ◽  
Benoit Thézé ◽  
Thomas Viel ◽  
...  
2017 ◽  
Vol 51 (4) ◽  
pp. 1199-1208 ◽  
Author(s):  
Jing Guo ◽  
Jing Cai ◽  
Yunxia Zhang ◽  
Yapei Zhu ◽  
Ping Yang ◽  
...  

2014 ◽  
Vol 4 (1_suppl) ◽  
pp. s-0034-1376757-s-0034-1376757
Author(s):  
Lori A Setton ◽  
Virginia B Kraus ◽  
Robby D. Bowles

2012 ◽  
Vol 69 (1) ◽  
pp. 18-26 ◽  
Author(s):  
Benjamin Lemasson ◽  
Samuel Valable ◽  
Régine Farion ◽  
Alexandre Krainik ◽  
Chantal Rémy ◽  
...  

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 ◽  
...  

2016 ◽  
Vol 54 (12) ◽  
pp. 1343-1404
Author(s):  
A Ghallab ◽  
R Reif ◽  
R Hassan ◽  
AS Seddek ◽  
JG Hengstler

1972 ◽  
Vol 11 (01) ◽  
pp. 70-78
Author(s):  
Esther Miller ◽  
Leopoldo Anghileri

SummaryThe distribution of 32P-polyphosphates (lineal and cross-linked) and 32Porthophosphate in normal and tumor bearing animals has been studied. Differences between the cross-linked and the lineal form are related to a different degree of susceptibility to the hydrolysis by the phosphatases. In contrast to orthophosphate, the polyphosphates showed a lower accumulation in soft tissues which gives an advantageous reduction of the total body radiation dose.


2020 ◽  
Author(s):  
J Iking ◽  
S Hermann ◽  
L Honold ◽  
M Kuhlmann ◽  
M Schäfers ◽  
...  

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