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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  a network of chaperones, including TRiC and prefoldin.
5                      The molecular chaperone prefoldin 1 (PFDN1) was identified as a novel binding pa
6 ovide evidence for an additional driver gene prefoldin 4 (PFDN4), coregulated genes, conserved noncod
7 e a defective interaction with the chaperone prefoldin, a reduced efficiency in the generation of pro
8 oldin-like complex, which possesses chaperon/prefoldin activities required during protein complex ass
9 protein aggregation, the precise function of prefoldin against protein aggregation under physiologica
10                               In addition to prefoldin and the TCP-1 Ring Complex, five tubulin-speci
11 uted the folding of beta-tubulin using human prefoldin and TRiC.
12 zation when tubulins are correctly folded by Prefoldin and tubulin destruction when they are not.
13 hose of other chaperones such as Tim9-Tim10, prefoldin, and Skp, in which long helices extend from a
14 wide label-free quantification, we find that prefoldin assists in folding ubiquitin-like-modifier-act
15 istinctive open, closed, substrate-bound and prefoldin-associated states of TRiC, and reconstructed i
16 very of a heterohexameric chaperone protein, prefoldin, based on its ability to capture unfolded acti
17 n that is compatible with both substrate and prefoldin binding.
18                                              Prefoldin binds specifically to cytosolic chaperonin (c-
19 ption in the murine Pfdn5 gene, a subunit of prefoldin, causes a syndrome characterized by photorecep
20  "Biperiden" that restricts the formation of Prefoldin complex and inhibits its interaction with its
21 in complex TRiC and the functionally related prefoldin complex are all hypersensitive to arsenic comp
22 esolution mass spectrometry, we identify the prefoldin complex as the top cellular binding partner of
23 ldin monoclonal antibody that recognizes the prefoldin complex but not its subunits.
24                                 Although the prefoldin complex containing L110R MM-1alpha was properl
25                                 The mosquito prefoldin complex is needed to fold proteins and macromo
26 ) complex, with the hetero-hexameric Tubulin Prefoldin complex, and with proteins having conserved ro
27 at DELLA proteins directly interact with the prefoldin complex, thus regulating tubulin subunit avail
28 quitin E3 ligase as well as a subunit of the prefoldin complex.
29 fdn1, which encodes the first subunit of the Prefoldin complex.
30  protein associations, especially in the Uri/Prefoldin complex.
31 opies the effects of mutations in mst or the Prefoldin-encoding gene merry-go-round (mgr), leading to
32 IP-MS to probe the organization of the human prefoldin family of complexes, resolving distinct prefol
33 nd that knockdown of PFD2 and PFD5 disrupted prefoldin formation in HTT-expressing cells, resulting i
34 ly thermophilic archaea, including the gamma prefoldin (gammaPFD) in the deep-sea methanogen Methanoc
35 ronin TRiC/CCT cooperates with the chaperone prefoldin/GIMc (PFD), we integrate cryoelectron microsco
36 re of Skp is unexpectedly similar to that of Prefoldin/GimC, a cytosolic chaperone present in eukaria
37                              Consistent with prefoldin having a general role in chaperonin-mediated f
38 ldin family of complexes, resolving distinct prefoldin holo- and subcomplex variants, complex-complex
39 nfer a distinct substrate specificity to the prefoldin holocomplex.
40 roaches, we establish functions for TRiC and prefoldin in folding o3 and promoting its assembly into
41                                 Knockdown of prefoldin increased the level of SDS-insoluble ubiquitin
42                  These results indicate that prefoldin inhibits elongation of large oligomers of path
43                                              Prefoldin is a hexameric chaperone that facilitates post
44                                              Prefoldin is a molecular chaperone composed of six subun
45  protein aggregation and that dysfunction of prefoldin is one of the causes of neurodegenerative dise
46 P3 interferes with the chaperone activity of prefoldin, leading to unstable UBA3, reduces IRF9, and s
47                Although it is predicted that prefoldin, like other chaperones, modulates protein aggr
48 caffold to coordinate the activities of R2TP/prefoldin-like and HSP90 chaperone complexes during the
49 ma cell survival through engagement with the prefoldin-like chaperone complex.
50                      WDR92 associates with a prefoldin-like cochaperone complex and known dynein asse
51 volved in apoptosis and also to be part of a prefoldin-like cochaperone complex.
52 2 in vitro and is required for the TEL2-R2TP/prefoldin-like complex interaction in vivo.
53  in cells, failure to interact with the R2TP/prefoldin-like complex results in instability of the PIK
54 sphosite of TEL2 confers binding to the R2TP/prefoldin-like complex, which possesses chaperon/prefold
55 SP90 cochaperone hSpagh (RPAP3) and the R2TP/Prefoldin-like complex.
56 creased tubulin instability, indicating that Prefoldin might only be required when tubulins are synth
57  In this study, we first established an anti-prefoldin monoclonal antibody that recognizes the prefol
58            Opposite results were obtained in prefoldin-overexpressed cells.
59 insight into the mechanism by which TRiC and prefoldin participate in the assembly of protein complex
60  nascent chain-binding chaperones, including prefoldin (PFD) and chaperonin-containing TCP-1 (CCT).
61 aperonin TRiC/CCT partners with cochaperones prefoldin (PFD) and phosducin-like proteins (PhLPs) to f
62                                   Eukaryotic prefoldin (PFD) is a heterohexameric chaperone with a je
63 ly identified heteromeric chaperone protein, prefoldin (PFD).
64                                              Prefoldin (PFDN), a ubiquitously expressed heterohexamer
65 e show that the conserved Anopheles mosquito prefoldin (PFDN)-chaperonin system is a potent transmiss
66 unfolded protein response pathways involving Prefoldins (PFDs).
67                   These results suggest that prefoldin plays a role in quality control against protei
68  by directing target proteins to chaperonin, prefoldin promotes folding in an environment in which th
69 PB5 interactor protein) is an unconventional prefoldin, RNA polymerase II interactor that functions a
70 d colleagues demonstrate that unconventional prefoldin RPB5 interactor (URI) expression in hepatocyte
71       We demonstrate that the unconventional prefoldin RPB5 interactor (URI) is a new regulator of AR
72 tocyte-specific expression of unconventional prefoldin RPB5 interactor (URI) leads to a multistep pro
73 lifying (TA) cells, marked by unconventional prefoldin RPB5 interactor (URI), control R-spondin produ
74                          URI (unconventional prefoldin RPB5 interactor protein) is an unconventional
75             We now show that mgr encodes the Prefoldin subunit counterpart of human von Hippel Lindau
76 s, including actin-capping protein genes and prefoldin subunit genes, suppresses dhc-1(or195ts)-induc
77              Deletion of the gene encoding a prefoldin subunit in S. cerevisiae results in a phenotyp
78 virus infection is significantly enhanced in prefoldin subunit knockout cells.
79                                Silencing any prefoldin subunit or its CCT/TRiC partner via RNA interf
80   Here, we functionally characterized all Pf Prefoldin subunits (PFD1-6) and established a causative
81 ingle molecule observation demonstrated that prefoldin suppressed HTT aggregation at the small oligom
82 tion of several molecular chaperones, namely prefoldin, the cytosolic chaperonin CCT, and a series of
83 nd unstructured beta-tubulin is delivered by prefoldin to the open TRiC chamber followed by ATP-depen
84    Our findings report a novel function of a prefoldin-UBA3-IRF9-ISG axis in antiviral immunity and u
85       Using this antibody, it was found that prefoldin was localized in the cytoplasm with dots in co