A novel "channel diversity" approach

Author(s):  
I-Tai Lu ◽  
Joon-Sang Choi
Keyword(s):  
Author(s):  
Jiaqi Xu ◽  
Wei Sun ◽  
Kannan Srinivasan

RFID techniques have been extensively used in sensing systems due to their low cost. However, limited by the structural simplicity, collision is one key issue which is inevitable in RFID systems, thus limiting the accuracy and scalability of such sensing systems. Existing anti-collision techniques try to enable parallel decoding without sensing based applications in mind, which can not operate on COTS RFID systems. To address the issue, we propose COFFEE, which enables parallel channel estimation of COTS passive tags by harnessing the collision. We revisit the physical layer design of current standard. By exploiting the characteristics of low sampling rate and channel diversity of RFID tags, we separate the collided data and extract the channels of the collided tags. We also propose a tag identification algorithm which explores history channel information and identify the tags without decoding. COFFEE is compatible with current COTS RFID standards which can be applied to all RFID-based sensing systems without any modification on tag side. To evaluate the real world performance of our system, we build a prototype and conduct extensive experiments. The experimental results show that we can achieve up to 7.33x median time resolution gain for the best case and 3.42x median gain on average.


Author(s):  
Lou Byerly ◽  
Susumu Hagiwara

2014 ◽  
Vol 13 (12) ◽  
pp. 2919-2932 ◽  
Author(s):  
Karthikeyan Sundaresan ◽  
Sampath Rangarajan

Genetics ◽  
1998 ◽  
Vol 148 (3) ◽  
pp. 1159-1169
Author(s):  
Daniel F Eberl ◽  
Dejian Ren ◽  
Guoping Feng ◽  
Lori J Lorenz ◽  
David Van Vactor ◽  
...  

Abstract To begin unraveling the functional significance of calcium channel diversity, we identified mutations in Dmca1D, a Drosophila calcium channel α1 subunit cDNA that we recently cloned. These mutations constitute the l(2)35Fa lethal locus, which we rename Dmca1D. A severe allele, Dmca1DX10, truncates the channel after the IV-S4 transmembrane domain. These mutants die as late embryos because they lack vigorous hatching movements. In the weaker allele, Dmca1DAR66, a cysteine in transmembrane domain I-S1 is changed to tyrosine. Dmca1DAR66 embryos hatch but pharate adults have difficulty eclosing. Those that do eclose have difficulty in fluid-filling of the wings. These studies show that this member of the calcium channel α1 subunit gene family plays a nonredundant, vital role in larvae and adults.


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