Self-Assembled Biodegradable Protein–Polymer Vesicle as a Tumor-Targeted Nanocarrier

2014 ◽  
Vol 6 (4) ◽  
pp. 2393-2400 ◽  
Author(s):  
Zhongyun Liu ◽  
Chunhong Dong ◽  
Xiaomin Wang ◽  
Hanjie Wang ◽  
Wei Li ◽  
...  
Author(s):  
Zihao Li ◽  
Yanyan Jiang ◽  
Kilian Wüst ◽  
Manuela Callari ◽  
Martina H. Stenzel

2014 ◽  
Vol 24 (43) ◽  
pp. 6762-6770 ◽  
Author(s):  
Patrick van Rijn ◽  
Murat Tutus ◽  
Christine Kathrein ◽  
Nathalie C. Mougin ◽  
Hyunji Park ◽  
...  

2017 ◽  
Vol 75 (6) ◽  
pp. 2627-2639 ◽  
Author(s):  
Qi Cao ◽  
Naipu He ◽  
Yue Wang ◽  
Zhenwu Lu

2014 ◽  
Vol 24 (43) ◽  
pp. 6896-6896
Author(s):  
Patrick van Rijn ◽  
Murat Tutus ◽  
Christine Kathrein ◽  
Nathalie C. Mougin ◽  
Hyunji Park ◽  
...  

Author(s):  
G. C. Ruben ◽  
K. Iqbal ◽  
I. Grundke-Iqbal ◽  
H. Wisniewski ◽  
T. L. Ciardelli ◽  
...  

In neurons, the microtubule associated protein, tau, is found in the axons. Tau stabilizes the microtubules required for neurotransmitter transport to the axonal terminal. Since tau has been found in both Alzheimer neurofibrillary tangles (NFT) and in paired helical filaments (PHF), the study of tau's normal structure had to preceed TEM studies of NFT and PHF. The structure of tau was first studied by ultracentrifugation. This work suggested that it was a rod shaped molecule with an axial ratio of 20:1. More recently, paraciystals of phosphorylated and nonphosphoiylated tau have been reported. Phosphorylated tau was 90-95 nm in length and 3-6 nm in diameter where as nonphosphorylated tau was 69-75 nm in length. A shorter length of 30 nm was reported for undamaged tau indicating that it is an extremely flexible molecule. Tau was also studied in relation to microtubules, and its length was found to be 56.1±14.1 nm.


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