ライフサイエンスコーパス: cis-trans isomerase

1 A5), HSPA8, HSPD1, and PPIA (peptidyl-propyl cis-trans isomerase).

2 es a presumptive periplasmic peptidyl-prolyl cis-trans isomerase.

3 as a result of a mutation in the carotenoid cis-trans isomerase.

4 the CTD induced by the Ess1 peptidyl-prolyl cis/trans isomerase.

5 tA), the latter coding for a peptidyl-prolyl cis/trans isomerase.

6 hich specifies a periplasmic peptidyl-prolyl cis/trans isomerase.

7 This step is catalyzed by peptidyl-prolyl cis-trans isomerases.

8 me, eIF4E/m(7)GTP, and human peptidyl-prolyl cis-trans isomerase 1 (Pin1) in complex with the peptide

9 on proteins of Tau and Pin1 (peptidyl-prolyl cis-trans-isomerase 1) carrying complementary fragments

10 BISPHOSPHATASE (SBPase), the PEPTIDYL-PROLYL CIS-TRANS ISOMERASE 20-3 (CYP20-3), and ENOLASE2 (ENO2).

11 Cyclophilin A, also known as peptidylprolyl cis-/trans-isomerase A (PPIA), as a foldase is beneficia

12 cyclophilin A, also known as peptidylprolyl cis-/trans-isomerase A (PPIA), is a mediator of the neur

13 two peptides encoded by the peptidyl-prolyl cis-trans isomerase A (PPIA) gene whose abundance was in

14 Cyclophilin A, also known as peptidyl-prolyl cis-trans isomerase A (PPIA), is a foldase and molecular

15 ta-2-Microglobulin (B2M) and Peptidyl-Prolyl cis-trans Isomerase A (PPIA), respectively.

16 n esterase, a transposase, a peptidyl-prolyl cis-trans isomerase, a subtilisin inhibitor-like protein

17 In contrast, the peptidylprolyl cis/trans isomerase active site is utilized to promote C

18 hilin B in the complex shows peptidyl-prolyl cis-trans isomerase activity and that the P3H1.CRTAP.Cyp

19 e first time a direct role of peptidylprolyl cis-trans isomerase activity has been implicated in the

20 The peptidyl-prolyl cis-trans isomerase activity of cyclophilin B was shown

21 ecretory pathway and suggest that the prolyl cis-trans isomerase activity of FKBP65 may be important

22 The peptidylprolyl cis-trans isomerase activity of the mutant CypB is norma

23 pB) is a 21-kDa protein with peptidyl-prolyl cis-trans isomerase activity that functions as a transcr

24 a) cell membranes, has robust peptidylprolyl cis-trans isomerase activity that is strongly inhibited

25 lass of immunophilins with a peptidyl-prolyl cis-trans isomerase activity.

26 losporin A (CsA) and possess peptidyl-prolyl cis-trans isomerase activity.

27 families of enzymes sharing peptidyl-prolyl cis-trans isomerase activity.

28 nally normal as judged by its peptidylprolyl cis-trans-isomerase activity and its inhibition by cyclo

29 The peptidylprolyl cis-trans-isomerase activity of FKBP65 was previously sh

30 ally designed to abolish the peptidyl-prolyl cis-trans-isomerase activity of the protein failed to in

31 yclosporin A (CsA)-sensitive, peptidylprolyl cis-trans-isomerase activity that is characteristic of n

32 that CYP38 does not possess peptidyl-prolyl cis/trans isomerase activity and identifies a possible i

33 ophilin A and influences its peptidyl-prolyl cis/trans isomerase activity on residue Pro(314) of NS5A

34 (HIV-1 CA-NTD), and retains peptidyl prolyl cis/trans isomerase activity.

35 ins, which are proteins with peptidyl-prolyl cis/trans isomerase activity.

36 KBP12 (FK506 binding protein 12) is a prolyl cis-trans isomerase and a drug target.

37 lar cyclophilins function as peptidyl-prolyl cis-trans isomerases and are targets of the immunosuppre

38 d intracellular protein, is a peptidylprolyl cis-trans-isomerase and the major target of the potent i

39 een identified as a secreted peptidyl-prolyl cis/trans isomerase and chaperone that is dispensable fo

40 conserved mechanism of dual functionality in cis/trans isomerases and define its molecular determinan

41 sights into the mechanism of peptidyl-prolyl cis/trans isomerases and the general interplay between e

42 as a prolyl 3-hydroxylase, a peptidyl prolyl cis-trans isomerase, and a molecular chaperone.

43 n-disulfide isomerase (PDI), peptidyl-prolyl cis-trans isomerase, and immunoglobulin-binding protein

44 Peptidyl-prolyl cis-trans isomerases are a group of cytosolic enzymes in

45 We now identify Pin1, a cis-trans isomerase, as an essential component of the ri

46 e secreted antigen A and the peptidyl-prolyl cis-trans isomerase, as well as the Enterococcus faecali

47 proteoglycan 1 (LEPRE1) and peptidyl prolyl cis-trans isomerase B (PPIB) genes result in phenotypes

48 ects in the Escherichia coli peptidyl-prolyl cis/trans-isomerase B following mutation of two phenylal

49 two distinct types (racemases/epimerases and cis-trans isomerases), but reactions entailing structura

50 heir access to inward-facing peptidyl-prolyl cis/trans isomerase catalytic sites and ipsilateral chap

51 pite the fact that CypA is a peptidyl-prolyl cis/trans isomerase, catalytic activity on CA(N) has not

52 Pin1 is a peptide prolyl cis/trans isomerase conserved among eukaryotes that spec

53 desaturases (CrtP and CrtQ) and a plant-like cis-trans isomerase (CrtH) and thus differs from the pat

54 ',2'-hydratase (crtC/CT0301), and carotenoid cis-trans isomerase (crtH/CT0649).

55 Pseudomonas spp. possess a cis-trans isomerase (Cti) an enzyme that converts the ci

56 The dynamics of the prolyl cis-trans isomerase cyclophilin A (CypA) in its substrat

57 1) incorporates the cellular peptidyl-prolyl cis-trans isomerase cyclophilin A (CyPA), the cytosolic

58 Peptidyl prolyl cis/trans isomerase cyclophilin A (CypA) serves as a cel

59 Peptidyl prolyl cis-trans isomerase (cyclophilin), which has been shown

60 tion to the cyclophilin-like peptidyl-prolyl cis-trans isomerase domain, the latter contain a variety

61 an FKBP (FK506 binding protein)-like prolyl-cis/trans-isomerase domain, making them attractive targe

62 ene, tentatively named PPIE (peptidyl-prolyl cis-trans isomerase E), has 83% amino acid identity with

63 ne of at least two predicted peptidyl-prolyl cis/trans-isomerases encoded by L. monocytogenes; these

64 Finally, two immunophilins, peptidyl-prolyl cis-trans isomerase F and FKBP52, the latter of which pl

65 in Methanococcus jannaschii peptidyl-prolyl cis/trans isomerase FKBP26.

66 s in FKBP10, which encodes the 65 kDa prolyl cis-trans isomerase, FKBP65, in 38 members of 21 familie

67 lpha-helical linker of the bacterial proline cis/trans isomerase FkpA and the periplasmic oxidase Dsb

68 alysis identified p74 as the peptidyl-prolyl cis-trans isomerase, FKPB65.

69 of the cyclophilin family of peptidyl-prolyl cis-trans isomerases has been isolated from the human pa

70 CYPB, a prolyl cis-trans isomerase, has been thought to drive the proly

71 secreted protein (HP1286); putative peptidyl cis-trans isomerase (HP0175); six proteins encoded by HP

72 , a phosphorylation-specific peptidyl-prolyl cis-trans isomerase implicated in several cancers.

73 There are seven peptidyl-prolyl cis-trans isomerases in the rER, and so far, two of thes

74 Ess1 is an essential peptidylprolyl-cis/trans-isomerase in the yeast Saccharomyces cerevisia

75 a FK506 binding protein-type peptidyl-prolyl cis-trans isomerase, is not fully understood.

76 t prsA2, an extracytoplasmic peptidyl-prolyl cis/trans isomerase, is critical for virulence and contr

77 Yeast ESS1, a peptidyl-prolyl cis/trans isomerase, is involved in RNA processing and c

78 mutations in PPIL4, encoding peptidyl-prolyl cis-trans isomerase-like 4, in both familial and index I

79 These findings suggest that prolyl cis-trans isomerase may be required to effectively fold

80 udies have shown that Pin1, a peptidylprolyl cis/trans-isomerase, may be actively involved in the reg

81 al reaction centre for aldoxime dehydratase, cis-trans isomerase, N-N bond formation, hydrazine forma

82 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1) has been f

83 is coupled with binding of a peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1) to p53-RS,

84 ing the protein stability of peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), a key dri

85 lane/sulfolene inhibitors of peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), a phospho

86 S-transferase Pi (GSTP1) and peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), emerging

87 s MATalpha1 interaction with peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1), which blo

88 Peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (PIN1)-catalyzed

89 Here, we describe a peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 (Pin1)-dependent

90 rly protein 6 (HPV16 E6) and peptidyl-prolyl cis-trans isomerase NIMA-interacting 1 protein (Pin1).

91 Peptidyl-prolyl cis/trans isomerase NIMA-interacting 1 (Pin1) promotes b

92 GldI is similar to peptidyl-prolyl cis/trans-isomerases of the FK506-binding protein family

93 ut competitive inhibitors of peptidyl-prolyl cis-trans isomerases or that dipeptides are subject to d

94 ently we have shown that the peptidyl-prolyl cis/trans isomerase parvulin 17 (Par17) interacts with t

95 difications catalyzed by the peptidyl-prolyl cis-/trans isomerase Pin1.

96 nal changes catalyzed by the peptidyl-prolyl cis-/trans isomerase Pin1.

97 Here we identify the peptidyl-prolyl cis-trans isomerase Pin1 as an important factor mediatin

98 Here we reveal the role of prolyl cis-trans isomerase Pin1 in activating LSF, by facilitat

99 The human rotamase or peptidyl-prolyl cis-trans isomerase Pin1 is a conserved mitotic regulato

100 through interaction with the peptidyl-prolyl cis-trans isomerase Pin1.

101 tability is regulated by the peptidyl-prolyl cis/trans isomerase Pin1 and highlight the importance of

102 ssion levels of an oncogenic peptidyl-prolyl cis/trans isomerase Pin1 and levels of Akt phosphorylati

103 ex containing cyclin E, Cdk2, and the prolyl cis/trans isomerase Pin1 and promotes the activity of Pi

104 the phosphorylation-specific peptidyl-prolyl cis/trans isomerase Pin1.

105 esults in recruitment of the peptidyl prolyl cis/trans isomerase Pin1.

106 yrosine phosphatase 1B and a peptidyl-prolyl cis-trans isomerase (Pin1) isomerase resulted in potent,

107 iously demonstrated that the peptidyl-prolyl cis-trans isomerase, Pin1, binds and targets PML for deg

108 A peptidyl-prolyl cis/trans isomerase, Pin1 is involved in many cellular e

109 which is a substrate for the peptidylprolyl cis/trans isomerase, Pin1, as well as the ERK1/2 kinases

110 enzymological studies, FKBP38 peptidylprolyl cis/trans isomerase plays an important role in membrane

111 adhesins (VompA and VompB), peptidyl-prolyl cis-trans-isomerase (PpI), and hemin-binding protein E (

112 The chaperone has a peptidyl-prolyl cis-trans isomerase (PPIase) activity that catalyzes the

113 ose members typically exhibit peptidylprolyl cis-trans isomerase (PPIase) activity which is inhibitab

114 sis of CyPD that compromises peptidyl-prolyl cis-trans isomerase (PPIase) activity, we demonstrate th

115 splayed monomeric functional peptidyl-prolyl cis-trans isomerase (PPIase) activity.

116 known as immunophilins, with peptidylprolyl cis-trans isomerase (PPIase) activity.

117 nvolved in Hsp90 binding and peptidyl-prolyl cis-trans isomerase (PPIase) activity.

118 llular proteins that share a peptidyl prolyl cis-trans isomerase (PPIase) activity.

119 etween CypB (which possesses peptidyl-prolyl cis-trans isomerase (PPIase) and chaperone functions) an

120 Cyclophilin A is a conserved peptidyl-prolyl cis-trans isomerase (PPIase) best known as the cellular

121 n this study, we demonstrate that the prolyl cis-trans isomerase (PPIase) cyclophilin A (CypA) is hij

122 tratricopeptide domain and a peptidyl-prolyl cis-trans isomerase (PPIase) domain, prevents tau cleara

123 unophilins, a superfamily of peptidyl-prolyl cis-trans isomerase (PPIase) enzymes have been shown to

124 ein which is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family.

125 lysyl hydroxylase (LH) 2 or peptidyl-prolyl cis-trans isomerase (PPIase) FKBP65.

126 ssembly were inhibited by the peptidylprolyl cis-trans isomerase (PPIase) inhibitors cyclosporin A (C

127 Peptidyl prolyl cis-trans isomerase (PPIase) interacting with NIMA-1 (Pi

128 ranslocation chaperone and a peptidyl prolyl cis-trans isomerase (PPIase) that contributes to the vir

129 BP42/Twisted Dwarf1 (TWD1), a peptidylprolyl cis-trans isomerase (PPIase), but all attempts to demons

130 demonstrate that a cellular peptidyl-prolyl cis-trans isomerase (PPIase), cyclophilin B (CyPB), is c

131 ome-associated chaperone and peptidyl-prolyl cis-trans isomerase (PPIase), is essential for the secre

132 lyD gene encodes a FKBP-type peptidyl-prolyl cis-trans isomerase (PPIase).

133 r 1 was utilized to confirm peptidyl-prolyl cis-trans-isomerase (PPIase) activity by a PPIase assay

134 or optimal infection and has peptidylproline cis-trans-isomerase (PPIase) activity.

135 ence homology, but both have peptidyl prolyl cis/trans isomerase (PPIase) activity that is involved i

136 olding catalysts and possess peptidyl-prolyl cis/trans isomerase (PPIase) activity.

137 Ess1 is a peptidyl-prolyl cis/trans isomerase (PPIase) that binds to the carboxy-t

138 be the human protein Pin1, a peptidyl-prolyl cis/trans isomerase (PPIase) that interacts with NIMA.

139 n immunophilin that possesses peptidylprolyl cis/trans-isomerase (PPIase) activity and is a component

140 binding proteins (FKBPs) are peptidyl-prolyl cis/trans isomerases PPIases) that bind the immunosuppre

141 Peptidyl prolyl cis-trans isomerases (PPIases) are ubiquitous enzymes in

142 Peptidyl-prolyl cis/trans isomerases (PPIases) play a pivotal role in ca

143 ccordingly, the rER-resident peptidyl prolyl cis/trans isomerases (PPIases) play an important role in

144 on by controlling binding to peptidyl-prolyl cis/trans isomerases (PPIases).

145 ng protein H16_B0227 and the peptidyl-prolyl cis-trans isomerase PpiB, strongly repress gene expressi

146 riplasmic cyclophilin B-type peptidyl prolyl cis-trans isomerase (PpiB).

147 erate dehydrogenase (PGHDH), peptidyl-prolyl cis-trans isomerase (PPIF), solute carrier 15 (SLC15), s

148 Pin1, a peptidyl-prolyl cis/trans isomerase, recognizes phosphorylated serine/th

149 signaling activates Pin1, a peptidyl-prolyl cis-trans isomerase that binds to Bax and prevents its a

150 cyclophilin 33 (Cyp33) is a peptidyl-prolyl cis-trans isomerase that catalyzes cis-trans isomerizati

151 at CyPB is not the exclusive peptidyl-prolyl cis-trans isomerase that catalyzes the rate-limiting ste

152 philin D (PPIF or CypD) is a peptidyl-prolyl cis-trans isomerase that regulates mPTP opening in the i

153 tor is a ribosome-associated peptidyl-prolyl cis/trans isomerase that is highly conserved in most bac

154 Pin1 is a peptidyl-prolyl cis/trans isomerase that stabilizes beta-catenin by inhi

155 coli the ribosome-associated peptidyl-prolyl-cis-trans isomerase, trigger factor, plays a predominant

156 yclophilin A, a well-studied peptidyl-prolyl cis-trans isomerase, using normal and accelerated, atomi

157 and zeta-carotene desaturase [ZDS]), and two cis-trans isomerases (zeta-carotene isomerase [ZISO] and