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

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

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

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

6 the CTD induced by the Ess1 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 Cyclophilin A, also known as peptidylprolyl cis-/trans-isomerase A (PPIA), as a foldase is beneficia

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

47 ',2'-hydratase (crtC/CT0301), and carotenoid cis-trans isomerase (crtH/CT0649).

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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

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