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 ase), but all attempts to demonstrate such a PPIase activity by TWD1 have failed so far.

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

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

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

20 s a conformation in which it uses the WW and PPIase domains to engage two conserved phosphorylated PK

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

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

23 nd functional studies of BfUbb and the BfUbb-PPIase complex uncover a unique disulfide bond at the ca

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

25 ins in SurA activity, we deleted one or both PPIase domains from E.coli SurA and investigated the abi

26 Cellular PPIase Pin1 binds specifically to phosphoserine- or phos

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

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

29 It has a conserved PPIase domain at the C-terminus and a highly charged N-t

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

31 ypD inhibitor, ebselen, using a conventional PPIase assay to screen a library of ~2000 FDA-approved d

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

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

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

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

36 The catalytic domain (PPIase) and the other ligand-binding domain (WW) sample

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

38 (pS/pT-P) canonical motifs and an enzymatic PPIase domain that catalyzes proline cis-trans isomeriza

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

40 in D (CypD), the peptidylprolyl isomerase F (PPIase), is a key component in opening the mitochondrial

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

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

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

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

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

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

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

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

49 genes, produced mutant proteins deficient in PPIase activity.

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

51 (>40 fold), and prolyl isomerase inhibition (PPIase) activity (>200 fold), which is ascribed to a pre

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

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

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

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

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

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

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

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

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

61 P52 comprising its peptidylprolyl isomerase (PPIase) domain.

62 ore domain and two peptidylprolyl isomerase (PPIase) domains, the role(s) of which remain unresolved.

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

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

65 ain and catalyzes peptidyl-prolyl isomerase (PPIase) activity during folding of kinases, nuclear rece

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

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

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

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

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

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

72 bly tethered to a peptidyl-prolyl isomerase (PPIase) domain, resulting in interdomain interactions im

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

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

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

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

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

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

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

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

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

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

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

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

85 ting an essential peptidyl-prolyl isomerase (PPIase).

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

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

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

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

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

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

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

93 ing and peptidyl-prolyl cis-trans isomerase (PPIase) activity.

94 ctional peptidyl-prolyl cis-trans isomerase (PPIase) activity.

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

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

97 nstrate that the prolyl cis-trans isomerase (PPIase) cyclophilin A (CypA) is hijacked by Listeria at

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

99 mily of peptidyl-prolyl cis-trans isomerase (PPIase) enzymes have been shown to be important for viru

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

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

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

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

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

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

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

107 TWD1), a peptidylprolyl cis-trans isomerase (PPIase), but all attempts to demonstrate such a PPIase a

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

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

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

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

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

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

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

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

116 Peptidylprolyl isomerases (PPIases) catalyze cis/trans isomerization of prolines.

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

135 ent tOmpA aggregation does not depend on its PPIase domains, deletion of even a single PPIase domain

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

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

138 90 complex to the nucleus by binding via its PPIase domain to cytoplasmic dynein, the motor protein r

139 verexpressing mutant forms of CyPD that lack PPIase activity.

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

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

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

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

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

145 one reason for the conservation of multiple PPIase domains in SurA in proteobacteria.

146 the S1' binding pocket, leading to potent nM PPIase inhibition and binding.

147 y proteobacteria typically contain one or no PPIase domains, the presence of two PPIase domains is co

148 6, suggesting that the PPIase domain but not PPIase activity is involved in dynein binding.

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

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

151 ndence phenotype for identifying elements of PPIase selectivity.

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

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

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

155 ric chaperone ability, while the presence of PPIase domains enhances its chaperone activity for speci

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

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

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

159 ten showcasing the "undruggable" features of PPIases.

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

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

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

163 Profound effects on PPIase activity were demonstrated in transiently transfe

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

165 BfUbb) that targets an essential periplasmic PPIase to drive intraspecies bacterial competition.

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

167 PPID PPIase activity and C-terminal tetratricopeptide repeats

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

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

170 involved in this protective effect requires PPIase activity.

171 nformation on the activity of individual rER PPIases.

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

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

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

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

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

177 nant BbCypA displayed cyclosporine sensitive PPIase activity.

178 ts PPIase domains, deletion of even a single PPIase domain ablates the ability of SurA to prevent Omp

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

180 The C-terminal domain showed strong PPIase activity, no role in histone chaperoning and reve

181 pansion by SurA, and uncover a role for SurA PPIase domains in limiting the extent of expansion.

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

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

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

185 The PPIase CypA colocalizes with the Parkinson's disease (PD

186 The PPIase domain is positioned along the middle domain, adj

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

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

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

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

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

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

193 d tether Pin1 to a target, which enables the PPIase domain to exert catalytic cis-trans isomerization

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

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

196 ealed a key tyrosine residue (Tyr119) in the PPIase and strains that encode a glutamic acid residue a

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

198 hile FFpSPR binding displaces a helix in the PPIase that leads to repositioning of the PPIase catalyt

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

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

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

202 he PPIase that leads to repositioning of the PPIase catalytic loop.

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

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

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

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

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

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

209 To investigate the role of the PPIase domains in SurA activity, we deleted one or both

210 o mediate the interaction with Tyr119 of the PPIase.

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

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

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

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

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

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

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

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

219 CypA bound Itk via the PPIase active site.

220 omain alters its transient contacts with the PPIase domain via means that are only partially understo

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

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

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

224 ter understand the molecular details of this PPIase with histone chaperoning activity, we have solved

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

226 SurA comprises three domains: a core and two PPIase domains (P1 and P2).

227 ne or no PPIase domains, the presence of two PPIase domains is common in SurA in later proteobacteria

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

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

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

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

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

233 mmon among cell-cycle proteins; thus, the WW-PPIase domain cross-talk mechanisms of Pin1 may be relev