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1                                              Peptidylprolyl isomerase 1 (Pin1), a protein overexpress
2                            Here, we identify peptidylprolyl isomerase A (PPIA) is required for NRF2 p
3 ing cyclophilin A (CYPA, also known as PPIA, peptidylprolyl isomerase A) to the so-called CYPA-bindin
4 osphate dehydrogenase, alpha-enolase, actin, peptidylprolyl isomerase A, phosphatidylethanolamine-bin
5                     Catalysis is achieved by peptidylprolyl isomerases, a superfamily of molecular ch
6 ed FK506-binding immunophilin that possesses peptidylprolyl isomerase activity and a tetratricopeptid
7 t to cyclophilins is distinct from cis-trans-peptidylprolyl isomerase activity and is similar to that
8 compounds are shown to disrupt the cis-trans peptidylprolyl isomerase activity of FKBP12 with inhibit
9    Immunophilins are protein chaperones with peptidylprolyl isomerase activity that belong to one of
10 a wide range of tissues, and the protein has peptidylprolyl isomerase activity that is inhibited by F
11 atter effect being strongly dependent on the peptidylprolyl-isomerase activity and also on the TPR do
12 bitory action of FKBP51 requires neither the peptidylprolyl-isomerase activity of the immunophilin no
13 e and function are regulated by the cellular peptidylprolyl isomerase cyclophilin A (CyPA).
14                                          The peptidylprolyl isomerase, cyclophilin D (CypD, PPIF), is
15                                              Peptidylprolyl isomerase cyclophilins play critical role
16                                  Because the peptidylprolyl isomerase CYPA also interacts with HIV-1
17 57BL/6J mice (control) and mice deficient in peptidylprolyl isomerase D (cyclophilin D, encoded by Pp
18 sion of QTL-linked genes, we nominated Ppid (peptidylprolyl isomerase D, a member of the tetratricope
19 22% identity with the central portion of the peptidylprolyl isomerase domain of human FKBP52.
20 E. coli SurA comprises a core domain and two peptidylprolyl isomerase domains (P1 and P2), but its me
21                    Cyclophilin D (CypD), the peptidylprolyl isomerase F (PPIase), is a key component
22 ild-type mice and knockout mice deficient in peptidylprolyl isomerase F (Ppif) or deficient in both P
23 atly reduced in cyclophilin D null [Ppif-/- (peptidylprolyl isomerase F)] mice.
24                     FKBP8 is a member of the peptidylprolyl isomerase family that mediates the cis/tr
25                                          The peptidylprolyl isomerase FKBP12 interacts with FK506 for
26  the immunophilin-related co-chaperones: the peptidylprolyl isomerases FKBP51, FKBP52 or CyP40, or th
27 ion level or alteration of its activity by a peptidylprolyl isomerase inhibitor alter CFTR stability
28                                              Peptidylprolyl isomerase Pin1 regulates the function and
29  inhibitors of the phosphorylation-dependent peptidylprolyl isomerase Pin1, an essential regulator of
30 e characterized the backbone dynamics of the peptidylprolyl isomerase (Pin1) catalytic domain in the
31                                 By using the peptidylprolyl isomerase, Pin1, as a probe for proline-d
32  high molecular mass immunophilin possessing peptidylprolyl isomerase (PPIase) activity that is inhib
33 oth prokaryotes and eukaryotes, that exhibit peptidylprolyl isomerase (PPIase) activity.
34 teract either directly or indirectly via its peptidylprolyl isomerase (PPIase) domain with cytoplasmi
35  through the association of the immunophilin peptidylprolyl isomerase (PPIase) domain with dynamitin,
36 -binding immunophilins possess the signature peptidylprolyl isomerase (PPIase) domain, but no role fo
37  expressed fragment of FKBP52 comprising its peptidylprolyl isomerase (PPIase) domain.
38 herichia coli SurA has a core domain and two peptidylprolyl isomerase (PPIase) domains, the role(s) o
39   Escherichia coli SlyD protein, a cis-trans peptidylprolyl isomerase (PPIase), copurifies with AC7 C
40                                              Peptidylprolyl isomerases (PPIases) catalyze cis/trans i
41                        Current inhibitors of peptidylprolyl isomerases show no selectivity between th
42  associate with Pin1, a WW domain-containing peptidylprolyl isomerase that does not detectably bind t
43 romotes the association of Dab2 with Pin1, a peptidylprolyl isomerase that regulates the rate of Dab2