The role of g9/2 intruder state in the nuclear matrix elements of 76Ge → 76Se 2νββ(0+ → 0+) decay

2016 ◽  
Author(s):  
J. P. Valencia
2011 ◽  
Author(s):  
R. Chandra ◽  
K. Chaturvedi ◽  
P. K. Rath ◽  
P. K. Raina ◽  
S. K. Singh ◽  
...  

1997 ◽  
Vol 394 (1-2) ◽  
pp. 23-28 ◽  
Author(s):  
Hidetoshi Akimune ◽  
Hiroyasu Ejiri ◽  
Mamoru Fujiwara ◽  
Izuru Daito ◽  
Toru Inomata ◽  
...  

2009 ◽  
Vol 79 (5) ◽  
Author(s):  
Fedor Šimkovic ◽  
Amand Faessler ◽  
Herbert Müther ◽  
Vadim Rodin ◽  
Markus Stauf

2015 ◽  
Vol 93 ◽  
pp. 01055
Author(s):  
N. Yoshinaga ◽  
K. Higashiyama ◽  
D. Taguchi ◽  
E. Teruya

1994 ◽  
Vol 107 (10) ◽  
pp. 2851-2859
Author(s):  
E.C. Joly ◽  
E. Tremblay ◽  
R.M. Tanguay ◽  
Y. Wu ◽  
V. Bibor-Hardy

We have recently reported the cloning of a novel protein, TRiC-P5, with significant homology with protein 1 of the t-complex (TCP1). In the present study, the cellular localization of TRiC-P5 in Raji cells has been determined using an antiserum raised against a 18.5 kDa fusion protein. Results from cell fractionation and immunoblot studies indicate that TRiC-P5 is mainly localized in the cytoplasm. In addition, a significant part of TRiC-P5 is also found in the nucleus where it is attached to the nuclear matrix, a complex filament network involved in essential cellular functions such as DNA replication, and RNA transcription and maturation. Immunofluorescence experiments using the anti-TRiC-P5 antibodies confirm these results. We also provide evidence that, in the cytoplasm, TRiC-P5 is part of a large protein complex, most probably the TCP1-ring complex (TRiC), a hetero-oligomeric ring complex that plays a role of molecular chaperone in the folding of actin and tubulin.


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