ライフサイエンスコーパス: PPIase

1 PPIase activity is necessary for Ess1/Pin1 function in y

2 PPIase inhibition led to failure of hensin polymerizatio

3 PPIases are important in protein folding, assembly and/o

4 PPIases catalyze the cis/trans isomerization of proline,

5 Of the 13 PPIases in Saccharomyces cerevisiae only Ess1, a parvuli

6 l cis-trans-isomerase (PPIase) activity by a PPIase assay and the allergenic property by an IgE-speci

7 CyP33 contains a PPIase and a RRM domain and regulates MLL1 function thro

8 Employing the cyclophilin A PPIase together with its biologically relevant and nativ

9 Here we show that cyclophilin 40 (CyP40), a PPIase, dissolves tau amyloids in vitro.

10 acking both parvulin-like domains exhibits a PPIase-independent chaperone-like activity in vitro and

11 formation and CyP-A binds to dynamitin in a PPIase domain-dependent manner.

12 and they bind rabbit cytoplasmic dynein in a PPIase domain-specific manner.

13 ROC1 suppresses RPM1 immunity in a PPIase-dependent manner.

14 nctional NifH component of nitrogenase, is a PPIase.

15 to dynein is competed for by expression of a PPIase domain fragment in the same manner as when dynein

16 m, which encodes a periplasmic chaperone and PPIase, suggesting that NlpB and YraP play roles in a pe

17 drawal of colcemid, microtubules reform, and PPIase inhibition of GFP-GR movement is restored.

18 Interestingly, both FKBP51 TPR and PPIase domains are required for its interaction with TRA

19 nct mechanistic and biological links between PPIase and chaperone activities of Ranbp2 cyclophilin to

20 The results forge a strong link between PPIases and the transcription machinery and suggest a ne

21 ding FK506, rapamycin, and cyclosporin, bind PPIases with nanomolar or better affinity.

22 Cellular PPIase Pin1 binds specifically to phosphoserine- or phos

23 myces cerevisiae only Ess1, a parvulin-class PPIase, is essential for growth.

24 e that cyclophilin A, one of the most common PPIases, provides a catalytic environment that acts on t

25 ribosome, a central domain II that contains PPIase activity, and a C-terminal domain III.

26 embers of two other families of conventional PPIases, cyclophilins and FKBPs (FK-506 binding proteins

27 export, and a biological function for Cpr1p PPIase activity.

28 own that Pin1 is a phosphorylation-dependent PPIase that can recognize specifically the phosphorylate

29 here shown to be a phosphorylation-dependent PPIase that specifically recognizes the phosphoserine-pr

30 Furthermore, deletion of the entire PPIase domain did not significantly affect growth or Hsp

31 Pin1 is thus an essential PPIase that regulates mitosis presumably by interacting

32 al form in the absence of the trigger factor PPIase homolog RopA, and its translocation is delayed wh

33 ence WEYIPNV and NFTLKFWDIFRK with the first PPIase domain of the Escherichia coli SurA protein at 1.

34 cotransfection of 3T3 cells with the FKBP52 PPIase domain and a green fluorescent protein (GFP) gluc

35 Inhibition of movement by the FKBP52 PPIase domain is abrogated in cells treated with colcemi

36 depletion of FKBP65 and inhibition of FKBP65 PPIase activity reduced the dimeric (active) form of LH2

37 ase prodomain suppressed the requirement for PPIase activity, suggesting that this residue is the tar

38 hat reflects the coding sequence of the four PPIase, or FK506-binding, domains present in the mature

39 It is also unclear if PPIase and chaperone activities reflect distinct cycloph

40 genes, produced mutant proteins deficient in PPIase activity.

41 t BPSS1823 protein has rapamycin-inhibitable PPIase activity, indicating that it is a functional FKBP

42 type but not mutant FKBP65 that lacks intact PPIase domains.

43 y catalyzed by full-length Pin1 and isolated PPIase domain.

44 mutations in the prolyl-peptidyl isomerase (PPIase) motif of CyPA and demonstrated a critical role o

45 nteracts with the prolyl-peptidyl isomerase (PPIase) ROC1, which is reduced upon RIN4 Thr166 phosphor

46 ophilin possessing peptidylprolyl isomerase (PPIase) activity that is inhibited by the immunosuppress

47 otes, that exhibit peptidylprolyl isomerase (PPIase) activity.

48 indirectly via its peptidylprolyl isomerase (PPIase) domain with cytoplasmic dynein, a motor protein

49 f the immunophilin peptidylprolyl isomerase (PPIase) domain with dynamitin, a component of the dynein

50 sess the signature peptidylprolyl isomerase (PPIase) domain, but no role for their PPIase activity in

51 P52 comprising its peptidylprolyl isomerase (PPIase) domain.

52 otein, a cis-trans peptidylprolyl isomerase (PPIase), copurifies with AC7 C1b (7C1b).

53 hibitor that binds to the proline isomerase (PPIase) domain of Fpr3.

54 e postulated that peptidyl prolyl isomerase (PPIase) activity of FKBP65 positively modulates LH2 enzy

55 A (CyPA) and its peptidyl-prolyl isomerase (PPIase) activity play an essential role in hepatitis C v

56 n chaperones with peptidyl-prolyl isomerase (PPIase) activity.

57 les for the PrsA2 peptidyl-prolyl isomerase (PPIase) and the N- and C-terminal domains in pathogenesi

58 The peptidyl-prolyl isomerase (PPIase) cyclophilin A (Cpr1p) is conserved from eubacter

59 rted by the first peptidyl-prolyl isomerase (PPIase) domain of SurA.

60 he characteristic peptidyl-prolyl isomerase (PPIase) domain, whereas three copies of the tetratricope

61 nhibited the Pin1 peptidyl-prolyl isomerase (PPIase) enzymatic activity.

62 e ligands for the peptidyl-prolyl isomerase (PPIase) FKBP12 possess powerful neuroprotective and neur

63 The Ess1/Pin1 peptidyl-prolyl isomerase (PPIase) is thought to control mitosis by binding to cell

64 Human peptidyl-prolyl isomerase (PPIase) Pin1 plays key roles in developmental processes,

65 how here that the peptidyl-prolyl isomerase (PPIase) Pin1 promoted the stability of TGF-beta1 mRNA in

66 coli periplasmic peptidyl-prolyl isomerase (PPIase) SurA is involved in the maturation of outer memb

67 (CypA/Ppia) is a peptidyl-prolyl isomerase (PPIase) that binds the immunosuppressive drug cyclospori

68 a novel essential peptidyl-prolyl isomerase (PPIase) that inhibits entry into mitosis and is also req

69 conserved mitotic peptidyl-prolyl isomerase (PPIase) that is distinct from members of two other famil

70 highly conserved peptidyl prolyl isomerase (PPIase) that selectively eliminates Rbf(-) cells from th

71 philin A (CpA), a peptidyl-prolyl isomerase (PPIase).

72 e has a peptidyl-prolyl cis-trans isomerase (PPIase) activity that catalyzes the rate-limiting prolin

73 th have peptidyl prolyl cis/trans isomerase (PPIase) activity that is involved in protein folding pro

74 exhibit peptidylprolyl cis-trans isomerase (PPIase) activity which is inhibitable by the immunosuppr

75 romises peptidyl-prolyl cis-trans isomerase (PPIase) activity, we demonstrate that the mechanism invo

76 ns, with peptidylprolyl cis-trans isomerase (PPIase) activity.

77 possess peptidyl-prolyl cis/trans isomerase (PPIase) activity.

78 share a peptidyl prolyl cis-trans isomerase (PPIase) activity.

79 ssesses peptidyl-prolyl cis-trans isomerase (PPIase) and chaperone functions) and ADAMTS13 is demonst

80 nserved peptidyl-prolyl cis-trans isomerase (PPIase) best known as the cellular receptor of the immun

81 n and a peptidyl-prolyl cis-trans isomerase (PPIase) domain, prevents tau clearance and regulates its

82 of the peptidyl-prolyl cis-trans isomerase (PPIase) family.

83 H) 2 or peptidyl-prolyl cis-trans isomerase (PPIase) FKBP65.

84 d by the peptidylprolyl cis-trans isomerase (PPIase) inhibitors cyclosporin A (CsA) and a derivative

85 Peptidyl prolyl cis-trans isomerase (PPIase) interacting with NIMA-1 (Pin1) catalyzes the cis

86 s1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that binds to the carboxy-terminal domain (CTD)

87 e and a peptidyl prolyl cis-trans isomerase (PPIase) that contributes to the virulence of the Gram-po

88 Pin1, a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA.

89 ellular peptidyl-prolyl cis-trans isomerase (PPIase), cyclophilin B (CyPB), is critical for the effic

90 one and peptidyl-prolyl cis-trans isomerase (PPIase), is essential for the secretion and maturation o

91 BP-type peptidyl-prolyl cis-trans isomerase (PPIase).

92 ossesses peptidylprolyl cis/trans-isomerase (PPIase) activity and is a component of a subclass of ste

93 confirm peptidyl-prolyl cis-trans-isomerase (PPIase) activity by a PPIase assay and the allergenic pr

94 and has peptidylproline cis-trans-isomerase (PPIase) activity.

95 Ps) are peptidyl-prolyl cis/trans isomerases PPIases) that bind the immunosuppressive drug FK506.

96 ands for the peptidyl and prolyl isomerases (PPIase) of FKBP12 have been shown to possess powerful ne

97 Peptidyl-proline isomerases (PPIases) are a chaperone superfamily comprising the FK50

98 Peptidyl-prolyl isomerases (PPIases) are emerging as key regulators of many diverse

99 Peptidyl-prolyl isomerases (PPIases) are ubiquitous cellular enzymes that play roles

100 hat functions as peptidyl-prolyl isomerases (PPIases) in protein folding.

101 (FKBP) family of peptidyl-prolyl isomerases (PPIases) is characterized by a common catalytic domain t

102 ted by cis/trans peptidyl-prolyl isomerases (PPIases).

103 Prolyl-isomerases (PPIases) are found in all organisms and are important fo

104 Peptidyl prolyl cis-trans isomerases (PPIases) are ubiquitous enzymes in biology that catalyze

105 Peptidyl-prolyl cis/trans isomerases (PPIases) play a pivotal role in catalyzing the correct f

106 sident peptidyl prolyl cis/trans isomerases (PPIases) play an important role in the zipper-like tripl

107 ing to peptidyl-prolyl cis/trans isomerases (PPIases).

108 ymes, known as "peptidyl-prolyl isomerases" (PPIases), catalyze this reaction, which involves the int

109 perone, cis/trans peptidyl prolyl isomerise (PPIase) and involved in various other metabolic pathways

110 yze peptidyl cis-trans prolyl-isomerization (PPIase), a rate-limiting step in protein folding and a c

111 ing peptidyl-prolyl cis-trans isomerization (PPIase activity) and functioning in diverse cellular pro

112 th a purified FKBP52 fragment comprising its PPIase domain but is not affected by the immunosuppressa

113 peted by a fragment of FKBP52 containing its PPIase domain, but not by a TPR domain fragment that blo

114 rified FKBP52 binds directly by means of its PPIase domain to purified dynamitin.

115 e active sites of SlyD, which suppresses its PPIase and chaperone activities.

116 Fpr3 interacts with PP1 through its PPIase domain, regulates PP1 localization, and counterac

117 90 complex to the nucleus by binding via its PPIase domain to cytoplasmic dynein, the motor protein r

118 verexpressing mutant forms of CyPD that lack PPIase activity.

119 Moreover, CyP40 lacking PPIase activity prevented its capacity for disaggregatio

120 ROC1 mutants lacking PPIase enzymatic activity were unable to activate AvrRpt

121 cture domains and cellular localization make PPIases a versatile superfamily of proteins that clearly

122 tein, raising the possibility that mammalian PPIase may regulate enzymatic activity of mammalian aden

123 omains of Pin1 bind the pSer/pThr-Pro motif; PPIase enzymatic activity occurs in the catalytic domain

124 6, suggesting that the PPIase domain but not PPIase activity is involved in dynein binding.

125 Pin1 is nuclear PPIase containing a WW protein interaction domain, and i

126 is critical when interpreting the effects of PPIase mutations in biological assays.

127 ndence phenotype for identifying elements of PPIase selectivity.

128 equired for catalysis, showed a low level of PPIase activity that was unaffected on reduction by Trx.

129 of the mPTP, is not affected by the loss of PPIase activity.

130 have experienced gene elongation by means of PPIase domain duplication.

131 Elucidating the role of PPIase activity in vivo has been challenging because mut

132 hilin A, is a member of a distinct family of PPIases that are targets of immuno suppressive drugs.

133 Parvulins represent another family of PPIases that are unrelated to immunophilins in protein s

134 ten showcasing the "undruggable" features of PPIases.

135 and ongoing challenges in the inhibition of PPIases, with a focus on how natural products might info

136 A complete understanding of the mechanism of PPIases is still lacking, and current experimental techn

137 However, the active site of PPIases is shallow, solvent-exposed, and well conserved

138 ism that we describe here is common to other PPIases and, more generally, in characterizing other enz

139 Both proteins possess PPIase homology domains, and co-immunoadsorption of cyto

140 e, an absolute in vivo requirement for PrsA2 PPIase activity is evident in mouse infection models.

141 Mutant forms of SlyD with reduced PPIase activity are less potent in the inhibition of AC7

142 involved in this protective effect requires PPIase activity.

143 nformation on the activity of individual rER PPIases.

144 rved changes in activity of six rER-resident PPIases, cyclophilin B (encoded by the PPIB gene), FKBP1

145 nuclei contains predominantly CsA-resistant PPIase activity, the corresponding activity in the nucle

146 f HCV and identify a critical role of CyPA's PPIase activity in the proper assembly and function of t

147 formation of extensive contacts between TF's PPIase domain and the Arm 1 domain that is involved in n

148 ptide and a SurA fragment lacking the second PPIase domain at 3.4 A resolution, have been solved.

149 nant BbCypA displayed cyclosporine sensitive PPIase activity.

150 of a model for the specific role of the SlyD PPIase in E folding, and of the use of the very strict S

151 Mip and the first indication that a surface PPIase is involved in the secretion or activation of pro

152 he solution structure of the Fpr4 C-terminal PPIase domain by using NMR spectroscopy.

153 , and psychiatric disorders, suggesting that PPIase inhibitors could be important therapeutics.

154 ated the effects of mutations that alter the PPIase domain of the Saccharomyces cerevisiae CyP-40 hom

155 y blocking this critical interaction and the PPIase activity of CyPA.

156 proteins, we show that FKBP52, PP5, and the PPIase domain fragment bind directly to the intermediate

157 ired for forming the dynein complex, but the PPIase domain fragment of FKBP52 blocks complex formatio

158 toplasmic dynein with each is blocked by the PPIase domain fragment of FKBP52.

159 c dynein in a manner that is competed by the PPIase domain of FKBP52.

160 binding to Hsp90, but a requirement for the PPIase domain has not been established.

161 The functional role for the PPIase domain in receptor movement was demonstrated by s

162 on Lys6 in the WW domain and on Lys63 in the PPIase domain.

163 hensin, suggesting that cyclophilin A is the PPIase that mediates the polymerization and matrix assem

164 the antigenic surface particularly near the PPIase active site, which supports the pronounced cross-

165 Because neither the PPIase fragment nor the TPR fragment affects the binding

166 p90 activity, a functional assessment of the PPIase domain could be performed in vivo.

167 nein and microtubules, and expression of the PPIase domain fragment of FKBP52 in 3T3 cells disrupts i

168 monstrated by showing that expression of the PPIase domain fragment of FKBP52 in 3T3 cells inhibits d

169 ubules is disrupted by overexpression of the PPIase domain fragment.

170 The active site of the PPIase domain is occupied by a loop from domain III, sug

171 The exon organization of the PPIase domains differs from that of the other FKBP famil

172 Regulation of the latter is dependent on the PPIase activity of FKBP51.

173 ules with tau in a reaction depending on the PPIase activity of FKBP51.

174 that, while not required for targeting, the PPIase activity of trigger factor is essential for matur

175 a loop from domain III, suggesting that the PPIase activity of the protein could be regulated.

176 osuppressant drug FK506, suggesting that the PPIase domain but not PPIase activity is involved in dyn

177 We find that the PPIase domain of CyP33 regulates the conformation of MLL

178 We conclude that the PPIase domains of the hsp90-binding immunophilins intera

179 ployed a yeast two-hybrid strategy using the PPIase domain (domain I) as bait to screen a neonatal ra

180 CypA bound Itk via the PPIase active site.

181 erase (PPIase) domain, but no role for their PPIase activity in protein folding has been demonstrated

182 ins to p53-bound hsp90 and by means of their PPIase domains to the dynein complex.

183 estigated the substrate preferences of these PPIases in vitro using type III collagen, the unhydroxyl

184 to dissect residue-specific contributions to PPIase catalysis versus substrate binding utilizing NMR

185 -type histone deacetylases and the FKBP-type PPIases may have evolved from a common ancestor enzyme.

186 ophilin), or Fpr1p (a structurally unrelated PPIase).

187 nel of cyclophilin A mutants correlated with PPIase activity, confirming the relevance of this activi

188 s, and rescue of this defect correlated with PPIase activity.

189 erone and with (Tg-Ranbp2(WT-HA)) or without PPIase activities (Tg-Ranbp2(R2944A-HA)).