PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12502735-3 2002 Here we report that HDAC3 interacts with SMRT only after priming by cellular chaperones including the TCP-1 ring complex (TRiC), which is required for proper folding of HDAC3 in an ATP-dependent process. Adenosine Triphosphate 181-184 t-complex 1 Homo sapiens 102-107 7919008-6 1994 Side views from different forms of TCP-1 reveals that upon Mg-ATP binding, the cytoplasmic chaperonin undergoes a structural rearrangement that is confirmed using a new classification method. Adenosine Triphosphate 59-65 t-complex 1 Homo sapiens 35-40 11483510-3 2001 Here we find that upon ATP binding, mimicked by the non-hydrolysable analog AMP-PNP (5"-adenylyl-imido-diphosphate), to both CCT-alpha-actin and CCT- beta-tubulin complexes, the chaperonin component undergoes concerted movements of the apical domains, resulting in the cavity being closed off by the helical protrusions of the eight apical domains. Adenosine Triphosphate 23-26 t-complex 1 Homo sapiens 125-134