Chaperonin-containing TCP-1 complex directly binds to the cytoplasmic domain of the LOX-1 receptor
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چکیده
منابع مشابه
Horovitz containing TCP - 1 Nested allosteric interactions in the cytoplasmic chaperonin
Initial rates of ATP hydrolysis by the chaperonin containing TCP-1 (CCT) from bovine testis were measured as a function of ATP concentration. Two allosteric transitions are observed: one at relatively low concentrations of ATP (<100 M) and the second at higher concentrations of ATP. The data suggest that CCT has positive intra-ring cooperativity and negative inter-ring cooperativity in ATP hydr...
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We have cloned a novel Tcp-1-related mouse testis cDNA encoding a polypeptide of 531 amino acids which shares 81.2% identity with the zeta subunit of the mouse cytosolic chaperonin-containing TCP-1 (CCT). Immunoblot analysis of mouse testis CCT subunits separated by 2-dimensional gel electrophoresis indicates that this novel gene, Cctz-2, encodes a CCT subunit of Mr 57 000 and pI 7.1. Cctz-2 mR...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2014
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2014.04.049