ライフサイエンスコーパス: prolyl isomerase

1 conversion of which is catalysed by the Pin1 prolyl isomerase.

2 Rhodanese-like domain homologous to that of prolyl isomerase.

3 on in some proteins is catalysed by the Pin1 prolyl isomerase.

4 interaction with Pin1, a member of peptidyl-prolyl isomerase.

5 (3)) to catalysis by cyclophilin, a peptidyl-prolyl isomerase.

6 D (Cyp-D) is a mitochondrial matrix peptidyl-prolyl isomerase.

7 ce of human and periplasmic E. coli peptidyl-prolyl isomerase.

8 from the sensitivity of its rate to peptidyl prolyl isomerase.

9 e-specific binding protein and a nonspecific prolyl isomerase.

10 investigated the folding kinetics of FKBP, a prolyl isomerase.

11 a ubiquitously expressed cis-trans peptidyl-prolyl isomerase.

12 lding kinetics in the presence of a peptidyl prolyl isomerase.

13 by increased expression of Pin1, a peptidyl-prolyl isomerase.

14 erentiated ligands of human Pin1, a peptidyl-prolyl isomerase.

15 ns, is accelerated by the action of peptidyl-prolyl isomerases.

16 urA are the four known periplasmic cis-trans prolyl isomerases.

17 g experiments, and is unaffected by peptidyl-prolyl isomerases.

18 her is prevented by an inhibitor of peptidyl-prolyl isomerases.

19 embers of the cyclophilin family of peptidyl-prolyl isomerases.

20 nuclease T1, whose folding is accelerated by prolyl isomerases.

21 of prolyl residues, a reaction catalyzed by prolyl isomerases.

22 pregulation of other chaperones and peptidyl-prolyl isomerases.

23 gnaling since cyclophilins are also peptidyl-prolyl isomerases.

24 equired for an interaction with the peptidyl prolyl isomerase 1 (Pin1), a critical component of PDPK-

25 We demonstrate here that peptidyl-prolyl isomerase 1 (Pin1), which catalyzes the isomeriza

26 lymorphisms (SNPs) in the region of peptidyl-prolyl isomerase A (PPIA) that encodes CypA on HCV infec

27 er binding properties at the remote peptidyl-prolyl isomerase active site.

28 report that in addition to its known histone prolyl isomerase activities, the Fpr4 FKBP domain binds

29 tant enzymes exhibited substantial levels of prolyl isomerase activity (5-20% of wild-type), revealin

30 Although all immunophilins possess peptidyl-prolyl isomerase activity and are identified from a wide

31 important in protein folding, because TF has prolyl isomerase activity and associates with nascent po

32 Our findings provide evidence that both prolyl isomerase activity and other structural features

33 mically that the CTD possesses weak peptidyl-prolyl isomerase activity and show that the active-site

34 m of action of CyPA is likely to involve its prolyl isomerase activity because a mutant CyPA with a s

35 Additionally mimicyp lacks peptidyl-prolyl isomerase activity in contrast to human cyclophil

36 tant role for CyPA and enzymes with peptidyl-prolyl isomerase activity in the pathogenesis of vascula

37 e mutant enzymes had little or no detectable prolyl isomerase activity in the standard peptide substr

38 These molecules exhibit peptidyl-prolyl isomerase activity in vitro, suggesting that they

39 Prolyl isomerase activity is not required for forming th

40 The peptidyl-prolyl isomerase activity is required for ERK1/2 activat

41 tion and that the classic in vitro assay for prolyl isomerase activity may be misleading.

42 alytic activity is inhibited by the peptidyl prolyl isomerase activity of cyclophilin A (CypA).

43 be abrogated by the removal of the peptidyl-prolyl isomerase activity of cyclophilin B.

44 The peptidyl-prolyl isomerase activity of CYP-5 has been characterise

45 how that rapamycin, a drug that inhibits the prolyl isomerase activity of FKBP and dissociates FKBP f

46 uires both the Hsp90-binding ability and the prolyl isomerase activity of FKBP52.

47 2A show reciprocal genetic interactions, and prolyl isomerase activity of Pin1 is essential for cell

48 KBP12 and an F43Y FKBP12 mutant with reduced prolyl isomerase activity supported mdr3 function.

49 ecombinant TvCyP1 exhibited typical peptidyl-prolyl isomerase activity with kcat/Km of approximately

50 at SurA, a periplasmic protein with peptidyl-prolyl isomerase activity, is involved in the maturation

51 (CyP A), a cellular chaperone with cis-trans prolyl isomerase activity, is required for postassembly

52 While both have peptidyl-prolyl isomerase activity, this is not required for pote

53 e in CA that is independent of its cis-trans prolyl isomerase activity.

54 e altered by CyP A binding and/or by CyP A's prolyl isomerase activity.

55 BPs); immunophilins, with cis-trans peptidyl-prolyl isomerase activity.

56 inhibited by FK506, an inhibitor of the FKBP prolyl isomerase activity.

57 chaperone with remarkable properties: it has prolyl-isomerase activity, associates with nascent polyp

58 alled Ppif), a mitochondrial matrix peptidyl prolyl isomerase and apoptosis regulator, results in inc

59 Cyclophilin A is a peptidyl-prolyl isomerase and is widely expressed in a multitude

60 es a homologue of Trigger Factor, a peptidyl-prolyl isomerase and putative chaparone which is highly

61 Here we show that TaPIN1 is a bona fide prolyl isomerase and that it interacts with the host ubi

62 rther show interactions between the peptidyl-prolyl isomerase and Trp-Trp (WW) domains amplify the co

63 secretion of two proteins: cypA (a cis-trans prolyl isomerase) and galectin 3.

64 ion between Pin1, a phosphorylation-specific prolyl isomerase, and phosphorylated histone H1.

65 cascade involving GSK3beta kinase, the Pin1 prolyl isomerase, and the PP2A-B56alpha phosphatase cont

66 Calstabin2, an 11.8-kDa cis-trans peptidyl-prolyl isomerase (apparent molecular mass 12.6 kDa), sta

67 However, since prolyl isomerases are often believed to be constitutivel

68 ozygous start-codon mutation in the peptidyl-prolyl isomerase B gene (PPIB), which results in a lack

69 SurA is a periplasmic prolyl isomerase/chaperone that facilitates outer membra

70 widely distributed cyclophilin and peptidyl-prolyl isomerase, could inhibit c-Myb DNA binding activi

71 The peptidyl-prolyl isomerase cyclophilin A (CypA) binds a proline-ri

72 ration into virions of the cellular peptidyl-prolyl isomerase cyclophilin A (CyPA) by the Gag polypro

73 The peptidyl-prolyl isomerase cyclophilin A (CypA) embraces an expose

74 The peptidyl-prolyl isomerase cyclophilin A (CypA) increases the kine

75 HIV-1 specifically incorporates the peptidyl prolyl isomerase cyclophilin A (CyPA), the cytosolic rec

76 ifically incorporates the host cell peptidyl-prolyl isomerase cyclophilin A into virions via contacts

77 The cellular peptidyl-prolyl isomerase cyclophilin A is incorporated into huma

78 in a manner similar to that of the peptidyl-prolyl isomerase cyclophilin A, we probed purified virio

79 ecular Cell reveals a role for the host cell prolyl isomerase cyclophilin B (CyPB) in the replication

80 ATP synthase dimer may involve the peptidyl prolyl isomerase cyclophilin D.

81 emperature and are weakly accelerated by the prolyl isomerase cyclophilin.

82 ssential interaction with the human peptidyl prolyl isomerase, cyclophilin A (CypA), that results in

83 ening, by testing the effect of the peptidyl-prolyl isomerase, cyclophilin A, on the CFTR channel.

84 Capsid also binds the human peptidyl prolyl isomerase, cyclophilin A, thereby packaging the e

85 cellular function of the ubiquitous peptidyl prolyl isomerase, CypA.

86 receptors, red/green opsins, upon cis-trans prolyl isomerase-dependent and direct modification of op

87 and contains two domains, an amino-terminal prolyl isomerase domain and a carboxy-terminal tetratric

88 less than 0.0005, and mutants of Pin1 in the prolyl isomerase domain are not active.

89 ter function was dependent upon the peptidyl-prolyl isomerase domain of RopA and mutants that lacked

90 sA reveals a central catalytic parvulin-type prolyl isomerase domain, which is inserted into a larger

91 cyclophilin B, which contained its peptidyl-prolyl isomerase domain; this cyclophilin fragment repre

92 506-binding protein with an inactive peptide prolyl-isomerase domain that binds DOUBLETIME and tetrat

93 Here, we report that the Pin1 prolyl isomerase enhances recruitment of serine 62-phosp

94 The presence of the peptidyl-prolyl isomerase enzyme, Pin1, does not affect dephospho

95 Thus, a subclass of FKBP prolyl isomerase enzymes is recruited to linker regions

96 Here, we show that the prolyl isomerase Ess1 is required for Nrd1-dependent ter

97 showed previously that the WW domain of the prolyl isomerase, Ess1, can bind the phosphorylated carb

98 The yeast prolyl isomerase, Ess1, has recently been shown to inter

99 the protein-disulfide isomerase and peptidyl-prolyl isomerase families.

100 Rapamycin binds to the peptidyl-prolyl isomerase FKBP12 and forms protein-drug complexes

101 The peptidyl-prolyl isomerase FKBP12 was originally identified as the

102 In complex with the prolyl isomerase FKBP12, the natural product rapamycin b

103 ta327 mutation is suppressed by deleting the prolyl isomerase Fpr3, which is not MAT regulated.

104 Here we report that the Ess1 peptidyl prolyl isomerase functionally interacts with the transcr

105 Pin1, a major peptidyl-prolyl isomerase, has recently been associated with cert

106 Three families of prolyl isomerases have been identified: cyclophilins, FK

107 Although peptidyl-prolyl isomerases have been implicated in catalyzing pro

108 hilins, which are a large family of cellular prolyl isomerases, have been found to inhibit Tomato bus

109 ulated by the cyclophilin family of peptidyl-prolyl isomerases, highlighting the potential for regula

110 , while surA encodes a periplasmic cis-trans prolyl isomerase important in the biogenesis of outer me

111 The Ess1 prolyl isomerase in Saccharomyces cerevisiae regulates R

112 zymes such as Cyp-40, and implicate peptidyl-prolyl isomerases in the regulation of transcription, tr

113 st protein cyclophilin A (CypA), a cis-trans prolyl isomerase, in some way seems to assist in this as

114 hich are members of the large family of host prolyl isomerases, in TBSV replication.

115 slower phase of P117G SNase are catalyzed by prolyl isomerase, indicating that proline isomerization

116 in A and incorporates this cellular peptidyl prolyl-isomerase into virions.

117 Ess1/Pin1 is a peptidyl prolyl isomerase involved in both mitotic regulation and

118 These data indicate that a prolyl isomerase is required for specifying the "CTD cod

119 deficiency, the activity of Pin1, a peptidyl-prolyl isomerase, is reduced (see the related article be

120 FKBP12, a cis-trans peptidyl-prolyl isomerase, is required for the normal gating of t

121 We also find that Pin1, a prolyl-isomerase, is capable of binding Pim-1 and leads

122 pif gene) is a mitochondrial matrix peptidyl-prolyl isomerase known to modulate opening of the mitoch

123 and cyclophilin D (the Ppif gene product), a prolyl isomerase located within the mitochondrial matrix

124 function and indicate that the inhibition of prolyl isomerases may be a novel therapeutic strategy in

125 Pin1 is a prolyl isomerase of the parvulin family and specifically

126 enzymes that catalyze proline isomerization (prolyl isomerases) often catalyze protein folding.

127 he rate constants and the effect of peptidyl-prolyl isomerase on the rate constants.

128 ichia coli, has sequence similarity with the prolyl isomerase parvulin.

129 We show that the prolyl isomerase (PI) FKBP12 binds to H-Ras in a palmito

130 The prolyl isomerase Pin1 and glycogen synthase kinase-3beta

131 iquitination and degradation mediated by the prolyl isomerase Pin1 and the ubiquitin ligase KLHL20.

132 WW domains of the essential mitotic prolyl isomerase Pin1 and the ubiquitin ligase Nedd4 bou

133 The prolyl isomerase Pin1 binds and isomerizes tau and has b

134 Since the prolyl isomerase Pin1 binds the c-Myc phosphodegron and

135 gard, it has been recently observed that the prolyl isomerase Pin1 can interact with proteins phospho

136 The prolyl isomerase Pin1 enhanced p53-dependent BAX activat

137 The peptidyl-prolyl isomerase Pin1 has been implicated in regulating

138 The prolyl isomerase Pin1 has been shown to be overexpressed

139 unctions of BRD4 are positively regulated by prolyl isomerase PIN1 in gastric cancer cells.

140 mics to identify a homologue of the peptidyl-prolyl isomerase PIN1 in T. annulata (TaPIN1) that is se

141 we investigated the globular folded peptidyl-prolyl isomerase Pin1 in Xenopus laevis oocytes and in n

142 Here we show that the peptidyl-prolyl isomerase Pin1 influences the phosphorylation sta

143 Peptidyl-prolyl isomerase Pin1 inhibits the dephosphorylation of

144 Here, we report that the prolyl isomerase Pin1 interacts with Ser65-phosphorylate

145 We show that the peptidyl-prolyl isomerase Pin1 interacts with SMRT both in vitro

146 We have previously shown that the peptidyl-prolyl isomerase Pin1 is able to affect cell proliferati

147 The peptidyl-prolyl isomerase Pin1 is frequently up-regulated in huma

148 We show here that prolyl isomerase Pin1 is over expressed in HTLV-1 cell l

149 athways and a unique therapeutic target, the prolyl isomerase Pin1 is overexpressed in a majority of

150 Previously we reported that the peptidyl prolyl isomerase Pin1 modulates RNAP II function during

151 Here, we show that the peptidyl-prolyl isomerase Pin1 modulates the production of many p

152 re we report that chemical inhibition of the prolyl isomerase Pin1 or downregulation of Pin1 by small

153 igration was suppressed by inhibitors of the prolyl isomerase Pin1 or extracellular signal-regulated

154 The prolyl isomerase Pin1 plays important roles in numerous

155 Here, we show that the prolyl isomerase Pin1 protein modulates A3G expression.

156 Here we show that the peptidyl-prolyl isomerase Pin1 provides a timer for the lifetime

157 The prolyl isomerase Pin1 regulates multiple signaling casca

158 phosphorylated proteins is regulated by the prolyl isomerase Pin1 through isomerization of phosphory

159 le in targeting the phosphorylation-specific prolyl isomerase Pin1 to its substrates.

160 The prolyl isomerase PIN1, a critical modifier of multiple s

161 exhibited increased binding of p66(Shc) with prolyl isomerase Pin1, a protein implicated in transloca

162 and stability of proteins is mediated by the prolyl isomerase Pin1, but the role of Pin1 in the heart

163 omotes the interaction between Nanog and the prolyl isomerase Pin1, leading to Nanog stabilization by

164 n by ERK, conformation of XPO5 is altered by prolyl isomerase Pin1, resulting in reduction of pre-miR

165 Overexpression of the prolyl isomerase Pin1, which binds to the hyperphosphory

166 -mediated up-regulation of the expression of prolyl isomerase PIN1, which in turn increases enzyme ac

167 Here, we identify prolyl isomerase Pin1, which is often overexpressed in b

168 Nuclear protein peptidyl-prolyl isomerase Pin1-mediated prolyl isomerization is a

169 pho-peptide substrate ligand to the peptidyl-prolyl isomerase Pin1.

170 in proteins is catalyzed specifically by the prolyl isomerase Pin1.

171 ns with the protein phosphatase PP2A and the prolyl isomerase Pin1.

172 lation, but is catalyzed specifically by the prolyl isomerase Pin1.

173 potential recognition sites for the peptidyl-prolyl isomerase Pin1.

174 /Thr-Pro motifs are further regulated by the prolyl isomerase Pin1.

175 conversion is catalyzed specifically by the prolyl isomerase Pin1.

176 n is catalyzed specifically by the essential prolyl isomerase Pin1.

177 lated Ser/Thr-Pro motifs is regulated by the prolyl isomerase Pin1.

178 n is catalyzed specifically by the essential prolyl isomerase Pin1.

179 ates a binding site for the WW domain of the prolyl isomerase Pin1.

180 sor function are negatively regulated by the prolyl isomerase Pin1.

181 facilitated new interaction of Bax with the prolyl isomerase Pin1.

182 monstrate that the phosphorylation-dependent prolyl-isomerase Pin1 interacts with ADAR2 and is a posi

183 The phospho-Ser/Thr-directed prolyl-isomerase Pin1 was originally identified in verte

184 tively regulated by the interaction with the prolyl-isomerase Pin1, via proteasome-mediated degradati

185 that Notch3 is a novel target protein of the prolyl-isomerase Pin1, which is able to regulate Notch3

186 The prolyl isomerase, Pin1, has been found to bind directly

187 The cis/trans peptidyl-prolyl isomerase, Pin1, is a regulator of mitosis that i

188 We show that a peptidyl-prolyl isomerase, Pin1, is involved in the regulation of

189 118-ERalpha) is a substrate for the peptidyl prolyl isomerase, Pin1, which mediates cis-trans isomeri

190 We also show that a peptidyl-prolyl isomerase PINN-1 antagonizes SYDN-1 in the spatio

191 We report that the peptidyl-prolyl isomerase (PPI) cyclophilin A (CypA), which is im

192 oliferation and due to its specific peptidyl-prolyl-isomerase (PPI) function, the FKBP protein family

193 Here, we postulated that peptidyl prolyl isomerase (PPIase) activity of FKBP65 positively

194 Cyclophilin A (CyPA) and its peptidyl-prolyl isomerase (PPIase) activity play an essential rol

195 FKBPs), are protein chaperones with peptidyl-prolyl isomerase (PPIase) activity.

196 inct functional roles for the PrsA2 peptidyl-prolyl isomerase (PPIase) and the N- and C-terminal doma

197 The peptidyl-prolyl isomerase (PPIase) cyclophilin A (Cpr1p) is conse

198 ecognition is imparted by the first peptidyl-prolyl isomerase (PPIase) domain of SurA.

199 ophilins harbors the characteristic peptidyl-prolyl isomerase (PPIase) domain, whereas three copies o

200 three compounds inhibited the Pin1 peptidyl-prolyl isomerase (PPIase) enzymatic activity.

201 that small molecule ligands for the peptidyl-prolyl isomerase (PPIase) FKBP12 possess powerful neurop

202 The Ess1/Pin1 peptidyl-prolyl isomerase (PPIase) is thought to control mitosis

203 Human peptidyl-prolyl isomerase (PPIase) Pin1 plays key roles in develo

204 of TGF-beta1 and show here that the peptidyl-prolyl isomerase (PPIase) Pin1 promoted the stability of

205 The Escherichia coli periplasmic peptidyl-prolyl isomerase (PPIase) SurA is involved in the matura

206 Cyclophilin A (CypA/Ppia) is a peptidyl-prolyl isomerase (PPIase) that binds the immunosuppressi

207 Pin1 is a novel essential peptidyl-prolyl isomerase (PPIase) that inhibits entry into mitos

208 an essential and conserved mitotic peptidyl-prolyl isomerase (PPIase) that is distinct from members

209 utation in a novel highly conserved peptidyl prolyl isomerase (PPIase) that selectively eliminates Rb

210 of TTS-ExoS, cyclophilin A (CpA), a peptidyl-prolyl isomerase (PPIase).

211 small-molecule ligands for the peptidyl and prolyl isomerases (PPIase) of FKBP12 have been shown to

212 Peptidyl-prolyl isomerases (PPIases) are emerging as key regulato

213 Peptidyl-prolyl isomerases (PPIases) are ubiquitous cellular enzy

214 (FKBP) subfamily that functions as peptidyl-prolyl isomerases (PPIases) in protein folding.

215 06-binding protein (FKBP) family of peptidyl-prolyl isomerases (PPIases) is characterized by a common

216 residues is regulated by cis/trans peptidyl-prolyl isomerases (PPIases).

217 Prolyl-isomerases (PPIases) are found in all organisms a

218 rent families of enzymes, known as "peptidyl-prolyl isomerases" (PPIases), catalyze this reaction, wh

219 ber of the FKBP family of cis-trans peptidyl-prolyl isomerases (PPlases).

220 CypA (Cyclophilin A) is a peptidyl-prolyl isomerase previously shown to be required for cho

221 he genes encoding SpeB (speB) and a peptidyl-prolyl isomerase (prsA) constitute an operon with transc

222 fectants suggest the involvement of peptidyl-prolyl isomerase, Raf kinase inhibitor and 80 kDa protei

223 The Pin1 prolyl isomerase regulates phosphorylation signaling by

224 SurA is a periplasmic peptidyl-prolyl isomerase required for the efficient folding of e

225 Here, we report that cyclophilin B (CypB), a prolyl isomerase residing in the endoplasmic reticulum (

226 We show that cyclophilin, a peptidyl-prolyl isomerase secreted from T. cruzi epimastigotes, b

227 Pin1, a prolyl isomerase, selectively binds to phosphorylated pr

228 on of ribonuclease T1 in the presence of the prolyl isomerase SlyD from Escherichia coli to examine h

229 cal/mol, and are accelerated by the peptidyl-prolyl isomerase SlyD.

230 of cyclophilin A (CypA), a cellular peptidyl-prolyl isomerase that binds specifically to CA, was decr

231 Ess1 is an essential prolyl isomerase that binds the C-terminal domain (CTD)

232 FKBP12, a cis-trans prolyl isomerase that binds the immunosuppressants FK506

233 Cyclophilin A (CypA) is a peptidyl-prolyl isomerase that binds to the capsid protein (CA) o

234 s, rapamycin forms complexes with the FKBP12 prolyl isomerase that block cell cycle progression by in

235 PIN1 is a peptidyl-prolyl isomerase that catalyzes the cis/trans isomerizat

236 Pin1 is a prolyl isomerase that regulates cell signaling uniquely

237 Pin1 is a phospho-specific prolyl isomerase that regulates numerous key signaling m

238 D (CypD) is a mitochondrial matrix peptidyl-prolyl isomerase that regulates the MPTP and is a drug t

239 Cyclophilins are cis-trans-peptidyl-prolyl isomerases that bind to and are inhibited by the

240 o a large family of enzymes called "peptidyl prolyl isomerases" that assist protein folding and assem

241 utions of the cyclophilin subset of peptidyl-prolyl isomerases to protein folding and identified cycl

242 of immunophilins, which function as peptidyl-prolyl isomerases, to regulate Crk proteins in human T l

243 an inhibitor of the FKBP family of peptidyl prolyl isomerases, was shown to increase survival in ani

244 e formation of disulfide bonds; and peptidyl-prolyl isomerase-were immobilized on an agarose gel.

245 ude protein disulfide isomerase and peptidyl prolyl isomerase, which catalyze the rearrangement of di

246 feedback sites or overexpression of the Pin1 prolyl-isomerase, which facilitates B-Raf dephosphorylat