scholarly journals Bioluminescence tomography with structural information estimated via statistical mouse atlas registration

2018 ◽  
Vol 9 (8) ◽  
pp. 3544
Author(s):  
Bin Zhang ◽  
Wanzhou Yin ◽  
Hao Liu ◽  
Xu Cao ◽  
Hongkai Wang
2012 ◽  
Vol 57 (19) ◽  
pp. 6063-6077 ◽  
Author(s):  
Hongkai Wang ◽  
David B Stout ◽  
Richard Taschereau ◽  
Zheng Gu ◽  
Nam T Vu ◽  
...  

2017 ◽  
Vol 10 (03) ◽  
pp. 1750003 ◽  
Author(s):  
Shuang Zhang ◽  
Chengcai Leng ◽  
Hongbo Liu ◽  
Kun Wang ◽  
Jie Tian

Bioluminescence tomography (BLT) is a novel optical molecular imaging technique that advanced the conventional planar bioluminescence imaging (BLI) into a quantifiable three-dimensional (3D) approach in preclinical living animal studies in oncology. In order to solve the inverse problem and reconstruct tumor lesions inside animal body accurately, the prior structural information is commonly obtained from X-ray computed tomography (CT). This strategy requires a complicated hybrid imaging system, extensive post imaging analysis and involvement of ionizing radiation. Moreover, the overall robustness highly depends on the fusion accuracy between the optical and structural information. Here, we present a pure optical bioluminescence tomographic (POBT) system and a novel BLT workflow based on multi-view projection acquisition and 3D surface reconstruction. This method can reconstruct the 3D surface of an imaging subject based on a sparse set of planar white-light and bioluminescent images, so that the prior structural information can be offered for 3D tumor lesion reconstruction without the involvement of CT. The performance of this novel technique was evaluated through the comparison with a conventional dual-modality tomographic (DMT) system and a commercialized optical imaging system (IVIS Spectrum) using three breast cancer xenografts. The results revealed that the new technique offered comparable in vivo tomographic accuracy with the DMT system ([Formula: see text]) in much shorter data analysis time. It also offered significantly better accuracy comparing with the IVIS system ([Formula: see text]) without sacrificing too much time.


2011 ◽  
Vol 50 (3) ◽  
pp. 586-609 ◽  
Author(s):  
Tungyou Lin ◽  
Carole Le Guyader ◽  
Ivo Dinov ◽  
Paul Thompson ◽  
Arthur Toga ◽  
...  

2016 ◽  
Vol 7 (4) ◽  
pp. 1549 ◽  
Author(s):  
Shenghan Ren ◽  
Haihong Hu ◽  
Gen Li ◽  
Xu Cao ◽  
Shouping Zhu ◽  
...  

2014 ◽  
Vol 5 (6) ◽  
pp. 1861 ◽  
Author(s):  
Jun Zhang ◽  
Duofang Chen ◽  
Jimin Liang ◽  
Huadan Xue ◽  
Jing Lei ◽  
...  

2009 ◽  
Author(s):  
Tungyou Lin ◽  
Carole Le Guyader ◽  
Erh-Fang Lee ◽  
Ivo D. Dinov ◽  
Paul M. Thompson ◽  
...  

Author(s):  
R.M. Glaeser ◽  
S.B. Hayward

Highly ordered or crystalline biological macromolecules become severely damaged and structurally disordered after a brief electron exposure. Evidence that damage and structural disorder are occurring is clearly given by the fading and eventual disappearance of the specimen's electron diffraction pattern. The fading and disappearance of sharp diffraction spots implies a corresponding disappearance of periodic structural features in the specimen. By the same token, there is a oneto- one correspondence between the disappearance of the crystalline diffraction pattern and the disappearance of reproducible structural information that can be observed in the images of identical unit cells of the object structure. The electron exposures that result in a significant decrease in the diffraction intensity will depend somewhat upon the resolution (Bragg spacing) involved, and can vary considerably with the chemical makeup and composition of the specimen material.


Author(s):  
S. W. Hui ◽  
T. P. Stewart

Direct electron microscopic study of biological molecules has been hampered by such factors as radiation damage, lack of contrast and vacuum drying. In certain cases, however, the difficulties may be overcome by using redundent structural information from repeating units and by various specimen preservation methods. With bilayers of phospholipids in which both the solid and fluid phases co-exist, the ordering of the hydrocarbon chains may be utilized to form diffraction contrast images. Domains of different molecular packings may be recgnizable by placing properly chosen filters in the diffraction plane. These domains would correspond to those observed by freeze fracture, if certain distinctive undulating patterns are associated with certain molecular packing, as suggested by X-ray diffraction studies. By using an environmental stage, we were able to directly observe these domains in bilayers of mixed phospholipids at various temperatures at which their phases change from misible to inmissible states.


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