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1  folded tubulin in the absence of functional Prefoldin.
2 plexes, and the nutrient sensing complex Uri/Prefoldin.
3 ere they may be substituted by the chaperone prefoldin.
4 ovide evidence for an additional driver gene prefoldin 4 (PFDN4), coregulated genes, conserved noncod
5 e a defective interaction with the chaperone prefoldin, a reduced efficiency in the generation of pro
6 oldin-like complex, which possesses chaperon/prefoldin activities required during protein complex ass
7 protein aggregation, the precise function of prefoldin against protein aggregation under physiologica
8                               In addition to prefoldin and the TCP-1 Ring Complex, five tubulin-speci
9 zation when tubulins are correctly folded by Prefoldin and tubulin destruction when they are not.
10 hose of other chaperones such as Tim9-Tim10, prefoldin, and Skp, in which long helices extend from a
11 very of a heterohexameric chaperone protein, prefoldin, based on its ability to capture unfolded acti
12                                              Prefoldin binds specifically to cytosolic chaperonin (c-
13 ption in the murine Pfdn5 gene, a subunit of prefoldin, causes a syndrome characterized by photorecep
14 in complex TRiC and the functionally related prefoldin complex are all hypersensitive to arsenic comp
15 ldin monoclonal antibody that recognizes the prefoldin complex but not its subunits.
16                                 Although the prefoldin complex containing L110R MM-1alpha was properl
17 ) complex, with the hetero-hexameric Tubulin Prefoldin complex, and with proteins having conserved ro
18 at DELLA proteins directly interact with the prefoldin complex, thus regulating tubulin subunit avail
19 quitin E3 ligase as well as a subunit of the prefoldin complex.
20 fdn1, which encodes the first subunit of the Prefoldin complex.
21  protein associations, especially in the Uri/Prefoldin complex.
22 opies the effects of mutations in mst or the Prefoldin-encoding gene merry-go-round (mgr), leading to
23 nd that knockdown of PFD2 and PFD5 disrupted prefoldin formation in HTT-expressing cells, resulting i
24 re of Skp is unexpectedly similar to that of Prefoldin/GimC, a cytosolic chaperone present in eukaria
25                              Consistent with prefoldin having a general role in chaperonin-mediated f
26 nfer a distinct substrate specificity to the prefoldin holocomplex.
27                                 Knockdown of prefoldin increased the level of SDS-insoluble ubiquitin
28                  These results indicate that prefoldin inhibits elongation of large oligomers of path
29                                              Prefoldin is a hexameric chaperone that facilitates post
30                                              Prefoldin is a molecular chaperone composed of six subun
31  protein aggregation and that dysfunction of prefoldin is one of the causes of neurodegenerative dise
32                Although it is predicted that prefoldin, like other chaperones, modulates protein aggr
33 caffold to coordinate the activities of R2TP/prefoldin-like and HSP90 chaperone complexes during the
34 volved in apoptosis and also to be part of a prefoldin-like cochaperone complex.
35 2 in vitro and is required for the TEL2-R2TP/prefoldin-like complex interaction in vivo.
36  in cells, failure to interact with the R2TP/prefoldin-like complex results in instability of the PIK
37 sphosite of TEL2 confers binding to the R2TP/prefoldin-like complex, which possesses chaperon/prefold
38 SP90 cochaperone hSpagh (RPAP3) and the R2TP/Prefoldin-like complex.
39 creased tubulin instability, indicating that Prefoldin might only be required when tubulins are synth
40  In this study, we first established an anti-prefoldin monoclonal antibody that recognizes the prefol
41            Opposite results were obtained in prefoldin-overexpressed cells.
42  nascent chain-binding chaperones, including prefoldin (PFD) and chaperonin-containing TCP-1 (CCT).
43                                   Eukaryotic prefoldin (PFD) is a heterohexameric chaperone with a je
44 ly identified heteromeric chaperone protein, prefoldin (PFD).
45                                              Prefoldin (PFDN), a ubiquitously expressed heterohexamer
46                   These results suggest that prefoldin plays a role in quality control against protei
47  by directing target proteins to chaperonin, prefoldin promotes folding in an environment in which th
48 PB5 interactor protein) is an unconventional prefoldin, RNA polymerase II interactor that functions a
49 d colleagues demonstrate that unconventional prefoldin RPB5 interactor (URI) expression in hepatocyte
50       We demonstrate that the unconventional prefoldin RPB5 interactor (URI) is a new regulator of AR
51 tocyte-specific expression of unconventional prefoldin RPB5 interactor (URI) leads to a multistep pro
52                          URI (unconventional prefoldin RPB5 interactor protein) is an unconventional
53             We now show that mgr encodes the Prefoldin subunit counterpart of human von Hippel Lindau
54 s, including actin-capping protein genes and prefoldin subunit genes, suppresses dhc-1(or195ts)-induc
55              Deletion of the gene encoding a prefoldin subunit in S. cerevisiae results in a phenotyp
56 ingle molecule observation demonstrated that prefoldin suppressed HTT aggregation at the small oligom
57 tion of several molecular chaperones, namely prefoldin, the cytosolic chaperonin CCT, and a series of
58       Using this antibody, it was found that prefoldin was localized in the cytoplasm with dots in co

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