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1 in subunits in a complex with the eukaryotic cytosolic chaperonin.
2  mutational studies, is unique to eukaryotic cytosolic chaperonins.
3 interaction with cell wall LPS but also with cytosolic chaperonin 60.
4 a- and beta-subunits are partially folded by cytosolic chaperonin, a double-toroidal ATPase with homo
5 eterodimer in vitro depends on the action of cytosolic chaperonin and several protein cofactors.
6              Prefoldin binds specifically to cytosolic chaperonin (c-cpn) and transfers target protei
7 t on folding intermediates downstream of the cytosolic chaperonin CCT (1, 2).
8 are thought to require the assistance of the cytosolic chaperonin CCT and a cochaperone, phosducin-li
9 re, we determined how orphan subunits of the cytosolic chaperonin CCT are recognized.
10                                          The cytosolic chaperonin CCT is a 1-MDa protein-folding mach
11                               The eukaryotic cytosolic chaperonin CCT is an essential ATP-dependent p
12                                          The cytosolic chaperonin CCT was found to bind primarily to
13  molecular chaperones, namely prefoldin, the cytosolic chaperonin CCT, and a series of five tubulin-s
14 rated via ATP-dependent interaction with the cytosolic chaperonin CCT.
15 , we identified components of the eukaryotic cytosolic chaperonin CCT.
16 tide until its posttranslational delivery to cytosolic chaperonin (CCT).
17 a result of inefficient interaction with the cytosolic chaperonin, CCT, and, in several cases, a fail
18 n, and Galpha transducin are assisted by the cytosolic chaperonin, CCT, but many other proteins, for
19                               The eukaryotic cytosolic chaperonin, CCT, plays an essential role in me
20 , several lines of evidence suggest that the cytosolic chaperonin complex (CCT) may work in concert w
21 n 1 (PhLP1) works as a co-chaperone with the cytosolic chaperonin complex (CCT) to fold Gbeta and med
22 motes the interaction between LC3-II and the cytosolic chaperonin complex 2, triggering chaperone-med
23 a high-affinity interaction of PhLP with the cytosolic chaperonin complex appeared unnecessary.
24                                          The cytosolic chaperonin complex chaperonin containing t-com
25       Gene inactivation of components of the cytosolic chaperonin complex that induce increased longe
26 corresponds to the cellular concentration of cytosolic chaperonin complex, a recently described bindi
27  known chaperonin in the eukaryotic cytosol (cytosolic chaperonin containing T-complex polypeptide 1
28 osducin-like protein, a co-chaperone for the cytosolic chaperonin containing tailless complex polypep
29               pVHL formed a complex with the cytosolic chaperonin containing TCP-1 (CCT or TRiC) en r
30                               The eukaryotic cytosolic chaperonin containing TCP-1 (CCT) has an impor
31                         This system includes cytosolic chaperonin containing TCP-1 (CCT; also called
32 onin (TCP1-ring complex, also called CCT for cytosolic chaperonin containing TCP1) facilitates foldin
33 ences of a defect in Cct4, a subunit of CCT (cytosolic chaperonin-containing t-complex peptide-1), in
34 pally actins and tubulins, to the eukaryotic cytosolic chaperonin for facilitated folding.
35 the hypothesis that PFD, like the eukaryotic cytosolic chaperonin, has co-evolved specifically to fac
36 res two chaperone systems, i.e., the 900 kDa cytosolic chaperonin referred to as the TCP-1 complex or
37                              Subunits of the cytosolic chaperonin T-complex 1 (TCP-1) ring complex (T
38 d to bind multiple subunits of the mammalian cytosolic chaperonin TRiC (or CCT), primarily through it
39 identified in the subunits of the eukaryotic cytosolic chaperonin TRiC, a protein machine responsible
40  produced via ATP-dependent interaction with cytosolic chaperonin undergo a sequence of interactions
41 mbly of myosin is mediated by the eukaryotic cytosolic chaperonin with folding of the motor domain as