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

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

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

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

10 D (Cyp-D) is a mitochondrial matrix peptidyl-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 pregulation of other chaperones and peptidyl-prolyl isomerases.

16 gnaling since cyclophilins are also peptidyl-prolyl isomerases.

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

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

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

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

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

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

23 of prolyl residues, a reaction catalyzed by 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 In turn, genetic knockout (KO) of FKBP prolyl isomerase 1A (FKBP1A), which encodes a protein ta

27 Da FK506-binding protein (also known as FKBP prolyl isomerase 1A), regulates the neuronal resilience

28 We have identified peptidyl-prolyl isomerase A (PPIA or cyclophilin A) as a dominant

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

30 iquitous peptidyl prolyl isomerase, peptidyl prolyl isomerase A (PPIA), concentrates inside liquid-li

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

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

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

34 The compounds inhibited peptidyl-prolyl isomerase activity (half maximal inhibitory conce

35 the folding of type III collagen through its prolyl isomerase activity and acted as a molecular chape

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

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

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

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

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

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

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

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

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

45 Prolyl isomerase activity is not required for forming th

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

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

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

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

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

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

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

53 2A show reciprocal genetic interactions, and prolyl isomerase activity of Pin1 is essential for cell

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

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

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

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

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

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

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

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

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

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

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

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

66 live in extreme polar environments: the Ess1 prolyl isomerase and its target, the carboxy-terminal do

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

82 h sequence, whose interaction with the human prolyl isomerase cyclophilin A (CypA) is essential for v

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

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

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

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

87 strating interconversion acceleration by the prolyl isomerase Cyclophilin A.

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

89 he interaction between ANT3 and the peptidyl-prolyl isomerase cyclophilin D (CypD), mortalin decrease

90 tic depletion of the mitochondrial cis-trans prolyl isomerase cyclophilin D as in wild-type cells, in

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

92 ls that silencing the mitochondrial peptidyl prolyl isomerase cyclophilin-D (Cyp-D) reduces Vo(2).

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

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

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

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

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

98 s-induced cytosolic chaperone PPID (peptidyl-prolyl isomerase D/cyclophilin 40/Cyp40) drives OMM inse

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

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

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

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

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

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

105 506-binding protein with an inactive peptide prolyl-isomerase domain that binds DOUBLETIME and tetrat

106 mains, an E3 ligase domain, and a C-terminal prolyl-isomerase domain.

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

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

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

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

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

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

113 bitors synergized with inhibitors of PIN1, a prolyl isomerase essential for IRAK1 activation in respo

114 Cyclophilin D (CypD) is a peptidyl-prolyl isomerase expressed in the nucleus and transporte

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

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

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

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

119 haracterize SP3N, a specific degrader of the prolyl isomerase FKBP12.

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

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

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

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

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

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

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

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

128 The Ess1 prolyl isomerase in Saccharomyces cerevisiae regulates R

129 duced a deregulation of periplasmic peptidyl-prolyl isomerases in gram-negative bacteria.

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

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

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

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

134 ancement in binding affinity (>40 fold), and prolyl isomerase inhibition (PPIase) activity (>200 fold

135 The peptidyl-prolyl isomerase inhibitor Cyclosporine A (CsA) selectiv

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

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

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

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

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

141 ion, the cis/trans equilibrium, catalyzed by prolyl isomerases, is shifted towards trans, while stead

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

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

144 encoding the spliceosome components Peptidyl-Prolyl Isomerase Like-1 (PPIL1) or Pre-RNA Processing-17

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

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

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

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

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

150 little is known about the impact of peptidyl prolyl isomerases on the LLPS of IDPs, which often conta

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

152 emonstrate that the most ubiquitous peptidyl prolyl isomerase, peptidyl prolyl isomerase A (PPIA), co

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

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

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

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

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

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

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

160 The prolyl isomerase Pin1 catalyzes the cis-trans isomerizat

161 The prolyl isomerase Pin1 enhanced p53-dependent BAX activat

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

163 The prolyl isomerase Pin1 has been shown to be overexpressed

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

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

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

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

168 Peptidyl-prolyl isomerase Pin1 inhibits the dephosphorylation of

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

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

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

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

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

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

175 The prolyl isomerase PIN1 is overexpressed in cancer and con

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

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

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

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

180 The prolyl isomerase Pin1 plays important roles in numerous

181 ic LIC1-CTD phosphorylation also engages the prolyl isomerase Pin1 predominantly to Hook2-dynein-Nde1

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

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

184 The prolyl isomerase Pin1 regulates multiple signaling casca

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

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

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

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

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

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

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

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

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

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

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

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

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

198 nge mediated by the phosphorylation-directed prolyl isomerase PIN1.

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

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

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

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

203 conversion is catalyzed specifically by the prolyl isomerase Pin1.

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

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

206 issue via analysis of fission yeast peptidyl-prolyl isomerase Pin1.

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

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

209 tion pathway that is potentiated by peptidyl-prolyl isomerase Pin1.

210 CDK1/2 induces interaction with the peptidyl-prolyl isomerase PIN1.

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

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

213 to DNA double-strand breaks is regulated by prolyl isomerase Pin1.

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

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

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

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

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

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

220 The peptidyl-prolyl isomerase, Pin1, is exploited in cancer to activa

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

222 118-ERalpha) is a substrate for the peptidyl prolyl isomerase, Pin1, which mediates cis-trans isomeri

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

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

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

226 ition of MLK3 down-regulates expression of a prolyl-isomerase, Ppia, which is directly phosphorylated

227 e repeat (TPR) domain and catalyzes peptidyl-prolyl isomerase (PPIase) activity during folding of kin

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

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

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

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

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

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

234 (WW) domain flexibly tethered to a peptidyl-prolyl isomerase (PPIase) domain, resulting in interdoma

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

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

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

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

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

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

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

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

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

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

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

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

247 nding and inactivating an essential peptidyl-prolyl isomerase (PPIase).

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

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

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

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

252 06-binding protein (FKBP) family of peptidyl-prolyl isomerases (PPIases) is characterized by a common

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

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

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

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

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

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

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

260 The Pin1 prolyl isomerase regulates phosphorylation signaling by

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

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

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

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

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

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

267 cored by the ubiquitous presence of peptidyl prolyl isomerases such as cyclophilins that accelerate t

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

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

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

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

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

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

274 covalent agents targeting Pin1, a cis-trans prolyl isomerase that plays a crucial role in tumorigene

275 Pin1 is a prolyl isomerase that regulates cell signaling uniquely

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

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

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

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

280 ollagen a trimerization domain and cis-trans prolyl isomerases to facilitate and accelerate triple he

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

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

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

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

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

286 t class of molecular chaperones are peptidyl prolyl isomerases, which enhance the cis/trans-isomeriza

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