scholarly journals Enzymatic C‐to‐C Protein Ligation

Author(s):  
Fabian B. H. Rehm ◽  
Tristan J. Tyler ◽  
Simon J. de Veer ◽  
David J. Craik ◽  
Thomas Durek
Keyword(s):  
2022 ◽  
Author(s):  
Fabian B. H. Rehm ◽  
Tristan J. Tyler ◽  
Simon J. de Veer ◽  
David J. Craik ◽  
Thomas Durek
Keyword(s):  

Author(s):  
D. A. Fischman ◽  
J. E. Dennis ◽  
T. Obinata ◽  
H. Takano-Ohmuro

C-protein is a 150 kDa protein found within the A bands of all vertebrate cross-striated muscles. By immunoelectron microscopy, it has been demonstrated that C-protein is distributed along a series of 7-9 transverse stripes in the medial, cross-bridge bearing zone of each A band. This zone is now termed the C-zone of the sarcomere. Interest in this protein has been sparked by its striking distribution in the sarcomere: the transverse repeat between C-protein stripes is 43 nm, almost exactly 3 times the 14.3 nm axial repeat of myosin cross-bridges along the thick filaments. The precise packing of C-protein in the thick filament is still unknown. It is the only sarcomeric protein which binds to both myosin and actin, and the actin-binding is Ca-sensitive. In cardiac and slow, but not fast, skeletal muscles C-protein is phosphorylated. Amino acid composition suggests a protein of little or no αhelical content. Variant forms (isoforms) of C-protein have been identified in cardiac, slow and embryonic muscles.


2021 ◽  
Vol 349 ◽  
pp. 129207
Author(s):  
Séverine Thomas ◽  
Juan-David Vásquez-Benítez ◽  
Fabio-Alexander Cuéllar-Cepeda ◽  
Teresa Mosquera-Vásquez ◽  
Carlos-Eduardo Narváez-Cuenca

2011 ◽  
Vol 47 (16) ◽  
pp. 4742 ◽  
Author(s):  
Yuichi Yamamura ◽  
Hidehiko Hirakawa ◽  
Satoshi Yamaguchi ◽  
Teruyuki Nagamune

2000 ◽  
Vol 65 (1) ◽  
pp. 35-40 ◽  
Author(s):  
Rika Watanabe ◽  
Hideo Wada ◽  
Miho Sakakura ◽  
Yoshitaka Mori ◽  
Takahiro Nakasaki ◽  
...  

Pancreatology ◽  
2013 ◽  
Vol 13 (3) ◽  
pp. S75-S76
Author(s):  
Maria Rachele Angiolini ◽  
Ccristina Ridolfi ◽  
Francesca Gavazzi ◽  
Maria Carla Tinti ◽  
Marco Montorsi ◽  
...  

2004 ◽  
Vol 85 (10) ◽  
pp. 3001-3006 ◽  
Author(s):  
Naoko Miyajima ◽  
Makoto Takeda ◽  
Masato Tashiro ◽  
Koji Hashimoto ◽  
Yusuke Yanagi ◽  
...  

Two nucleotide differences in the P/C/V and M genes between B95a cell- and Vero cell-isolated wild-type measles viruses (MV) have previously been found from the same patient. The nucleotide difference in the P/C/V gene resulted in an amino acid difference (M175I) in the P and V proteins and a 19 aa deletion in the C protein. The nucleotide difference in the M gene resulted in an amino acid difference (P64H) in the M protein. To verify this result and to examine further whether the amino acid difference or truncation is important for MV cell tropism, recombinant MV strains containing one of the two nucleotide substitutions, or both, were generated. It was found that the P64H substitution in the M protein was important for efficient virus growth and dissemination in Vero cells and that the M175I substitution in the P and V protein or truncation of the C protein was required for optimal growth.


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