High molecular weight soft segment based polyethylene shape memory polymers

2012 ◽  
Vol 9 (3) ◽  
pp. 179-186 ◽  
Author(s):  
Manzoor Ahmad ◽  
J. Luo ◽  
Ben Xu ◽  
Hendra Purnawali ◽  
Peter King ◽  
...  
2012 ◽  
Vol 2 (2) ◽  
pp. 535-548 ◽  
Author(s):  
Manzoor Ahmad ◽  
Bin Xu ◽  
Hendra Purnawali ◽  
Yongqing Fu ◽  
Weimin Huang ◽  
...  

2012 ◽  
Vol 1403 ◽  
Author(s):  
Sergey Kaloshkin ◽  
Aleksey Maksimkin ◽  
Maria Kaloshkina ◽  
Mihail Zadorozhnyy ◽  
Margarita Churyukanova

ABSTRACTShape memory effect in pure ultra-high molecular weight polyethylene (UHMWPE) has been studied using dynamic mechanical analysis. Temperature dependencies of properties that define functional characteristics of shape memory polymers (SMP) such as recovery stress, recovery strain and activation temperature of transition were determined for UHMWPE. The recovery stress in UHMWPE deformed by 200% achieved rather high values, up to 7 MPa.


2017 ◽  
Vol 75 (5) ◽  
pp. 2181-2196 ◽  
Author(s):  
Tenghui Chen ◽  
Qiuying Li ◽  
Zhiwei Fu ◽  
Lewen Sun ◽  
Weihong Guo ◽  
...  

2010 ◽  
Vol 49 (3) ◽  
pp. 754-761 ◽  
Author(s):  
Dawei Zhang ◽  
Melissa L. Giese ◽  
Stacy L. Prukop ◽  
Melissa A. Grunlan

Author(s):  
Richard B. Vallee

Microtubules are involved in a number of forms of intracellular motility, including mitosis and bidirectional organelle transport. Purified microtubules from brain and other sources contain tubulin and a diversity of microtubule associated proteins (MAPs). Some of the high molecular weight MAPs - MAP 1A, 1B, 2A, and 2B - are long, fibrous molecules that serve as structural components of the cytamatrix. Three MAPs have recently been identified that show microtubule activated ATPase activity and produce force in association with microtubules. These proteins - kinesin, cytoplasmic dynein, and dynamin - are referred to as cytoplasmic motors. The latter two will be the subject of this talk.Cytoplasmic dynein was first identified as one of the high molecular weight brain MAPs, MAP 1C. It was determined to be structurally equivalent to ciliary and flagellar dynein, and to produce force toward the minus ends of microtubules, opposite to kinesin.


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