Thrombin effectuates therapeutic arteriogenesis in the rabbit hindlimb ischemia model: A quantitative analysis by computerized in vivo imaging

2006 ◽  
Vol 569 (2) ◽  
pp. 622-625 ◽  
Author(s):  
George C. Kagadis ◽  
Dimitrios Karnabatidis ◽  
Konstantinos Katsanos ◽  
Athanassios Diamantopoulos ◽  
Nikolaos Samaras ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
In Vivo Imaging ◽  
Hindlimb Ischemia

scholarly journals In Vivo Imaging and Quantitative Analysis of Leukocyte Directional Migration and Polarization in Inflamed Tissue

PLoS ONE ◽  
2009 ◽  
Vol 4 (3) ◽  
pp. e4693 ◽  
Author(s):  
Alexander Georg Khandoga ◽  
Andrej Khandoga ◽  
Christoph Andreas Reichel ◽  
Peter Bihari ◽  
Markus Rehberg ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
In Vivo Imaging ◽  
Directional Migration ◽  
Inflamed Tissue

Quantitative analysis of cell tracing by in vivo imaging system

2010 ◽  
Vol 30 (4) ◽  
pp. 541-545 ◽  
Author(s):  
Junmeng Zheng ◽  
Lijun Xu ◽  
Hongmin Zhou ◽  
Weina Zhang ◽  
Zhonghua Chen
Keyword(s):  
Quantitative Analysis ◽  
In Vivo Imaging ◽  
Imaging System ◽  
Cell Tracing ◽  
In Vivo Imaging System

In vivo imaging and quantitative analysis of TSPO in rat peripheral tissues using small-animal PET with [18F]FEDAC

2010 ◽  
Vol 37 (7) ◽  
pp. 853-860 ◽  
Author(s):  
Kazuhiko Yanamoto ◽  
Katsushi Kumata ◽  
Masayuki Fujinaga ◽  
Nobuki Nengaki ◽  
Makoto Takei ◽  
...  
Keyword(s):  
Quantitative Analysis ◽  
In Vivo Imaging ◽  
Small Animal ◽  
Small Animal Pet ◽  
Peripheral Tissues ◽  
Animal Pet

scholarly journals In vivo imaging and quantitative analysis of insulin-receptor interaction in lean and obese Zucker rats

Diabetologia ◽  
1984 ◽  
Vol 26 (3) ◽  
pp. 229-233 ◽  
Author(s):  
J. C. Sodoyez ◽  
F. Sodoyez-Goffaux ◽  
S. Treves ◽  
C. R. Kahn ◽  
R. von Frenckell
Keyword(s):  
Quantitative Analysis ◽  
Insulin Receptor ◽  
In Vivo Imaging ◽  
Zucker Rats ◽  
Receptor Interaction ◽  
Obese Zucker Rats

Solving the mechanisms responsible for organelle behavior in vivo by same-cell correlative light and electron microscopy

1992 ◽  
Vol 50 (1) ◽  
pp. 14-15
Author(s):  
Conly L. Rieder
Keyword(s):  
Electron Microscopy ◽  
Quantitative Analysis ◽  
Light Microscopy ◽  
Living Cell ◽  
Light And Electron Microscopy ◽  
Time Behavior ◽  
Dynamic Interactions ◽  
Positive Identification ◽  
Cellular Components

The behavior of many cellular components, and their dynamic interactions, can be characterized in the living cell with considerable spatial and temporal resolution by video-enhanced light microscopy (video-LM). Indeed, under the appropriate conditions video-LM can be used to determine the real-time behavior of organelles ≤ 25-nm in diameter (e.g., individual microtubules—see). However, when pushed to its limit the structures and components observed within the cell by video-LM cannot be resolved nor necessarily even identified, only detected. Positive identification and a quantitative analysis often requires the corresponding electron microcopy (EM).

Fluorescent proteins for in vivo imaging, where's the biliverdin?

2020 ◽  
Vol 48 (6) ◽  
pp. 2657-2667
Author(s):  
Felipe Montecinos-Franjola ◽  
John Y. Lin ◽  
Erik A. Rodriguez
Keyword(s):  
Hydrogen Peroxide ◽  
In Vivo Imaging ◽  
Near Infrared ◽  
Fluorescent Protein ◽  
Fluorescent Proteins ◽  
Fluorescent Imaging ◽  
Infrared Light ◽  
Red Fluorescent Protein ◽  
Color Palette

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.

In vivo imaging of beta-amyloid load in transgenic rodents with [F-18]FDDNP microPET

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