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1 in subunits in a complex with the eukaryotic cytosolic chaperonin.
2 mutational studies, is unique to eukaryotic cytosolic chaperonins.
4 a- and beta-subunits are partially folded by cytosolic chaperonin, a double-toroidal ATPase with homo
8 are thought to require the assistance of the cytosolic chaperonin CCT and a cochaperone, phosducin-li
12 molecular chaperones, namely prefoldin, the cytosolic chaperonin CCT, and a series of five tubulin-s
16 a result of inefficient interaction with the cytosolic chaperonin, CCT, and, in several cases, a fail
17 n, and Galpha transducin are assisted by the cytosolic chaperonin, CCT, but many other proteins, for
19 , several lines of evidence suggest that the cytosolic chaperonin complex (CCT) may work in concert w
20 n 1 (PhLP1) works as a co-chaperone with the cytosolic chaperonin complex (CCT) to fold Gbeta and med
24 corresponds to the cellular concentration of cytosolic chaperonin complex, a recently described bindi
25 known chaperonin in the eukaryotic cytosol (cytosolic chaperonin containing T-complex polypeptide 1
26 osducin-like protein, a co-chaperone for the cytosolic chaperonin containing tailless complex polypep
30 ences of a defect in Cct4, a subunit of CCT (cytosolic chaperonin-containing t-complex peptide-1), in
32 the hypothesis that PFD, like the eukaryotic cytosolic chaperonin, has co-evolved specifically to fac
33 res two chaperone systems, i.e., the 900 kDa cytosolic chaperonin referred to as the TCP-1 complex or
35 d to bind multiple subunits of the mammalian cytosolic chaperonin TRiC (or CCT), primarily through it
36 identified in the subunits of the eukaryotic cytosolic chaperonin TRiC, a protein machine responsible
37 produced via ATP-dependent interaction with cytosolic chaperonin undergo a sequence of interactions
38 mbly of myosin is mediated by the eukaryotic cytosolic chaperonin with folding of the motor domain as
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